<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE article PUBLIC "-//NLM//DTD Journal Publishing DTD v2.3 20070202//EN" "journalpublishing.dtd">
<article article-type="review-article" dtd-version="2.3" xml:lang="EN" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink">
<front>
<journal-meta>
<journal-id journal-id-type="publisher-id">Front. Cell Dev. Biol.</journal-id>
<journal-title>Frontiers in Cell and Developmental Biology</journal-title>
<abbrev-journal-title abbrev-type="pubmed">Front. Cell Dev. Biol.</abbrev-journal-title>
<issn pub-type="epub">2296-634X</issn>
<publisher>
<publisher-name>Frontiers Media S.A.</publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id pub-id-type="publisher-id">1386149</article-id>
<article-id pub-id-type="doi">10.3389/fcell.2024.1386149</article-id>
<article-categories>
<subj-group subj-group-type="heading">
<subject>Cell and Developmental Biology</subject>
<subj-group>
<subject>Review</subject>
</subj-group>
</subj-group>
</article-categories>
<title-group>
<article-title>Golgi defect as a major contributor to lysosomal dysfunction</article-title>
<alt-title alt-title-type="left-running-head">Akaaboune and Wang</alt-title>
<alt-title alt-title-type="right-running-head">
<ext-link ext-link-type="uri" xlink:href="https://doi.org/10.3389/fcell.2024.1386149">10.3389/fcell.2024.1386149</ext-link>
</alt-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname>Akaaboune</surname>
<given-names>Sarah R.</given-names>
</name>
<uri xlink:href="https://loop.frontiersin.org/people/2685328/overview"/>
<role content-type="https://credit.niso.org/contributor-roles/conceptualization/"/>
<role content-type="https://credit.niso.org/contributor-roles/data-curation/"/>
<role content-type="https://credit.niso.org/contributor-roles/writing-original-draft/"/>
<role content-type="https://credit.niso.org/contributor-roles/Writing - review &#x26; editing/"/>
<role content-type="https://credit.niso.org/contributor-roles/validation/"/>
</contrib>
<contrib contrib-type="author" corresp="yes">
<name>
<surname>Wang</surname>
<given-names>Yanzhuang</given-names>
</name>
<xref ref-type="corresp" rid="c001">&#x2a;</xref>
<uri xlink:href="https://loop.frontiersin.org/people/228474/overview"/>
<role content-type="https://credit.niso.org/contributor-roles/conceptualization/"/>
<role content-type="https://credit.niso.org/contributor-roles/data-curation/"/>
<role content-type="https://credit.niso.org/contributor-roles/writing-original-draft/"/>
<role content-type="https://credit.niso.org/contributor-roles/Writing - review &#x26; editing/"/>
<role content-type="https://credit.niso.org/contributor-roles/funding-acquisition/"/>
</contrib>
</contrib-group>
<aff>
<institution>Department of Molecular</institution>, <institution>Cellular and Developmental Biology</institution>, <institution>University of Michigan</institution>, <addr-line>Ann Arbor</addr-line>, <addr-line>MI</addr-line>, <country>United States</country>
</aff>
<author-notes>
<fn fn-type="edited-by">
<p>
<bold>Edited by:</bold> <ext-link ext-link-type="uri" xlink:href="https://loop.frontiersin.org/people/949309/overview">Zolt&#xe1;n Wiener</ext-link>, Semmelweis University, Hungary</p>
</fn>
<fn fn-type="edited-by">
<p>
<bold>Reviewed by:</bold> <ext-link ext-link-type="uri" xlink:href="https://loop.frontiersin.org/people/320165/overview">Yusong Guo</ext-link>, Hong Kong University of Science and Technology, Hong Kong SAR, China</p>
<p>
<ext-link ext-link-type="uri" xlink:href="https://loop.frontiersin.org/people/2659412/overview">Szabolcs Tak&#xe1;ts</ext-link>, E&#xf6;tv&#xf6;s Lor&#xe1;nd University, Hungary</p>
</fn>
<corresp id="c001">&#x2a;Correspondence: Yanzhuang Wang, <email>yzwang@umich.edu</email>
</corresp>
</author-notes>
<pub-date pub-type="epub">
<day>24</day>
<month>04</month>
<year>2024</year>
</pub-date>
<pub-date pub-type="collection">
<year>2024</year>
</pub-date>
<volume>12</volume>
<elocation-id>1386149</elocation-id>
<history>
<date date-type="received">
<day>14</day>
<month>02</month>
<year>2024</year>
</date>
<date date-type="accepted">
<day>03</day>
<month>04</month>
<year>2024</year>
</date>
</history>
<permissions>
<copyright-statement>Copyright &#xa9; 2024 Akaaboune and Wang.</copyright-statement>
<copyright-year>2024</copyright-year>
<copyright-holder>Akaaboune and Wang</copyright-holder>
<license xlink:href="http://creativecommons.org/licenses/by/4.0/">
<p>This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.</p>
</license>
</permissions>
<abstract>
<p>The Golgi apparatus plays a crucial role in lysosome biogenesis and the delivery of lysosomal enzymes, essential for maintaining cellular homeostasis and ensuring cell survival. Deficiencies in Golgi structure and function can profoundly impact lysosomal homeostasis, leading to various lysosomal storage diseases and neurodegenerative disorders. In this review, we highlight the role of the Golgi Reassembly Stacking Proteins (GRASPs) in the formation and function of the Golgi apparatus, emphasizing the current understanding of the association between the Golgi apparatus, lysosomes, and lysosomal storage diseases. Additionally, we discuss how Golgi dysfunction leads to the secretion of lysosomal enzymes. This review aims to serve as a concise resource, offering insights into Golgi structure, function, disease-related defects, and their consequential effects on lysosomal biogenesis and function. By highlighting Golgi defects as an underappreciated contributor to lysosomal dysfunction across various diseases, we aim to enhance comprehension of these intricate cellular processes.</p>
</abstract>
<kwd-group>
<kwd>HexA</kwd>
<kwd>Golgi</kwd>
<kwd>GRASP55</kwd>
<kwd>GRASP65</kwd>
<kwd>lysosome</kwd>
<kwd>lysosomal storage diseases</kwd>
<kwd>neurodegenerative diseases</kwd>
<kwd>secretion</kwd>
</kwd-group>
<custom-meta-wrap>
<custom-meta>
<meta-name>section-at-acceptance</meta-name>
<meta-value>Membrane Traffic</meta-value>
</custom-meta>
</custom-meta-wrap>
</article-meta>
</front>
<body>
<sec id="s1">
<title>1 Introduction</title>
<p>The Golgi apparatus, also known as the Golgi complex, was discovered by the Italian physician scientist Camillo Golgi in the late 19th century (<xref ref-type="bibr" rid="B138">Ludford, 1924</xref>; <xref ref-type="bibr" rid="B160">Palade and Claude, 1949</xref>). It forms a stack of flattened membranous sacs or cisternae, typically consisting of several cisternae, although the number can vary depending on the cell type and function (<xref ref-type="bibr" rid="B195">Shorter and Warren, 2002</xref>; <xref ref-type="bibr" rid="B240">Wang and Seemann, 2011</xref>). The Golgi stack comprises the <italic>cis</italic>-Golgi, the region closest to the endoplasmic reticulum (ER) and serves as the entry or receiving side of the Golgi apparatus; the <italic>medial</italic>-Golgi, structures located between the <italic>cis</italic>- and <italic>trans</italic>-Golgi that play a central role in modifying and processing proteins and lipids; and the <italic>trans</italic>-Golgi, the exit side of the Golgi where fully processed molecules are packaged into vesicles for delivery to various cellular destinations (<xref ref-type="bibr" rid="B86">Guo et al., 2014</xref>).</p>
<p>The importance of the Golgi in cellular function has been extensively studied (<xref ref-type="bibr" rid="B82">Goldfischer, 1982</xref>). The Golgi apparatus is responsible for various functions in eukaryotic cells, including protein and lipid processing, sorting, packaging, trafficking, and secretion (<xref ref-type="bibr" rid="B65">Farquhar and Palade, 1998</xref>). One primary function of the Golgi is post-translational modifications of proteins, such as glycosylation, phosphorylation, and proteolytic cleavage (<xref ref-type="bibr" rid="B94">Huang and Wang, 2017</xref>). These modifications are essential for their proper structure and physiological function (<xref ref-type="bibr" rid="B274">Zhang and Wang, 2016</xref>). It is also well documented that the Golgi apparatus is actively involved in lipid metabolism and synthesis of complex lipids such as glycolipids and sphingolipids (<xref ref-type="bibr" rid="B141">Maccioni et al., 2011</xref>; <xref ref-type="bibr" rid="B169">Quinville et al., 2021</xref>).</p>
<p>The Golgi also plays an important role in the delivery of lysosomal enzymes, formation of lysosomes, and maintenance of cellular homeostasis (<xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>). The sorting and packaging of post-translationally modified proteins and lipids involve the formation of various transport vesicles that bud from the <italic>trans</italic>-Golgi network (<xref ref-type="bibr" rid="B86">Guo et al., 2014</xref>). These vesicles, containing cargo molecules, are then directly delivered to their intended destinations in various intracellular organelles within the cell, such as endosomes and lysosomes, the plasma membrane, or the extracellular space (<xref ref-type="bibr" rid="B94">Huang and Wang, 2017</xref>). It is also well-established that the Golgi apparatus is indispensable for the secretion of essential molecules, including hormones, enzymes, and various proteins, through regulated and/or constitutive secretion mechanisms (<xref ref-type="bibr" rid="B96">Huttner et al., 1995</xref>). For instance, in neuronal cells, upon stimulation, vesicles containing proteins transiently stored within the cell fuse with the plasma membrane and release their contents into the extracellular space (<xref ref-type="bibr" rid="B246">Wu et al., 2014</xref>; <xref ref-type="bibr" rid="B185">Rudolph et al., 2015</xref>). A crucial role of the Golgi apparatus in constitutive secretion, ensuring a continuous supply of essential molecules from the cell to the extracellular environment, has also been documented (<xref ref-type="bibr" rid="B37">Burgess and Kelly, 1987</xref>; <xref ref-type="bibr" rid="B24">Bauerfeind and Huttner, 1993</xref>). Additionally, the Golgi apparatus is involved in regulating the lipid composition, which is crucial for the integrity, fluidity, and function of cell membranes (<xref ref-type="bibr" rid="B4">Agliarulo and Parashuraman, 2022</xref>).</p>
<p>Lysosomes are membrane-bound organelles that contain various hydrolytic enzymes that break down different types of biomolecules. Lysosomes are known for their high dynamics, capable of fusing with membrane vesicles originating from endocytosis, autophagocytosis, and phagocytosis (<xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>; <xref ref-type="bibr" rid="B10">Amaral et al., 2023</xref>). Lysosomes play a crucial role in cellular waste disposal, digestion of foreign materials, recycling of cellular components, and signaling. Lysosome dysfunction can lead to lysosomal storage diseases (LSDs).</p>
<p>LSDs are a group of rare inherited disorders characterized by defects in lysosomal function, leading to the accumulation of undegraded substances within lysosomes throughout the body. Lysosomes are cellular compartments containing enzymes that break down various biomolecules, such as carbohydrates, lipids, and proteins (<xref ref-type="bibr" rid="B186">Samie and Xu, 2014</xref>). In LSDs, genetic mutations result in the deficiency or malfunction of specific lysosomal enzymes, preventing the proper breakdown of these substances (<xref ref-type="bibr" rid="B177">Ren and Wang, 2020</xref>). Consequently, undegraded materials accumulate within lysosomes, causing cellular dysfunction and impairing the functioning of organs and tissues (<xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>). The diverse array of LSDs manifests in a spectrum of symptoms, including neurological impairment, skeletal abnormalities, organ dysfunction, and other systemic complications. These disorders often present challenges for diagnosis and management due to their rarity, complexity, and variability in clinical manifestations (<xref ref-type="bibr" rid="B208">Sun, 2018</xref>; <xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>). Though individually rare, as a group, LSDs underscore the critical role of lysosomes in maintaining cellular homeostasis and the severe consequences that result from their dysfunction (<xref ref-type="bibr" rid="B186">Samie and Xu, 2014</xref>).</p>
<p>While the role of genetic mutations in causing LSDs has been extensively investigated, the impact of Golgi defects observed in diseases on lysosomal biogenesis and function has been somewhat overlooked in the research field. This review aims to consolidate current knowledge on the mechanism of Golgi structure formation, function, and defects in diseases. We then explore the connection between the Golgi and lysosomes under physiological and pathological conditions. By drawing attention to Golgi defects as an underappreciated contributor to lysosomal dysfunction across various diseases, we seek to enhance comprehension of these intricate cellular processes, particularly by investigating Golgi defects in human diseases associated with LSDs not linked to genetic mutations.</p>
</sec>
<sec id="s2">
<title>2 GRASP proteins and their impact on Golgi structure, function, and disease-related defects</title>
<p>The Golgi apparatus has been extensively studied in recent decades (<xref ref-type="bibr" rid="B65">Farquhar and Palade, 1998</xref>). With proteomics, engineered genetics, and biochemical approaches, several essential structural proteins associated with this cellular organelle were identified (<xref ref-type="bibr" rid="B199">Slusarewicz et al., 1994</xref>; <xref ref-type="bibr" rid="B148">Nakamura et al., 1995</xref>; <xref ref-type="bibr" rid="B245">Wu et al., 2000</xref>). The stacking of the Golgi apparatus is a complex and dynamic process involving a series of proteins, including Golgins, Golgi Reassembly and Stacking Proteins (GRASPs), Golgi matrix proteins, microtubules, and motor proteins (<xref ref-type="bibr" rid="B248">Xiang and Wang, 2011</xref>; <xref ref-type="bibr" rid="B273">Zhang and Wang, 2015b</xref>). All these proteins are essential for the formation and preservation of the structural integrity and shape of the Golgi apparatus within eukaryotic cells (<xref ref-type="bibr" rid="B81">Glick and Nakano, 2009</xref>; <xref ref-type="bibr" rid="B240">Wang and Seemann, 2011</xref>).</p>
<p>In mammalian and other eukaryotic cells, the Golgi apparatus consists of flattened cisternae (membrane-enclosed sacs) that originate from vesicular clusters budding off the ER (<xref ref-type="bibr" rid="B105">Jensen and Schekman, 2011</xref>), and Golgi stacks are interconnected by tubular membrane structures to form a ribbon (<xref ref-type="bibr" rid="B120">Klumperman, 2011</xref>). Golgi ribbon formation requires the integrity of a microtubule network (<xref ref-type="bibr" rid="B243">Wei and Seemann, 2010</xref>). Without these connections, the Golgi would exist as individual stacks dispersed in the cytoplasm. In plant cells, however, Golgi stacks are linked by actin filaments rather than microtubules (<xref ref-type="bibr" rid="B58">Driouich et al., 2012</xref>). In this section, we will focus on the role of GRASPs in the structure and function of the Golgi under physiological and pathological conditions. The role of Golgins, Golgi matrix proteins, and microtube/motor proteins in the preservation of Golgi stacks was reviewed elsewhere (<xref ref-type="bibr" rid="B194">Short et al., 2005</xref>; <xref ref-type="bibr" rid="B135">Lowe, 2011</xref>; <xref ref-type="bibr" rid="B248">Xiang and Wang, 2011</xref>).</p>
<sec id="s2-1">
<title>2.1 GRASP proteins and Golgi structure formation</title>
<p>GRASPs, initially identified as Golgi stacking factors (<xref ref-type="bibr" rid="B22">Barr et al., 1997</xref>; <xref ref-type="bibr" rid="B196">Shorter et al., 1999</xref>), have been shown to play crucial roles in the formation and maintenance of Golgi stacks and the overall function of the Golgi apparatus (<xref ref-type="bibr" rid="B273">Zhang and Wang, 2015b</xref>; <xref ref-type="bibr" rid="B171">Rabouille and Linstedt, 2016</xref>). They have the capability to link adjacent cisternae by forming <italic>trans</italic>-oligomers, effectively tethering one cisterna to another in an orderly fashion (<xref ref-type="bibr" rid="B241">Wang et al., 2003</xref>; <xref ref-type="bibr" rid="B247">Xiang and Wang, 2010</xref>; <xref ref-type="bibr" rid="B104">Jarvela and Linstedt, 2014</xref>). Two main GRASP proteins have been identified: GRASP55 (molecular weight 55&#xa0;kDa) and GRASP65 (molecular weight 65&#xa0;kDa) (<xref ref-type="fig" rid="F1">Figure 1</xref>) (<xref ref-type="bibr" rid="B22">Barr et al., 1997</xref>; <xref ref-type="bibr" rid="B196">Shorter et al., 1999</xref>). These proteins display distinct localizations within the Golgi stack (<xref ref-type="bibr" rid="B196">Shorter et al., 1999</xref>). GRASP65 predominantly localizes to the <italic>cis</italic>-Golgi, while GRASP55 localizes to the <italic>medial</italic>- and <italic>trans</italic>-cisternae (<xref ref-type="fig" rid="F2">Figure 2A</xref>) (<xref ref-type="bibr" rid="B196">Shorter et al., 1999</xref>).</p>
<fig id="F1" position="float">
<label>FIGURE 1</label>
<caption>
<p>Domain structure, modification, and binding sites on GRASP55 <bold>(A)</bold> and GRASP65 <bold>(B)</bold>. Rat GRASP55 and GRASP65 sequences are used for illustration. Both GRASPs exhibit a similar structural organization: a conserved N-terminal GRASP domain comprising two PDZ domains (PDZ1 and PDZ2), and a C-terminal Serine/Proline-Rich (SPR) domain featuring multiple phosphorylation sites, which play crucial roles in GRASP regulation throughout the cell cycle. GRASP55 is also acetylated on K50; deacetylation is required for postmitotic Golgi reassembly. GRASP65 and GRASP55 are both peripheral membrane proteins anchored to the Golgi membranes via N-terminal myristoylation and interaction with their respective membrane-bound partner proteins (GM130 and Golgin-45). Mena and DjA1 are GRASP65-binding proteins identified to enhance Golgi ribbon linking and stacking, respectively. GRASP55 undergoes regulation by O-GlcNAcylation in response to glucose levels and interacts with LC3 and LAMP2 to facilitate autophagy induction during glucose starvation [modified from (<xref ref-type="bibr" rid="B6">Ahat et al., 2019a</xref>; <xref ref-type="bibr" rid="B131">Li et al., 2019a</xref>)].</p>
</caption>
<graphic xlink:href="fcell-12-1386149-g001.tif"/>
</fig>
<fig id="F2" position="float">
<label>FIGURE 2</label>
<caption>
<p>Golgi fragmentation causes lysosomal dysfunction by missorting and secretion of lysosomal enzymes. <bold>(A)</bold>. In wildtype cells, GRASP55 and GRASP65 maintain the stacked Golgi structure and ensure correct protein sorting. While both lysosomal enzymes and secretory proteins are synthesized in the endoplasmic reticulum (ER), they are processed differently in the Golgi. Lysosomal enzymes modified by mannose-6-phosphate (M6P), which serves as a sorting signal, are recognized by the M6P receptor (M6PR) and delivered to lysosomes via endosomes. Secretory proteins are transported through the Golgi and to the plasma membrane (PM) for secretion (<xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>; <xref ref-type="bibr" rid="B273">Zhang and Wang, 2015b</xref>). <bold>(B)</bold>. In GRASP knockout cells, particularly GRASP55 knockout cells (<xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>), the Golgi stacked structure is disrupted, and mannose-6-phosphorylation of lysosomal enzymes becomes less efficient, leading to missorting and secretion of lysosomal enzymes. Under this condition, only the proform of lysosome enzymes are secreted. Consequently, lysosomes become dysfunctional due to the lack of lysosomal hydrolases (<xref ref-type="bibr" rid="B274">Zhang and Wang, 2016</xref>; <xref ref-type="bibr" rid="B277">2020a</xref>).</p>
</caption>
<graphic xlink:href="fcell-12-1386149-g002.tif"/>
</fig>
<p>Structural analysis of GRASP55 and GRASP65 revealed that these proteins share similar conserved two PDZ domains (PDZ1 and PDZ2) at the N-terminus (<xref ref-type="fig" rid="F1">Figure 1</xref>). These conserved PDZ domains facilitate the ability of GRASP to form dimers and <italic>trans</italic>-oligomers between stacks and to enable interactions with various Golgi proteins, such as GM130 (associated with GRASP65) and Golgin-45 (associated with GRASP55) (<xref ref-type="bibr" rid="B91">Hu et al., 2015</xref>; <xref ref-type="bibr" rid="B281">Zhao et al., 2017</xref>), as well as enzymes and cytoskeletal components, which are critical for the organization and function of the Golgi apparatus (<xref ref-type="bibr" rid="B6">Ahat et al., 2019a</xref>; <xref ref-type="bibr" rid="B131">Li et al., 2019a</xref>). GRASP55 and GRASP65, however, differ in the serine proline-rich (SPR) domain at the C-terminus, which contains several phosphorylation sites that play an important role in Golgi dynamics during the cell cycle or under pathological conditions (<xref ref-type="bibr" rid="B238">Wang et al., 2005</xref>; <xref ref-type="bibr" rid="B235">Vielemeyer et al., 2009</xref>; <xref ref-type="bibr" rid="B218">Tang et al., 2012</xref>; <xref ref-type="bibr" rid="B112">Joshi et al., 2014</xref>).</p>
<p>Recently, several new GRASP-binding proteins have been identified. For instance, GRASP65 has been shown to interact with the actin elongation factor Mena (mammalian-enabled homolog) and the Hsc70 co-chaperone DjA1 (DnaJ homolog subfamily A member 1) (<xref ref-type="fig" rid="F1">Figure 1</xref>) (<xref ref-type="bibr" rid="B220">Tang et al., 2016</xref>; <xref ref-type="bibr" rid="B132">Li et al., 2019b</xref>). Mena-GRASP65 interaction promotes actin polymerization and GRASP65 oligomerization in Golgi structure formation (<xref ref-type="bibr" rid="B220">Tang et al., 2016</xref>). DjA1 was initially identified as a GRASP65-interacting protein through affinity purification and mass spectrometry. Depletion of DjA1 in cells led to Golgi fragmentation, characterized by short and improperly aligned cisternae, as well as delayed Golgi reassembly following nocodazole washout. DjA1 is known as a co-chaperone of Heat shock cognate 71&#xa0;kDa protein (Hsc70) that also indirectly interacts with GRASP65 through DjA1. Initially, it was speculated that DjA1 facilitated GRASP65 folding. However, subsequent experiments ruled out this notion, demonstrating that DjA1&#x2019;s role in Golgi structure formation is independent of its co-chaperone activity or Hsc70. Despite being recognized primarily as an Hsc70 co-chaperone, DjA1 directly interacts with GRASP65 to facilitate its oligomerization and promote Golgi stack formation in an Hsc70-independent manner, revealing a novel function of this protein (<xref ref-type="bibr" rid="B132">Li et al., 2019b</xref>).</p>
<p>On the other hand, GRASP55 can interact with Microtubule-associated protein one light chain 3 (LC3) on autophagosomes and LAMP2 on lysosomes to facilitate autophagosome-lysosome fusion (<xref ref-type="bibr" rid="B271">Zhang et al., 2018</xref>; <xref ref-type="bibr" rid="B276">Zhang and Wang, 2018b</xref>; <xref ref-type="bibr" rid="B275">a</xref>). GRASP55 also interacts with Beclin-1 (BECN1) to facilitate the UVRAG phosphatidylinositol 3-kinase (PI3K) complex formation and membrane association (<xref ref-type="bibr" rid="B270">Zhang et al., 2019b</xref>). Moreover, GRASP55 is required for unconventional secretion of cystic fibrosis transmembrane conductance regulator (CFTR) and transforming growth factor beta 1 (TGF&#x3b2;1) (<xref ref-type="bibr" rid="B77">Gee et al., 2011</xref>; <xref ref-type="bibr" rid="B155">Nuchel et al., 2018</xref>). These interactions highlight the diverse roles of GRASP proteins in cellular processes beyond Golgi structure maintenance, involving functions in actin dynamics, autophagy, and unconventional protein secretion (<xref ref-type="bibr" rid="B278">Zhang and Wang, 2020b</xref>).</p>
<p>Several studies have documented that the tethering of Golgi cisternae in an ordered manner by GRASP proteins is essential for the proper function of the Golgi. This organized tethering and stacking process is likely required for the precise and sequential posttranslational modifications of proteins and lipids as they move between cisternae, facilitating efficient processing and sorting (<xref ref-type="bibr" rid="B273">Zhang and Wang, 2015b</xref>; <xref ref-type="bibr" rid="B94">Huang and Wang, 2017</xref>). Experiments of inhibition and depletion of GRASP proteins have played a crucial role in elucidating the functions of GRASPs in Golgi stacking and trafficking processes. For example, inhibiting GRASPs&#x2019; function through microinjecting GRASP antibodies, knocking down GRASPs expression levels with siRNA, or depleting GRASPs from cells using the CRISPR/Cas9 approach led to significant alterations in Golgi stacks, including Golgi fragmentation (<xref ref-type="bibr" rid="B241">Wang et al., 2003</xref>; <xref ref-type="bibr" rid="B219">Tang et al., 2010b</xref>; <xref ref-type="bibr" rid="B25">Bekier et al., 2017</xref>). It is noteworthy that a cell-based study concluded that acute GRASP depletion did not affect Golgi stacking (<xref ref-type="bibr" rid="B280">Zhang and Seemann, 2021</xref>). However, the average number of cisternae per stack in this study was about 4, significantly lower than what is typically seen in various cell lines. Based on the literature, the number of cisternae within a stack varies between 4 and 11 in mammalian cells (<xref ref-type="bibr" rid="B175">Rambourg and Clermont, 1997</xref>). In our electron microscopy (EM) studies of the Golgi, we consistently observe that the typical number of cisternae per Golgi stack is approximately five to six in HeLa cells (<xref ref-type="bibr" rid="B219">Tang et al., 2010b</xref>; <xref ref-type="bibr" rid="B247">Xiang and Wang, 2010</xref>; <xref ref-type="bibr" rid="B220">Tang et al., 2016</xref>; <xref ref-type="bibr" rid="B25">Bekier et al., 2017</xref>; <xref ref-type="bibr" rid="B132">Li et al., 2019b</xref>; <xref ref-type="bibr" rid="B100">Ireland et al., 2020</xref>), CHO cells, and primary cultured hippocampal neurons (<xref ref-type="bibr" rid="B112">Joshi et al., 2014</xref>). Importantly, it appears that this study only counted properly aligned stacked membranes, which may have impacted the conclusion. In another study, mice deficient in either GRASP55 or GRASP65 exhibited limited defects in Golgi structure and function (<xref ref-type="bibr" rid="B231">Veenendaal et al., 2014</xref>; <xref ref-type="bibr" rid="B45">Chiritoiu et al., 2019</xref>). One potential concern regarding the GRASP65 knockout mouse strain is the presence of mRNA encoding exon one to three, which encodes a 115 aa N-terminal fragment of GRASP65. If this fragment is translated, it could potentially be sufficient for Golgi stacking (<xref ref-type="bibr" rid="B219">Tang et al., 2010b</xref>). Alternatively, the organized Golgi structure may be attributed to the redundancy of the other GRASP protein, which could compensate for the knockout effect of one GRASP. Indeed, it has been shown that, in cells where one GRASP is depleted, the level of the remaining GRASP protein may increase to offset the knockout effect (<xref ref-type="bibr" rid="B25">Bekier et al., 2017</xref>; <xref ref-type="bibr" rid="B6">Ahat et al., 2019a</xref>). In cells, the expression of phosphorylation-deficient mutants of GRASP55 and GRASP65 has been shown to increase the number of cisternae per stack in interphase cells and to inhibit the disassembly of Golgi stacks in mitosis (<xref ref-type="bibr" rid="B238">Wang et al., 2005</xref>; <xref ref-type="bibr" rid="B219">Tang et al., 2010b</xref>; <xref ref-type="bibr" rid="B247">Xiang and Wang, 2010</xref>). Overexpression of either GRASP55 or GRASP65 alone in HEK293 cells transfected with a plasmid containing the deleted phenylalanine-508 (&#x394;F508) mutation in the cystic fibrosis transmembrane conductance regulator (CFTR) could induce the surface expression of &#x394;F508-CFTR and rescue chloride channel activity. In &#x394;F508-CFTR transgenic mice, overexpression of GRASP55 led to a significant improvement in the survival of the mice (<xref ref-type="bibr" rid="B77">Gee et al., 2011</xref>). These findings suggest that GRASP proteins play dual roles in Golgi structure formation and unconventional trafficking of CFTR.</p>
</sec>
<sec id="s2-2">
<title>2.2 Cell cycle regulation of Golgi membrane dynamics via GRASP proteins</title>
<p>The Golgi apparatus is a highly dynamic organelle capable of adapting its structure to various cellular signals (<xref ref-type="bibr" rid="B19">Bankaitis et al., 2012</xref>; <xref ref-type="bibr" rid="B215">Tang and Wang, 2013</xref>). During mammalian cell division, Golgi stacks undergo disassembly and subsequent reassembly after division (<xref ref-type="bibr" rid="B240">Wang and Seemann, 2011</xref>; <xref ref-type="bibr" rid="B215">Tang and Wang, 2013</xref>). The mechanism by which GRASP proteins control the unstacking and stacking of Golgi cisternae has been extensively investigated. Converging data indicate that phosphorylation and dephosphorylation events of GRASP proteins play crucial roles in the disassembly and reassembly of Golgi stacks (<xref ref-type="bibr" rid="B217">Tang et al., 2010a</xref>). GRASP proteins undergo phosphorylation during cell division, leading to their de-oligomerization and subsequent disassembly of Golgi stacks. After cell division, GRASP proteins are dephosphorylated, facilitating the formation of GRASP65 oligomers and the subsequent reassembly of Golgi cisternae (<xref ref-type="bibr" rid="B241">Wang et al., 2003</xref>; <xref ref-type="bibr" rid="B238">Wang et al., 2005</xref>; <xref ref-type="bibr" rid="B247">Xiang and Wang, 2010</xref>).</p>
<p>These findings were further substantiated by experiments demonstrating that phosphorylation of GRASP by recombinant Cyclin dependent kinase 1 (Cdk1)/cyclin B1 and Polo-like kinase (Plk1) in mitosis induces the disassembly of GRASP oligomers, resulting in unstacking of Golgi cisternae (<xref ref-type="fig" rid="F1">Figure 1</xref>) (<xref ref-type="bibr" rid="B238">Wang et al., 2005</xref>; <xref ref-type="bibr" rid="B217">Tang et al., 2010a</xref>). In cells overexpressing mutant GRASP proteins lacking the phosphorylation sites, the mitotic Golgi disassembly of stacks is inhibited, as GRASP proteins cannot undergo de-oligomerization (<xref ref-type="bibr" rid="B238">Wang et al., 2005</xref>; <xref ref-type="bibr" rid="B219">Tang et al., 2010b</xref>). Similarly, in <italic>Drosophila</italic> cells, knockdown of dGRASP (the sole GRASP protein in <italic>Drosophila</italic>) using RNAi induces the disassembly of Golgi stacks (<xref ref-type="bibr" rid="B122">Kondylis et al., 2005</xref>). Phosphorylation of GRASP65 by JNK2 has been demonstrated to control Golgi fragmentation at the G2/M transition (<xref ref-type="bibr" rid="B40">Cervigni et al., 2015</xref>). Furthermore, GRASP65 has been identified as a regulator of spindle dynamics, playing an essential role in cell division (<xref ref-type="bibr" rid="B210">Sutterlin et al., 2005</xref>).</p>
<p>The role of GRASP55 in Golgi stacking is also regulated by Sirtuin 2 (SIRT2) (<xref ref-type="bibr" rid="B268">Zhang et al., 2019a</xref>), a NAD-dependent sirtuin deacetylase that involves various cellular processes, such as microtubule and chromatin dynamics, gene expression, cell cycle progression, and nuclear envelope reassembly (<xref ref-type="bibr" rid="B154">North et al., 2003</xref>; <xref ref-type="bibr" rid="B161">Pandithage et al., 2008</xref>; <xref ref-type="bibr" rid="B103">Janke, 2014</xref>; <xref ref-type="bibr" rid="B114">Kaufmann et al., 2016</xref>). Depletion of SIRT2 in cells induces Golgi fragmentation and impairs Golgi reassembly at the end of mitosis due to acetylation of GRASP55 (<xref ref-type="bibr" rid="B268">Zhang et al., 2019a</xref>). During mitosis, SIRT2 interacts with highly acetylated GRASP55, regulating its acetylation levels. When expressed in GRASP55 and GRASP65 double-knockout cells, both wild-type (WT) and acetylation-deficient mutant of GRASP55, but not an acetylation mimetic mutant, successfully restored the Golgi structure and facilitated post-mitotic Golgi reassembly. Notably, the acetylation-deficient mutant of GRASP55 showed a higher self-interaction efficiency, which is essential for Golgi structure formation. These findings highlight the regulatory role of SIRT2 in Golgi structure through the modulation of GRASP55 acetylation at the end of mitosis (<xref ref-type="bibr" rid="B268">Zhang et al., 2019a</xref>).</p>
<p>In addition to GRASP proteins, other Golgi proteins are regulated by other mechanisms during the cell cycle. For example, the SNARE protein syntaxin-5 (<xref ref-type="bibr" rid="B93">Huang et al., 2016</xref>) is regulated by ubiquitination mediated by the HECT domain and ankyrin repeat-containing E3 ubiquitin protein ligase 1 (HACE1) (<xref ref-type="bibr" rid="B216">Tang et al., 2011</xref>) and the deubiquitinase valosin-containing protein (VCP) complex-interacting protein 135&#xa0;kDa (VCIP135) (<xref ref-type="bibr" rid="B239">Wang et al., 2004</xref>; <xref ref-type="bibr" rid="B279">Zhang et al., 2014</xref>; <xref ref-type="bibr" rid="B272">Zhang and Wang, 2015a</xref>). The monoubiquitination and deubiquitination cycle regulates p97/VCP-mediated Golgi membrane fusion (<xref ref-type="bibr" rid="B170">Rabouille et al., 1995</xref>; <xref ref-type="bibr" rid="B226">Uchiyama et al., 2002</xref>); disruption of this cycle impairs post-mitotic Golgi membrane fusion (<xref ref-type="bibr" rid="B269">Zhang et al., 2015</xref>; <xref ref-type="bibr" rid="B107">Jiang et al., 2022</xref>). GM130 is known to be phosphorylated by Cdk1 at the onset of mitosis (<xref ref-type="bibr" rid="B136">Lowe et al., 1998</xref>), which regulates spindle assembly (<xref ref-type="bibr" rid="B121">Kodani and Sutterlin, 2008</xref>; <xref ref-type="bibr" rid="B244">Wei et al., 2015</xref>). These different modifications of different proteins coordinate with each other to regulate Golgi membrane dynamics during the cell cycle (<xref ref-type="bibr" rid="B240">Wang and Seemann, 2011</xref>; <xref ref-type="bibr" rid="B215">Tang and Wang, 2013</xref>).</p>
</sec>
<sec id="s2-3">
<title>2.3 Golgi structure formation controls protein trafficking and processing within the Golgi</title>
<p>Upon the arrival of proteins from the ER into the Golgi, a diverse array of post-translational modifications occurs, including the addition or removal of sugar residues in carbohydrate chains (glycosylation), phosphorylation, sulfation, as well as lipid metabolism and the synthesis of complex lipids such as glycolipids and sphingolipids (<xref ref-type="bibr" rid="B94">Huang and Wang, 2017</xref>; <xref ref-type="bibr" rid="B131">Li et al., 2019a</xref>; <xref ref-type="bibr" rid="B124">Kweon et al., 2024</xref>). In addition to these modifications, the Golgi serves as the focal point for sorting and directing proteins and lipids to their intended destinations within the cell, such as the plasma membrane, lysosomes, or various intracellular organelles, where they can carry out their functions (<xref ref-type="bibr" rid="B19">Bankaitis et al., 2012</xref>; <xref ref-type="bibr" rid="B167">Pothukuchi et al., 2021</xref>).</p>
<p>As described earlier, GRASP proteins (GRASP55 and GRASP65) are indispensable for Golgi stack formation and are also involved in the trafficking and sorting of proteins across the Golgi (<xref ref-type="bibr" rid="B53">D&#x27;Angelo et al., 2009</xref>). Depletion of GRASP proteins has been associated with several deficiencies in cargo sorting and trafficking within the Golgi apparatus (<xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>). The intra-Golgi trafficking speed, the accessibility of coat proteins to Golgi membranes, and accurate glycosylation and sorting have all been impacted (<xref ref-type="bibr" rid="B242">Wang et al., 2008</xref>; <xref ref-type="bibr" rid="B273">Zhang and Wang, 2015b</xref>; <xref ref-type="bibr" rid="B274">2016</xref>). GRASP proteins have been implicated in the regulation of cargo trafficking through direct interaction. Certain proteins, such as TGF&#x3b1;, CD83, CD8&#x3b1;, and Frizzled4, possess a C-terminal valine residue that interacts with the PDZ domains of GRASP proteins (<xref ref-type="bibr" rid="B53">D&#x27;Angelo et al., 2009</xref>). Additionally, recent findings have demonstrated that some lipid droplet-associated proteins, including adipose triglyceride lipase (ATGL) and monoglyceride lipase (MGL), utilize a Golgi- and GRASP55-dependent pathway to reach lipid droplets. Interestingly, this process requires a direct interaction between GRASP55 and ATGL, despite the absence of a C-terminal valine in these proteins (<xref ref-type="bibr" rid="B118">Kim et al., 2020</xref>). Furthermore, GRASP55 can directly bind Golgi enzymes such as glucosylceramide synthase and lactosylceramide synthase, facilitating proper compartmentalization within the Golgi (<xref ref-type="bibr" rid="B167">Pothukuchi et al., 2021</xref>). Consequently, GRASP proteins may influence protein trafficking by directly interacting with cargo molecules or by modulating Golgi stacking and vesicle budding.</p>
<p>While the intuitive assumption might be that proper Golgi stacking should increase the trafficking of proteins and Golgi unstacking would decrease the rate of protein trafficking, experiments have shown the opposite (<xref ref-type="bibr" rid="B242">Wang et al., 2008</xref>; <xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>). Instead, Golgi unstacking accelerates protein trafficking. For example, the rate of COPI vesicle formation from Golgi membranes was significantly increased as vesicles formed more efficiently from unstacked cisternae (<xref ref-type="fig" rid="F2">Figure 2B</xref>). This process may enhance protein transport through the Golgi apparatus to the cell surface (<xref ref-type="bibr" rid="B240">Wang and Seemann, 2011</xref>). Consistent with this idea, studies have shown that the depletion of GRASPs accelerates the trafficking of several marker proteins, including CD8, vesicular stomatitis virus G-protein, cathepsin D, and integrins (<xref ref-type="bibr" rid="B242">Wang et al., 2008</xref>; <xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>; <xref ref-type="bibr" rid="B127">Lee et al., 2014</xref>; <xref ref-type="bibr" rid="B25">Bekier et al., 2017</xref>).</p>
<p>Disruption of the Golgi structure via GRASP depletion also significantly alters post-translational modifications of proteins, including a decrease in glycan abundance, glycan complexity, and glycoprotein composition at the plasma membrane (<xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>; <xref ref-type="bibr" rid="B25">Bekier et al., 2017</xref>). It causes missorting of lysosomal enzymes, such as cathepsin D, to the extracellular space (<xref ref-type="fig" rid="F2">Figure 2B</xref>) (<xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>; <xref ref-type="bibr" rid="B273">Zhang and Wang, 2015b</xref>). Disruption of the Golgi structure also impairs glycosaminoglycan synthesis, sulfation, and secretion (<xref ref-type="bibr" rid="B7">Ahat et al., 2022b</xref>). Subsequently, Golgi structural defects alter higher cellular activities such as cell attachment, migration, and growth (<xref ref-type="bibr" rid="B8">Ahat et al., 2019b</xref>). During mitosis, the phosphorylation of &#x3b1;-mannosidase I (ManIA1), the first glycosylation enzyme cargo proteins encounter upon arrival at the Golgi, impairs its interaction with Mgat1, another Golgi glycosylation enzyme, reducing its enzymatic activity. Golgi fragmentation during mitosis disrupts the organized structure of the Golgi apparatus, halting trafficking and leaving the enzymes and substrates within the same membrane compartments for an extended period until trafficking resumes upon mitotic exit. These events collectively contribute to prolonging the interaction between cargo proteins and glycosylation enzymes during mitosis. Mitotic phosphorylation of MAN1A1, the first enzyme that cargo molecules encounter upon arriving at the Golgi, reduces its enzymatic activity. This mechanism serves to prevent over-modification of cargo proteins by Golgi enzymes during cell division (<xref ref-type="bibr" rid="B92">Huang et al., 2022</xref>). All these observations collectively suggest that cisternae stacking is fundamentally important for the Golgi function (<xref ref-type="bibr" rid="B274">Zhang and Wang, 2016</xref>; <xref ref-type="bibr" rid="B277">2020a</xref>).</p>
</sec>
<sec id="s2-4">
<title>2.4 The role of the Golgi in lipid metabolism</title>
<p>The Golgi apparatus plays a pivotal role in lipid metabolism, serving as a central hub for synthesizing, modifying, and sorting lipids within the cell (<xref ref-type="bibr" rid="B19">Bankaitis et al., 2012</xref>). One of its primary functions is the processing of lipids, including the synthesis of complex sphingolipids and glycolipids. Sphingolipids, a diverse class of lipids, are crucial components of cellular membranes and are involved in various cellular processes, including signal transduction and the formation of membrane microdomains (<xref ref-type="bibr" rid="B197">Simons and Ikonen, 1997</xref>). Additionally, glycolipids synthesized in the Golgi contribute to the structural integrity of cell membranes and participate in cell signaling events (<xref ref-type="bibr" rid="B38">Campadelli et al., 1993</xref>).</p>
<p>Disruptions in Golgi function can have profound implications for lipid homeostasis and cellular health (<xref ref-type="bibr" rid="B38">Campadelli et al., 1993</xref>). Alterations in the Golgi apparatus may lead to dysregulation in the levels of specific lipid species, impacting cellular processes. Studies have shown that Golgi dysfunction can result in changes in the levels of key lipids. Indeed, disruption of the Golgi by knocking out GRASP55 and GRASP65 reduces globotriaosylceramide (Gb3) expression but increases monosialotetrahexosylganglioside (GM1) level (<xref ref-type="bibr" rid="B25">Bekier et al., 2017</xref>), highlighting the intricate connections between Golgi function and lipid metabolism. A recent study revealed that GRASP55 selectively binds and compartmentalizes essential glycosphingolipid biosynthetic enzymes. This specific compartmentalization within the Golgi ensures precise biosynthetic reactions and regulates the cellular glycosphingolipid profile (<xref ref-type="bibr" rid="B167">Pothukuchi et al., 2021</xref>).</p>
<p>The delicate balance between GM1 and Gb3 is particularly crucial in Golgi stacks, given their distinct roles in cellular processes (<xref ref-type="bibr" rid="B39">Celi et al., 2022</xref>). Although both GM1 and Gb3 are crucial for myelination, GM1 has also been shown to promote &#x3b2;-amyloid peptide (A&#x3b2;) aggregation and toxicity (<xref ref-type="bibr" rid="B198">Sipione et al., 2020</xref>). It is noteworthy that elevated Gb3 level correlates with the development of gastric, colon, and breast cancers, and Gb3 is also implicated in the mechanisms of Epithelial-to-Mesenchymal Transition (EMT) (<xref ref-type="bibr" rid="B282">Zhuo et al., 2018</xref>). Additionally, Gb3 has been linked to the susceptibility to chemotherapeutic agents, as evidenced by its increased level at the cell surface in cisplatin-resistant cells (<xref ref-type="bibr" rid="B225">Tyler et al., 2015</xref>). These findings further underscore Golgi&#x2019;s involvement in cancer cell adaptation. Further exploration of Golgi&#x2019;s role and its defects in lipid regulation holds promise for understanding the underlying mechanisms of lipid-related disorders. Such exploration may unveil potential therapeutic targets for conditions linked to aberrant lipid metabolism.</p>
</sec>
<sec id="s2-5">
<title>2.5 Golgi defects are observed in human diseases</title>
<p>Golgi structural and functional defects have been observed in various diseases, including Alzheimer&#x2019;s (<xref ref-type="bibr" rid="B13">Aridor and Balch, 1999</xref>; <xref ref-type="bibr" rid="B112">Joshi et al., 2014</xref>; <xref ref-type="bibr" rid="B64">Evin, 2015</xref>; <xref ref-type="bibr" rid="B111">Joshi et al., 2015</xref>; <xref ref-type="bibr" rid="B113">Joshi and Wang, 2015</xref>), Huntington&#x2019;s (<xref ref-type="bibr" rid="B89">Hilditch-Maguire et al., 2000</xref>; <xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>), Parkinson&#x2019;s (<xref ref-type="bibr" rid="B146">Mizuno et al., 2001</xref>), amyotrophic lateral sclerosis (ALS) (<xref ref-type="bibr" rid="B147">Mourelatos et al., 1996</xref>; <xref ref-type="bibr" rid="B84">Gonatas et al., 1998</xref>; <xref ref-type="bibr" rid="B73">Fujita and Okamoto, 2005</xref>), autoimmune diseases (<xref ref-type="bibr" rid="B72">Fritzler et al., 1984</xref>; <xref ref-type="bibr" rid="B27">Bizzaro et al., 1999</xref>), cancer (<xref ref-type="bibr" rid="B254">Yoshimura et al., 1996</xref>; <xref ref-type="bibr" rid="B181">Roberts et al., 1998</xref>; <xref ref-type="bibr" rid="B55">Dennis et al., 1999</xref>; <xref ref-type="bibr" rid="B56">Diaz-Corrales et al., 2004</xref>; <xref ref-type="bibr" rid="B157">Ono and Hakomori, 2004</xref>; <xref ref-type="bibr" rid="B123">Krishnan et al., 2005</xref>), viral infections (<xref ref-type="bibr" rid="B149">Ng et al., 2003</xref>; <xref ref-type="bibr" rid="B47">Cortese et al., 2020</xref>; <xref ref-type="bibr" rid="B263">Zhang et al., 2022</xref>), congenital disorders of glycosylation (<xref ref-type="bibr" rid="B261">Zeevaert et al., 2008</xref>; <xref ref-type="bibr" rid="B137">Lubbehusen et al., 2010</xref>), and Wiskott-Aldrich syndrome (<xref ref-type="bibr" rid="B59">Durand and Seta, 2000</xref>; <xref ref-type="bibr" rid="B71">Freeze and Ng, 2011</xref>). Despite increasing awareness of these associations, the causal relationship between Golgi defects and disease pathogenesis remains largely unexplored. Here, we present a few examples of Golgi defects in human diseases that have been investigated.</p>
<sec id="s2-5-1">
<title>2.5.1 Golgi defects in Alzheimer&#x2019;s diseases</title>
<p>Alzheimer&#x2019;s disease (AD) is characterized by the formation of two types of protein aggregates in the brain: neurofibrillary tangles (NFTs) in neurons formed by hyperphosphorylated tau and extracellular &#x3b2;-amyloid plaques formed by the accumulation of secreted A&#x3b2; (<xref ref-type="bibr" rid="B207">Suh and Checler, 2002</xref>; <xref ref-type="bibr" rid="B201">Small and Gandy, 2006</xref>). A&#x3b2;, a proteolytic product of the amyloid precursor protein (APP), undergoes cleavage by &#x3b1;-, &#x3b2;-, and &#x3b3;-secretases during the later steps of intracellular transport (<xref ref-type="bibr" rid="B201">Small and Gandy, 2006</xref>; <xref ref-type="bibr" rid="B87">Haass et al., 2012</xref>). Trafficking and maturation of APP and its processing enzymes require proper functioning of the Golgi apparatus (<xref ref-type="bibr" rid="B222">Thinakaran et al., 1996</xref>; <xref ref-type="bibr" rid="B57">Dries and Yu, 2008</xref>; <xref ref-type="bibr" rid="B46">Choy et al., 2012</xref>; <xref ref-type="bibr" rid="B168">Prabhu et al., 2012</xref>). APP and all three secretases are synthesized in the ER and transferred to the Golgi, where they are modified by glycosylation, phosphorylation, and proteolysis (<xref ref-type="bibr" rid="B21">Barlowe et al., 1994</xref>; <xref ref-type="bibr" rid="B32">Brandizzi and Barlowe, 2013</xref>). Importantly, glycosylation (<xref ref-type="bibr" rid="B224">Tomita et al., 1998</xref>) and phosphorylation (<xref ref-type="bibr" rid="B234">Vieira et al., 2009</xref>; <xref ref-type="bibr" rid="B20">Barbagallo et al., 2010</xref>) in the Golgi affect APP trafficking and processing. The Golgi plays a pivotal role in the assembly of the &#x3b3;-secretase complex, which includes the catalytic subunit presenilin 1 (PS1) and associated proteins. The complex is formed into active enzymes following PS1 processing and nicastrin glycosylation in the Golgi (<xref ref-type="bibr" rid="B251">Yang et al., 2002</xref>; <xref ref-type="bibr" rid="B211">Takasugi et al., 2003</xref>).</p>
<p>Significantly, the Golgi architecture is abnormally fragmented in neurons from AD human brain and AD mouse models (<xref ref-type="bibr" rid="B52">Dal Canto, 1996</xref>; <xref ref-type="bibr" rid="B205">Stieber et al., 1996</xref>; <xref ref-type="bibr" rid="B84">Gonatas et al., 1998</xref>; <xref ref-type="bibr" rid="B109">Joazeiro and Weissman, 2000</xref>; <xref ref-type="bibr" rid="B95">Huse et al., 2002</xref>; <xref ref-type="bibr" rid="B18">Baloyannis, 2014</xref>; <xref ref-type="bibr" rid="B112">Joshi et al., 2014</xref>; <xref ref-type="bibr" rid="B16">Ayala and Colanzi, 2017</xref>; <xref ref-type="bibr" rid="B188">Santos et al., 2017</xref>). Numerous pathologies in AD may be related to defects in the Golgi and the secretory pathway, including increased production of the toxic A&#x3b2; peptide, abnormal protein glycosylation, and impaired lysosomal/autophagosomal degradation (<xref ref-type="fig" rid="F3">Figure 3</xref>). Investigation into Golgi structure defects in AD reveals that A&#x3b2; oligomer accumulation causes Golgi fragmentation by activating Cdk5 and phosphorylating GRASP65. Expression of APPswe and PS1&#x2206;E9, or treatment of primary neurons with oligomeric A&#x3b2; peptides, leads to Golgi fragmentation. Interestingly, inhibition of &#x3b2;- and &#x3b3;-secretases, but not &#x3b1;-secretase in AD cells, reduces Golgi fragmentation (<xref ref-type="bibr" rid="B112">Joshi et al., 2014</xref>). Rescuing Golgi structure by inhibiting Cdk5 or expressing non-phosphorylatable GRASP mutants reduces A&#x3b2; secretion by elevating non-amyloidogenic &#x3b1;-cleavage of APP. These findings highlight Golgi defects as a critical mechanism for A&#x3b2; toxicity and demonstrate that rescuing Golgi structure reduces A&#x3b2; production by shifting APP cleavage towards the non-amyloidogenic pathway (<xref ref-type="bibr" rid="B112">Joshi et al., 2014</xref>; <xref ref-type="bibr" rid="B64">Evin, 2015</xref>; <xref ref-type="bibr" rid="B111">Joshi et al., 2015</xref>; <xref ref-type="bibr" rid="B113">Joshi and Wang, 2015</xref>).</p>
<fig id="F3" position="float">
<label>FIGURE 3</label>
<caption>
<p>Golgi fragmentation in stress or disease conditions leads to lysosomal dysfunction and unconventional secretion of lysosomal contents. Under stress conditions such as energy and nutrient deprivation (<xref ref-type="bibr" rid="B271">Zhang et al., 2018</xref>; <xref ref-type="bibr" rid="B270">Zhang et al., 2019b</xref>), or in diseases such as Alzheimer&#x2019;s disease (AD) or other types of neurodegeneration (<xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>), or upon viral infection (<xref ref-type="bibr" rid="B263">Zhang et al., 2022</xref>), the Golgi undergoes fragmentation, resulting in misssorting of lysosomal enzymes and reduced lysosomal function. Glucose starvation also reduces O-GlcNAcylation of GRASP55. De-O-GlcNAcylated GRASP55 is then targeted to the autophagosome-lysosome interface via interactions with LC3 and LAMP2, facilitating autophagosome-lysosome fusion (<xref ref-type="bibr" rid="B271">Zhang et al., 2018</xref>). Stress also induces lysosome exocytosis, leading to the secretion of lysosome contents (<xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>). Under these conditions, both the proform and the mature form of lysosomal enzymes, together with aggregative cytoplasmic proteins, are secreted.</p>
</caption>
<graphic xlink:href="fcell-12-1386149-g003.tif"/>
</fig>
</sec>
<sec id="s2-5-2">
<title>2.5.2 Golgi fragmentation in cancer</title>
<p>The role of the Golgi in cancer cells is a subject of ongoing debate, with the structure and function of this organelle being influenced by cancer hallmarks. The Golgi&#x2019;s involvement in cancer extends beyond a mere consequence of transformation, actively contributing to malignancy through aberrant glycosylation, enhanced survival, proliferation, and increased migration (<xref ref-type="bibr" rid="B26">Bisel et al., 2008</xref>). Abnormal Golgi morphology is a common feature in cancer, ranging from constitutively disassembled units to fragmented or indistinguishable structures (<xref ref-type="bibr" rid="B143">Maldonado et al., 1966</xref>; <xref ref-type="bibr" rid="B115">Kellokumpu et al., 2002</xref>; <xref ref-type="bibr" rid="B164">Petrosyan, 2015</xref>). Recent studies suggest that alteration of Golgi dynamics may contribute to cancer malignancy (<xref ref-type="bibr" rid="B266">Zhang, 2021</xref>).</p>
<p>Golgi dispersal is a prevalent feature in various cancer types, including colon, breast, gastric, and prostate cancers (<xref ref-type="bibr" rid="B60">Egea et al., 1993</xref>; <xref ref-type="bibr" rid="B191">Sewell et al., 2006</xref>; <xref ref-type="bibr" rid="B153">Nolfi et al., 2020</xref>). Cancer cell lines often display fragmented Golgi, and tissue sections from cancer patients exhibit distinct Golgi structures compared to non-cancerous cells (<xref ref-type="bibr" rid="B115">Kellokumpu et al., 2002</xref>). Golgi disorganization has been linked to altered protein glycosylation, sorting, and functions, all crucial for cell survival, proliferation, and migration-major hallmarks of cancer (<xref ref-type="bibr" rid="B8">Ahat et al., 2019b</xref>; <xref ref-type="bibr" rid="B36">Bui et al., 2021</xref>; <xref ref-type="bibr" rid="B266">Zhang, 2021</xref>).</p>
<p>Alterations in Golgi structure in cancer align with the progression of the disease. Golgi dispersal is linked to mitotic phosphorylation of Golgi structural proteins and kinase activation induced by proinflammatory cytokines, cellular stresses, and growth factors. Aberrant activation of kinases, such as PKC&#x3b1;, Src, ERK8, and Pak1, has been observed in various cancers, contributing to Golgi fragmentation (<xref ref-type="bibr" rid="B44">Ching et al., 2007</xref>; <xref ref-type="bibr" rid="B43">Chia et al., 2014</xref>; <xref ref-type="bibr" rid="B101">Ireland et al., 2020</xref>). The role of Golgi in mitotic Golgi disassembly and its link to cancer cell changes in cell cycle progression are essential areas of investigation.</p>
<p>Elevated expression of Golgi matrix proteins, including GRASP55 and GM130, has been associated with poor prognosis in some cancers, suggesting their importance in tumor cells (<xref ref-type="bibr" rid="B36">Bui et al., 2021</xref>; <xref ref-type="bibr" rid="B35">Bucurica et al., 2023</xref>). Golgi compaction in cancers has been linked to EMT, a spectrum of hybrid or partial states (<xref ref-type="bibr" rid="B212">Tan et al., 2017a</xref>; <xref ref-type="bibr" rid="B214">Tan et al., 2017b</xref>). Golgi&#x2019;s involvement in enhanced extracellular matrix (ECM) secretion during tumorigenesis, regulated by Golgin-45/myosin IIA-containing protein complex and tumor suppressor genes like p53, underscores its central role in cancer biology (<xref ref-type="bibr" rid="B213">Tan et al., 2021</xref>).</p>
<p>The Golgi stacking proteins GRASP65 and GRASP55 have also implicated in cell cycle control. Phosphorylation of GRASP65 by Cdk1 and Plk1, along with its role in Golgi ribbon formation, suggests a link to cell cycle progression (<xref ref-type="bibr" rid="B133">Lin et al., 2000</xref>; <xref ref-type="bibr" rid="B241">Wang et al., 2003</xref>). GRASP55 phosphorylation by ERK2 (<xref ref-type="bibr" rid="B106">Jesch et al., 2001</xref>; <xref ref-type="bibr" rid="B247">Xiang and Wang, 2010</xref>), a major mitotic kinase, further supports the connection between Golgi structure and cell cycle control. In addition, both GRASP65 and GM130 have been shown to regulate mitotic spindle assembly (<xref ref-type="bibr" rid="B210">Sutterlin et al., 2005</xref>; <xref ref-type="bibr" rid="B121">Kodani and Sutterlin, 2008</xref>; <xref ref-type="bibr" rid="B244">Wei et al., 2015</xref>). In summary, the Golgi&#x2019;s involvement in cancer is multifaceted, impacting cellular processes crucial for malignancy. Understanding the dynamic regulation of Golgi structure and its molecular interactions in cancer cells provides valuable insights into potential therapeutic targets for cancer treatment.</p>
</sec>
<sec id="s2-5-3">
<title>2.5.3 Golgi fragmentation in SARS-CoV-2 infection</title>
<p>The Golgi apparatus emerges as a key player in the intricate interaction between host cells and the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the cause of the COVID-19 pandemic. The virus employs host cell&#x2019;s angiotensin-converting enzyme 2 (ACE2) receptor for entry, where the spike (S) protein undergoes activation by transmembrane serine protease 2 (TMPRSS2) (<xref ref-type="bibr" rid="B236">V&#x27;Kovski et al., 2021</xref>). Following this interaction, the virus fuses with host cell membranes at the cell surface or within endosomes, depending on TMPRSS2 activity. The viral RNA is released into the host cell cytosol, initiating a cascade of events. SARS-CoV-2 engages the host cell&#x2019;s ER to form double-membrane vesicles (DMVs) that support viral genomic RNA replication (<xref ref-type="bibr" rid="B11">Angelini et al., 2013</xref>; <xref ref-type="bibr" rid="B158">Oudshoorn et al., 2017</xref>). The Golgi plays a center role in the later stages of the viral infection cycle, serving as the assembly site for three essential structural proteins - spike, envelope (E), and membrane (M). Intriguingly, the SARS-CoV-2 spike protein undergoes glycosylation in the Golgi, influencing its stability, interaction with ACE2, and susceptibility to vaccines (<xref ref-type="bibr" rid="B187">Sanda et al., 2021</xref>; <xref ref-type="bibr" rid="B223">Tian et al., 2021</xref>). Compared with other SARS-related coronaviruses, the SARS-CoV-2 spike protein possesses a unique furin cleavage site (<xref ref-type="bibr" rid="B41">Chan and Zhan, 2022</xref>), which is cleaved in the late Golgi to facilitate membrane fusion and viral entry (<xref ref-type="bibr" rid="B192">Shang et al., 2020</xref>).</p>
<p>Preliminary findings underscore the profound impact of SARS-CoV-2 infection on the Golgi, leading to Golgi fragmentation (<xref ref-type="bibr" rid="B263">Zhang et al., 2022</xref>). Disrupting Golgi function with small molecules, such as brefeldin A and monensin, significantly reduces viral infection (<xref ref-type="bibr" rid="B263">Zhang et al., 2022</xref>). This suggests a critical role of the Golgi in the SARS-CoV-2 lifecycle. Furthermore, the infection results in decreased expression of GRASP55 (<xref ref-type="bibr" rid="B263">Zhang et al., 2022</xref>). Intriguingly, expression of various SARS-CoV-2 viral proteins, including spike, ORF3a, M, and E, induces Golgi fragmentation, providing insights into the molecular mechanisms of viral-induced Golgi structural changes (<xref ref-type="bibr" rid="B263">Zhang et al., 2022</xref>). As described above, GRASP55 is a known key player in Golgi cisternae stacking (<xref ref-type="bibr" rid="B247">Xiang and Wang, 2010</xref>), its reduced expression disrupts the Golgi structure and accelerates protein trafficking (<xref ref-type="bibr" rid="B242">Wang et al., 2008</xref>; <xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>). These results indicate that SARS-CoV-2 modulates Golgi structure and function by decreasing GRASP55 expression to facilitate viral trafficking and secretion (<xref ref-type="bibr" rid="B263">Zhang et al., 2022</xref>). This finding is significant as it reveals a non-genetic factor affecting viral production and infectivity.</p>
<p>One profound impact of SARS-CoV-2 infection is that it can cause an AD-like neuropathological phenotype and clinical &#x201c;brain fog&#x201d; (<xref ref-type="bibr" rid="B67">Fernandez-Castaneda et al., 2022</xref>; <xref ref-type="bibr" rid="B260">Zazhytska et al., 2022</xref>). SARS-CoV-2 infection and AD are similar in that both diseases induce Golgi fragmentation (<xref ref-type="bibr" rid="B112">Joshi et al., 2014</xref>; <xref ref-type="bibr" rid="B263">Zhang et al., 2022</xref>). The convergence of SARS-CoV-2 infection and AD pathology at the Golgi raises questions about shared molecular pathways (<xref ref-type="bibr" rid="B237">Wang and Gandy, 2022</xref>). Both diseases involve type I membrane proteins, such as the SARS-CoV-2 spike protein and APP, which undergo similar modifications in the Golgi and are impacted by Golgi fragmentation. It is possible that SARS-CoV-2 infection-triggered Golgi fragmentation may potentially accelerate APP trafficking and processing, activating an AD-like program. The observed &#x201c;brain fog&#x201d; associated with SARS-CoV-2 infection, reflecting cognitive impairment, adds another layer of complexity. Golgi fragmentation induced by the virus may enhance cytokine secretion, contributing to cognitive symptoms. Additionally, SARS-CoV-2-induced defects in myelination, possibly related to Golgi fragmentation, might explain cognitive impairment, given the Golgi&#x2019;s role in lipid synthesis (<xref ref-type="bibr" rid="B67">Fernandez-Castaneda et al., 2022</xref>). Furthermore, the Golgi&#x2019;s involvement extends beyond its structure, as Golgi fragmentation may impact distal compartments of the secretory pathway, including autophagosomes and lysosomes (<xref ref-type="bibr" rid="B278">Zhang and Wang, 2020b</xref>), as discussed below. Understanding these molecular and cellular dysfunctions is crucial for comprehending the broader implications of Golgi fragmentation in SARS-CoV-2 infection and AD. Exploring the therapeutic potential of GRASPs and Golgi-targeted interventions may provide valuable insights into addressing currently untreatable human diseases (<xref ref-type="bibr" rid="B237">Wang and Gandy, 2022</xref>).</p>
</sec>
</sec>
</sec>
<sec id="s3">
<title>3 Lysosomes and their roles in cellular homeostasis</title>
<sec id="s3-1">
<title>3.1 Lysosomal functions</title>
<p>A defining feature of lysosomes is their ability to maintain an acidic pH of around 4.5, a critical condition for the optimal activity of hydrolytic enzymes (<xref ref-type="bibr" rid="B10">Amaral et al., 2023</xref>). These organelles contain numerous hydrolases that can break down various biomolecules, including proteins, lipids, carbohydrates, nucleic acids, misfolded or damaged proteins and organelles, and cellular debris. This enzymatic breakdown prevents the accumulation of toxic aggregates and upholds proper protein quality control (<xref ref-type="bibr" rid="B42">Chen et al., 2011</xref>). The resulting processed materials, such as amino acids and sugars, can either be recycled for reuse or eliminated, ensuring the cell remains devoid of accumulated waste materials that could disrupt cellular function, thereby maintaining cellular homeostasis (<xref ref-type="bibr" rid="B140">Luzio et al., 2014</xref>; <xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>).</p>
<p>Additionally, studies indicate that lysosomes can participate in cellular signaling pathways. They also release certain enzymes and molecules into the cytoplasm or extracellular space, affecting various cellular processes such as autophagy, cell growth, and apoptosis (<xref ref-type="bibr" rid="B29">Bonam et al., 2019</xref>). Furthermore, lysosomes contain potent enzymes that regulate lipid metabolism by breaking down complex lipids into their constituent components. This process allows the cell to utilize these molecules for energy or rebuild the membrane (<xref ref-type="bibr" rid="B252">Yim and Mizushima, 2020</xref>; <xref ref-type="bibr" rid="B250">Yang and Wang, 2021</xref>). In summary, lysosomal function is central to the cell&#x2019;s waste disposal, protein quality control, lipid metabolism, signaling, and protection against pathogens (<xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>; <xref ref-type="bibr" rid="B250">Yang and Wang, 2021</xref>).</p>
</sec>
<sec id="s3-2">
<title>3.2 Lysosomal storage diseases</title>
<p>Lysosomal storage diseases (LSDs) constitute a rare group of inherited genetic diseases characterized by impaired lysosomal function (<xref ref-type="bibr" rid="B208">Sun, 2018</xref>). While most LSDs follow an autosomal recessive inheritance pattern, some, such as Hunter disease, Fabry disease, and Danon disease, are X-linked inheritance patterns (<xref ref-type="bibr" rid="B173">Rajkumar and Dumpa, 2023</xref>). Mutations in genes encoding lysosomal enzymes are the primary cause of LSDs. LSDs encompass over 70 different genetic disorders. Each condition arises due to a deficiency in a specific lysosomal protein or activity (<xref ref-type="bibr" rid="B75">Futerman and van Meer, 2004</xref>; <xref ref-type="bibr" rid="B193">Sheth et al., 2023</xref>). LSDs are typically progressive and can affect multiple organ systems, including the central nervous system (<xref ref-type="bibr" rid="B173">Rajkumar and Dumpa, 2023</xref>). It is important to note that not all mutations result in defective enzymes.</p>
<p>LSDs are classified based on the specific enzyme deficiency or the accumulated material (<xref ref-type="bibr" rid="B208">Sun, 2018</xref>; <xref ref-type="bibr" rid="B173">Rajkumar and Dumpa, 2023</xref>). There are seven classes of LSDs. 1) Sphingolipidoses, caused by the accumulation of phospholipid materials. This class includes GM2 gangliosidosis (such as Tay-Sachs disease and Sandhoff disease), Niemann-Pick diseases (A, B, and C types), Gaucher disease, Fabry disease, Metachromatic leukodystrophy, Krabbe disease, and multiple sulfatase deficiency. 2) Oligosaccharidoses result from deficiencies in enzymes involved in oligosaccharide breakdown. This class includes alpha-mannosidosis, Schindler disease, Aspartylglucosaminuria, and Fucosidosis. 3) Mucopolysaccharidoses due to the buildup of mucopolysaccharides. Examples include Hurler syndrome, Hunter syndrome, Sanfilippo syndrome, Morquio syndrome, Maroteaux-Lamy syndrome, and Sly syndrome. 4) Neuronal ceroid lipofuscinoses that are characterized by the accumulation of lipopigments in neuronal tissues. 5) Galactosialidosis, which results from defects in enzyme protection proteins. This includes disorders like infantile sialic acid storage disease, Salla disease, and Sialuria. 6) Mucolipidoses, resulting from membrane transport defects, leading to targeting errors. Subtypes include Sialidosis I and II (Mucolipidosis I), I-cell disease (Mucolipidosis II), Pseudo-Hurler-Polydystrophy (Mucolipidosis III), and Mucolipidosis IV. 7) Miscellaneous LSDs, including conditions like Lysosomal Acid Lipase Deficiency (accumulation of cholesterol esters), Pompe disease (glycogen storage disease type II), Danon disease (glycogen), and Cystinosis (cystine) (<xref ref-type="bibr" rid="B190">Schulze and Sandhoff, 2011</xref>; <xref ref-type="bibr" rid="B68">Ferreira and Gahl, 2017</xref>; <xref ref-type="bibr" rid="B165">Platt et al., 2018</xref>).</p>
<p>Studies of fibroblast cells derived from patients with LSDs have played a crucial role in providing information about lysosomal enzyme deficiencies and the classification of LSD types (<xref ref-type="bibr" rid="B69">Filocamo and Morrone, 2011</xref>; <xref ref-type="bibr" rid="B233">Venkatarangan et al., 2023</xref>). Various forms of enzyme deficiencies have been identified. While many of these disorders are due to enzyme deficiencies, increasing cases have been attributed to issues such as failure to segregate into lysosomes, instability, rapid inactivation, or lack of function due to the absence of activator proteins (<xref ref-type="bibr" rid="B162">Parenti, 2009</xref>). Patients sharing the same enzyme deficiency may also possess allelic mutations causing the same defect via diverse mechanisms. This phenomenon is well-documented in Tay-Sachs disease (<xref ref-type="bibr" rid="B23">Barritt et al., 2017</xref>; <xref ref-type="bibr" rid="B174">Ramani and Parayil Sankaran, 2023</xref>), metachromatic leukodystrophy (<xref ref-type="bibr" rid="B80">Gieselmann et al., 1991</xref>; <xref ref-type="bibr" rid="B125">Lamichhane and Rocha Cabrero, 2023</xref>), and Pompe disease (<xref ref-type="bibr" rid="B12">Arad et al., 2005</xref>; <xref ref-type="bibr" rid="B232">Vellodi, 2005</xref>; <xref ref-type="bibr" rid="B230">van der Ploeg and Reuser, 2008</xref>).</p>
<p>LSDs comprise a diverse range of clinical phenotypes, and the severity of symptoms can vary significantly even within the same disorder type. For example, mucolipidosis II (ML-II) and mucolipidosis III (ML-III) are LSDs that exhibit different levels of deficiency in GlcNAc-1-phosphotransferase activity. Extremely low or undetectable enzyme levels characterize ML-II, whereas ML-III shows some residual phosphorylating activity (<xref ref-type="bibr" rid="B116">Khan and Tomatsu, 2020</xref>). Certain patients exhibit increased secretion of multiple lysosomal enzymes within ML-III, while others display highly elevated plasma lysosomal enzymes (<xref ref-type="bibr" rid="B159">Oussoren et al., 2018</xref>; <xref ref-type="bibr" rid="B116">Khan and Tomatsu, 2020</xref>). Due to the deficiency of phosphotransferase activity in these patients, the phosphomannosyl recognition marker on glycosylated enzymes cannot be synthesized, preventing their proper targeting to lysosomes. Consequently, some enzymes are secreted into the extracellular milieu instead of being directed to lysosomes (<xref ref-type="bibr" rid="B159">Oussoren et al., 2018</xref>; <xref ref-type="bibr" rid="B116">Khan and Tomatsu, 2020</xref>). Interestingly, not all cells deficient in phosphotransferase activity lead to the mistargeting of lysosomal enzymes. In certain cell types like hepatocytes, Kupffer cells, and leukocytes, there are nearly regular levels of lysosomal enzymes, suggesting an alternative targeting mechanism distinct from the M6P pathway (<xref ref-type="bibr" rid="B200">Sly, 2000</xref>). Moreover, in ML-III fibroblasts, it has been observed that the affinity of phosphotransferase for lysosomal enzymes is markedly reduced, indicating that these patients may possess normal levels of phosphotransferase but with impaired recognition function (<xref ref-type="bibr" rid="B159">Oussoren et al., 2018</xref>; <xref ref-type="bibr" rid="B116">Khan and Tomatsu, 2020</xref>).</p>
<p>In the case of Pompe disease (glycogenosis type II), it has been observed that the acid alpha-glucosidase enzyme is produced in normal quantities as a precursor form (110-kD). However, the mature 76-kD enzyme is either completely absent or highly inefficient (<xref ref-type="bibr" rid="B178">Reuser et al., 1995</xref>). In all reported cases of Pompe disease, it has been observed that glycosylation of the mutant precursors remains unaffected. This implies that either the glycosylated precursor fails to move from the ER to the Golgi apparatus, where phosphorylation typically occurs, or that the mutation leads to a loss of recognition by the phosphotransferase within the Golgi (<xref ref-type="bibr" rid="B145">Meena and Raben, 2020</xref>; <xref ref-type="bibr" rid="B221">Taverna et al., 2020</xref>).</p>
<p>Similarly, in Tay-Sachs disease, a lysosomal storage diseases caused by the loss of function of the enzyme &#x3b2;-hexosaminidase A (HEXA), it has been reported that the alpha-chain precursor of hexosaminidase is glycosylated normally but not phosphorylated in the Golgi. This indicates that the mutation may prevent the transport of the precursor out of the ER (<xref ref-type="bibr" rid="B23">Barritt et al., 2017</xref>; <xref ref-type="bibr" rid="B174">Ramani and Parayil Sankaran, 2023</xref>). In the case of Fabry disease, a lysosomal storage diseases it is characterized by the deposition of lysosomal glycosphingolipids due to the absence or deficient activity of lysosomal exoglycohydrolase &#x3b1;-galactosidase A (&#x3b1;-D-galactoside galactohydrolase). This leads to the gradual buildup of Gb3 (or GL-3) and related glycosphingolipids within lysosomes across different cell types (<xref ref-type="bibr" rid="B129">Lenders and Brand, 2021</xref>; <xref ref-type="bibr" rid="B48">Cortes-Saladelafont et al., 2023</xref>).</p>
</sec>
</sec>
<sec id="s4">
<title>4 Interplay between the Golgi and lysosomes under physiological and pathological conditions</title>
<p>Due to the dynamic nature of the Golgi and lysosomes within the same endomembrane system, the interplay between the Golgi apparatus and lysosomes is essential for maintaining cellular homeostasis and ensuring proper cellular function. Under physiological conditions, these organelles work in concert to regulate various cellular processes, including protein trafficking, sorting, and degradation. However, disruptions in the Golgi-lysosome axis can occur under pathological conditions, leading to dysregulation of cellular processes and the onset of various diseases. In this section, we explore the dynamic relationship between the Golgi and lysosomes, both in normal cellular physiology and in the context of disease pathology. We discuss how Golgi structure and function alterations impact lysosomal biogenesis, enzyme trafficking, and lysosome-related diseases. Additionally, we discuss the role of Golgi dysfunction in the pathogenesis of neurodegenerative disorders and LSDs, highlighting the interconnectedness of these organelles in health and disease.</p>
<sec id="s4-1">
<title>4.1 The importance of Golgi-dependent mannose 6-phosphate (M6P) pathway in lysosomal enzymes targeting and biogenesis</title>
<p>Lysosomal enzymes, as well as secretory and plasma membrane proteins, undergo cotranslational glycosylation with preformed N-linked oligosaccharides in the ER, typically consisting of three glucose, nine mannose, and two N-acetyl glucosamine residues, attached to specific asparagine residues (<xref ref-type="bibr" rid="B88">Helenius and Aebi, 2001</xref>). Following signal sequence cleavage, the protein mixture is transported to the Golgi apparatus, undergoing additional posttranslational modifications (<xref ref-type="bibr" rid="B202">Stanley, 2011</xref>). Subsequently, these proteins are sorted for targeting to their appropriate destinations, such as lysosomes, secretory granules, and the plasma membrane (<xref ref-type="bibr" rid="B274">Zhang and Wang, 2016</xref>).</p>
<p>In the Golgi apparatus, the path of lysosomal enzymes diverges from that of other glycoproteins. Golgi enzymes process most of the N-linked oligosaccharides on lysosomal enzymes, leading to the acquisition of phosphomannosyl residues (<xref ref-type="bibr" rid="B203">Staudt et al., 2016</xref>). This mannose 6-phosphate (M6P) recognition marker is generated through a two-step reaction catalyzed by two Golgi enzymes. First, UDP-GlcNAc: lysosomal enzyme N-acetylglucosamine-1-phosphate transferase (GNPTAB) transfers N-acetylglucosamine-l-phosphate to selected mannose residues on lysosomal enzymes, forming a phosphodiester intermediate (<xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>). Subsequently, alpha-N-acetylglucosaminidase removes the N-acetylglucosamine, exposing the Man-6-P monoester signal (<xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>; <xref ref-type="bibr" rid="B10">Amaral et al., 2023</xref>). It is worth noting that phosphotransferase can selectively phosphorylate lysosomal enzymes as opposed to non-lysosomal glycoproteins that harbor similar oligosaccharides. This discrimination is achieved by recognizing a protein domain common to nearly all lysosomal enzymes (<xref ref-type="bibr" rid="B140">Luzio et al., 2014</xref>; <xref ref-type="bibr" rid="B10">Amaral et al., 2023</xref>).</p>
<p>After the generation of phosphomannosyl residues, lysosomal enzymes bind with high affinity to mannose 6-phosphate receptors (M6PR) in the Golgi, facilitating their segregation from proteins destined for secretion (<xref ref-type="fig" rid="F2">Figure 2A</xref>) (<xref ref-type="bibr" rid="B49">Coutinho et al., 2012</xref>). Subsequently, the ligand-receptor complex exits the Golgi via clathrin-coated vesicles and enters endosomes (<xref ref-type="bibr" rid="B86">Guo et al., 2014</xref>). Within this compartment, ligand dissociation is prompted by acidification, allowing the receptor to recycle back to the Golgi for subsequent binding with another ligand molecule (<xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>; <xref ref-type="bibr" rid="B10">Amaral et al., 2023</xref>). A recent study employing a genome-wide CRISPR/Cas9 knockout screen revealed that the transmembrane protein 251 (TMEM251) plays a pivotal role in modulating M6P modification. TMEM251, localized in the Golgi apparatus, is indispensable for the cleavage and function of GNPTAB, the enzyme responsible for catalyzing M6P modification. Deletion of TMEM251 results in the mistargeting of most lysosomal enzymes due to the absence of M6P modification, leading to the accumulation of undigested materials (<xref ref-type="bibr" rid="B265">Zhang et al., 2022</xref>; <xref ref-type="bibr" rid="B163">Pechincha et al., 2022</xref>; <xref ref-type="bibr" rid="B179">Richards et al., 2022</xref>). Furthermore, in zebrafish models, TMEM251 deletion induces severe developmental anomalies reminiscent of Mucolipidosis Type II (<xref ref-type="bibr" rid="B265">Zhang et al., 2022</xref>).</p>
<p>While the phosphorylation of lysosomal enzymes with M6P is crucial for targeting numerous enzymes to lysosomes, some mammalian cell types do not phosphorylate lysosomal enzymes. Nevertheless, these enzymes are correctly targeted to lysosomes, suggesting the existence of other unknown mechanisms (<xref ref-type="bibr" rid="B51">Cuozzo and Sahagian, 1994</xref>). For example, the glucocerebrosidase lysosomal enzyme lacks phosphorylation on its oligosaccharide, yet it remains firmly bound to the membrane while targeting the lysosome (<xref ref-type="bibr" rid="B3">Aerts et al., 1988</xref>; <xref ref-type="bibr" rid="B33">Braulke et al., 2023</xref>).</p>
<p>The M6PR has been purified, and its localization has been investigated through EM and other immunological approaches (<xref ref-type="bibr" rid="B90">Hoflack and Kornfeld, 1985</xref>; <xref ref-type="bibr" rid="B166">Pohlmann et al., 1989</xref>). However, the precise localization of the M6PR within the Golgi apparatus was controversial. Brown and Farquhar, using an immunoperoxidase technique coupled with EM, found that receptors are restricted to the <italic>cis</italic> side of the Golgi stacks, supported by the presence of the two enzymes involved in generating phosphomannosyl residues within the Golgi stack (<xref ref-type="bibr" rid="B34">Brown and Farquhar, 1984</xref>). In contrast, Geuze and others, utilizing ultra-thin cryosections and double-label immune-EM with colloidal gold particles of varying sizes, discovered that the M6PR is localized throughout both <italic>cis</italic> and <italic>trans</italic>-Golgi cisternae (<xref ref-type="bibr" rid="B78">Geuze et al., 1984</xref>). This distribution is supported by the co-localization of the lysosomal enzyme cathepsin D with the M6PR in all Golgi cisternae. This suggests that M6PR/cathepsin D complexes move to lysosomes through the entire Golgi complex (<xref ref-type="bibr" rid="B78">Geuze et al., 1984</xref>).</p>
<p>Lysosomal enzymes are synthesized as inactive pro-proteins, and their activation is a tightly regulated process crucial for their proper function within lysosomes. The nascent lysosomal enzymes typically contain a prodomain, which acts as a molecular switch to keep them inactive during synthesis and transport. The prodomain prevents premature enzyme activity and protects other cellular components from potential damage. The prodomain must be selectively removed to render these inactive enzymes fully functional. This maturation process occurs within the acidic environment of the lysosome, where specific proteases, often other lysosomal enzymes, cleave the prodomain, activating the enzyme (<xref ref-type="fig" rid="F2">Figure 2A</xref>). For example, Cathepsin D originates as a 53-kDa polypeptide precursor synthesized in the ER, and it is then transported through the Golgi to reach the lysosome. Once within the lysosome, the precursor is converted into a 47-kDa intermediate form, which is further processed into the 31-kDa mature form. (<xref ref-type="bibr" rid="B79">Gieselmann et al., 1985</xref>; <xref ref-type="bibr" rid="B259">Zaidi et al., 2008</xref>). The precise cleavage of the prodomain is vital for controlling the timing and location of enzyme activation, ensuring that these powerful hydrolytic enzymes become active only within the lysosomal compartment. Dysregulation of this maturation process can lead to lysosomal dysfunction and contribute to the pathogenesis of LSDs. This information is crucial, considering that a proprotein is typically secreted directly from the Golgi, implying that a Golgi defect could potentially impair its sorting and trafficking (<xref ref-type="fig" rid="F2">Figure 2</xref>). Conversely, the secretion of a mature lysosome enzyme usually indicates enhanced lysosome exocytosis (<xref ref-type="fig" rid="F3">Figure 3</xref>).</p>
</sec>
<sec id="s4-2">
<title>4.2 Golgi structural defects affect lysosome biogenesis and function</title>
<p>As discussed above, the Golgi plays a critical role in lysosome biogenesis and function by controlling essential processes such as M6P phosphorylation, sorting, and delivery of enzymes to lysosomes. Furthermore, the proper functioning of the Golgi is vital for the glycosylation, processing, assembly, and trafficking of lysosomal membrane proteins, including Lamp1, Lamp2, lysosomal ion channels, and transporters. Disruption of Golgi structure formation, induced by GRASP depletion, results in the misplacement of lysosomal enzymes, such as cathepsin D, into the extracellular milieu (<xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>; <xref ref-type="bibr" rid="B273">Zhang and Wang, 2015b</xref>). It is noteworthy that only the proform of cathepsin D is secreted upon GRASP depletion, confirming that it is due to a sorting defect at the Golgi (<xref ref-type="fig" rid="F2">Figure 2</xref>), not lysosome exocytosis (<xref ref-type="fig" rid="F3">Figure 3</xref>).</p>
<p>The secretome analysis of WT and GRASP55 knockout (55KO) cells provides valuable insights into the impact of GRASP55 on protein secretion, particularly those associated with lysosomes (<xref ref-type="bibr" rid="B8">Ahat et al., 2019b</xref>). Through Tandem Mass Tag (TMT) labeling and liquid-chromatography mass spectrometry (LC-MS), 1,696 proteins were identified in the conditioned media, and their secretion patterns were compared between 55KO and WT cells. Further exploration of the 445 proteins significantly affected by 55KO highlighted distinct secretion patterns based on the presence or absence of ER signal sequences. Notably, proteins without ER signal sequences were less secreted; whereas proteins with ER signal sequences, including lysosomal enzymes, exhibited increased secretion in 55KO cells (<xref ref-type="bibr" rid="B8">Ahat et al., 2019b</xref>). This suggests a critical role of GRASP55 in the secretion of lysosomal components, impacting lysosomal biogenesis, consistent with the observation that GRASP depletion disrupts the Golgi structure and accelerates protein trafficking and secretion (<xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>). Unlike secretory proteins that follow the conventional ER-Golgi-plasma membrane pathway, cytosolic proteins lacking ER signal sequences utilize an unconventional autophagosome-autolysosome-plasma membrane pathway for transport. GRASP55 has been shown to facilitate autophagosome-lysosome fusion (<xref ref-type="bibr" rid="B276">Zhang and Wang, 2018b</xref>; <xref ref-type="bibr" rid="B271">Zhang et al., 2018</xref>), thereby promoting the secretion of cytoplasmic proteins. Additionally, stress-induced Golgi fragmentation may impair the sorting of lysosomal enzymes. Consequently, lysosomal dysfunction cause by lysosome enzyme missorting could diminish the degradation of cytoplasmic proteins in autolysosomes, potentially leading to their increased secretion (<xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>; <xref ref-type="bibr" rid="B278">Zhang and Wang, 2020b</xref>; <xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>).</p>
<p>Gene Ontology (GO) term analysis highlights the importance of lysosomal enzymes and structural proteins in the GRASP55-dependent secretome. This finding aligns with the concept that Golgi unstacking due to GRASP depletion leads to missorting and elevated secretion of lysosomal enzymes (<xref ref-type="fig" rid="F2">Figure 2B</xref>) (<xref ref-type="bibr" rid="B249">Xiang et al., 2013</xref>). The identified enzymes in this context include Arylsulfatase B (ARSB), Cathepsin A (CTSA), Cathepsin B (CTSB), Cathepsin C (CTSC), Cathepsin D (CTSD), Cathepsin F (CTSF), Cathepsin L (CTSL), Cathepsin S (CTSS), Cathepsin V (CTSV), Cathepsin Z (CTSZ), HEXA, Hexosaminidase B (HEXB), and N-acetylgalactosamine-6-sulfatase (GALNS), among numerous other lysosomal enzymes (<xref ref-type="table" rid="T1">Table 1</xref>) (<xref ref-type="bibr" rid="B8">Ahat et al., 2019b</xref>).</p>
<table-wrap id="T1" position="float">
<label>TABLE 1</label>
<caption>
<p>Lysosomal enzymes with enhanced secretion due to GRASP55 knockout. Associated diseases sourced from GeneCards. Secretion effects represented as fold changes [log2FC(55KO/WT media)] and <italic>p</italic>-values based on prior secretome analysis (<xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>).</p>
</caption>
<table>
<thead valign="top">
<tr>
<th align="left">Gene Symbol</th>
<th align="left">Full Name</th>
<th align="left">Function</th>
<th align="left">Associated disease</th>
<th align="left">log2FC (55KO/WT media)</th>
<th align="left">
<italic>p</italic>-value</th>
</tr>
</thead>
<tbody valign="top">
<tr>
<td align="left">AGA</td>
<td align="left">Aspartylglucosaminidase</td>
<td align="left">Lysosomal breakdown of glycoproteins</td>
<td align="left">Aspartylglucosaminuria and Lysosomal Storage Disease</td>
<td align="left">1.0473</td>
<td align="left">5.11E-03</td>
</tr>
<tr>
<td align="left">ARSA</td>
<td align="left">Arylsulfatase A</td>
<td align="left">Hydrolyzes cerebroside sulfate to cerebroside and sulfate</td>
<td align="left">Metachromatic leucodystrophy (MLD)</td>
<td align="left">1.0813</td>
<td align="left">3.03E-03</td>
</tr>
<tr>
<td align="left">ARSB</td>
<td align="left">Arylsulfatase B</td>
<td align="left">Hydrolyzes sulfate groups of N-Acetyl-D-galactosamine, chondriotin sulfate, and dermatan sulfate</td>
<td align="left">Mucopolysaccharidosis, Type Vi and Mucopolysaccharidosis Type 6, Slowly Progressing</td>
<td align="left">1.2963</td>
<td align="left">5.35E-04</td>
</tr>
<tr>
<td align="left">ARSK</td>
<td align="left">Arylsulfatase Family Member K</td>
<td align="left">hydrolyze sulfate esters from sulfated steroids, carbohydrates, proteoglycans, and glycolipids</td>
<td align="left">Mucopolysaccharidosis, Type X and Mucopolysaccharidosis-Plus Syndrome</td>
<td align="left">0.8600</td>
<td align="left">9.08E-04</td>
</tr>
<tr>
<td align="left">ASAH1</td>
<td align="left">N-Acylsphingosine Amidohydrolase 1</td>
<td align="left">Catalyzes the degradation of ceramide into sphingosine and free fatty acid</td>
<td align="left">Farber Lipogranulomatosis and Spinal Muscular Atrophy With Progressive Myoclonic Epilepsy</td>
<td align="left">0.8230</td>
<td align="left">5.15E-03</td>
</tr>
<tr>
<td align="left">CPQ</td>
<td align="left">Carboxypeptidase Q</td>
<td align="left">Catalyzes the hydrolysis of dipeptides with unsubstituted terminals into amino acids</td>
<td align="left">Episodic Ataxia Type 4</td>
<td align="left">0.6963</td>
<td align="left">6.55E-02</td>
</tr>
<tr>
<td align="left">CTSB</td>
<td align="left">Cathepsin B</td>
<td align="left">Lysosomal cysteine protease with both endopeptidase and exopeptidase activity</td>
<td align="left">Keratolytic Winter Erythema and Annular Erythema</td>
<td align="left">0.9350</td>
<td align="left">4.92E-03</td>
</tr>
<tr>
<td align="left">CTSC</td>
<td align="left">Cathepsin C</td>
<td align="left">Lysosomal cysteine proteinase, activates many serine proteinases in cells of the immune system, degrades glucagon</td>
<td align="left">Papillon-Lefevre Syndrome and Haim-Munk Syndrome</td>
<td align="left">1.0063</td>
<td align="left">2.77E-03</td>
</tr>
<tr>
<td align="left">CTSF</td>
<td align="left">Cathepsin F</td>
<td align="left">A papain family cysteine protease that participates in intracellular degradation and turnover of proteins</td>
<td align="left">Ceroid Lipofuscinosis, Neuronal, 13 and Neuronal Ceroid Lipofuscinosis</td>
<td align="left">0.9113</td>
<td align="left">3.48E-03</td>
</tr>
<tr>
<td align="left">CTSL</td>
<td align="left">Cathepsin L</td>
<td align="left">Lysosomal cysteine proteinase, degrades collagen and elastin, as well as S1 subunit of the SARS-CoV-2 spike protein</td>
<td align="left">Middle East Respiratory Syndrome and COVID-19</td>
<td align="left">0.7843</td>
<td align="left">1.52E-02</td>
</tr>
<tr>
<td align="left">CTSV</td>
<td align="left">Cathepsin V</td>
<td align="left">A lysosomal cysteine proteinase that may play an important role in corneal physiology</td>
<td align="left">Endochondral ossification with skeletal dysplasias</td>
<td align="left">1.2883</td>
<td align="left">2.67E-04</td>
</tr>
<tr>
<td align="left">CTSZ</td>
<td align="left">Cathepsin Z</td>
<td align="left">A lysosomal cysteine proteinase that exhibits both carboxy-monopeptidase and carboxy-dipeptidase activities; expressed in cancer cells</td>
<td align="left">Cercarial Dermatitis and Rosacea</td>
<td align="left">1.0747</td>
<td align="left">3.46E-03</td>
</tr>
<tr>
<td align="left">DNASE2</td>
<td align="left">Deoxyribonuclease 2, Lysosomal</td>
<td align="left">Hydrolyzes DNA under acidic conditions</td>
<td align="left">Autoinflammatory-Pancytopenia Syndrome and Transient Neonatal Thrombocytopenia</td>
<td align="left">1.2037</td>
<td align="left">1.69E-03</td>
</tr>
<tr>
<td align="left">FUCA1</td>
<td align="left">Alpha-L-Fucosidase 1</td>
<td align="left">Lysosomal enzyme involved in the degradation of fucose-containing glycoproteins and glycolipids</td>
<td align="left">Fucosidosis and Nervous System Disease</td>
<td align="left">0.8787</td>
<td align="left">1.44E-02</td>
</tr>
<tr>
<td align="left">FUCA2</td>
<td align="left">Alpha-L-Fucosidase 2</td>
<td align="left">Hydrolyze the alpha-1,6-linked fucose of glycoproteins</td>
<td align="left">Fucosidosis and Skin Hemangioma</td>
<td align="left">1.3780</td>
<td align="left">1.06E-03</td>
</tr>
<tr>
<td align="left">GAA</td>
<td align="left">Alpha Glucosidase</td>
<td align="left">Degrades glycogen to glucose in lysosomes</td>
<td align="left">Glycogen storage disease II, aka Pompe&#x2019;s disease, Glycogen Storage Disease Due To Acid Maltase Deficiency, Late-Onset</td>
<td align="left">1.0637</td>
<td align="left">2.45E-03</td>
</tr>
<tr>
<td align="left">GALNS</td>
<td align="left">N-acetylgalactosamine-6-sulfatase</td>
<td align="left">Hydrolysis of the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of chondroitin sulfate</td>
<td align="left">Mucopolysaccharidosis, Type Iva and Mucopolysaccharidosis Iv</td>
<td align="left">1.2107</td>
<td align="left">2.45E-03</td>
</tr>
<tr>
<td align="left">GGH</td>
<td align="left">Gamma-Glutamyl Hydrolase</td>
<td align="left">Hydrolyzes folylpoly-gamma-glutamates and antifolylpoly-gamma-glutamates</td>
<td align="left">Tropical Sprue and Pulmonary Neuroendocrine Tumor</td>
<td align="left">1.3750</td>
<td align="left">1.23E-03</td>
</tr>
<tr>
<td align="left">GLA</td>
<td align="left">Galactosidase Alpha</td>
<td align="left">Hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins</td>
<td align="left">Fabry Disease and Hypertrophic Cardiomyopathy</td>
<td align="left">0.4927</td>
<td align="left">4.43E-02</td>
</tr>
<tr>
<td align="left">GUSB</td>
<td align="left">Glucuronidase Beta</td>
<td align="left">A lysosomal hydrolase that degrades glycosaminoglycans, including heparan sulfate, dermatan sulfate, and chondroitin-4,6-sulfate</td>
<td align="left">Mucopolysaccharidosis, Type Vii and Mucopolysaccharidosis, Type Vi</td>
<td align="left">1.4460</td>
<td align="left">1.99E-04</td>
</tr>
<tr>
<td align="left">HEXA</td>
<td align="left">Hexosaminidase A</td>
<td align="left">Degradation of GM2 gangliosides in the presence of GM2A</td>
<td align="left">Tay-Sachs Disease</td>
<td align="left">0.6767</td>
<td align="left">3.56E-02</td>
</tr>
<tr>
<td align="left">HEXB</td>
<td align="left">Hexosaminidase B</td>
<td align="left">Degrades ganglioside GM2, and other molecules containing terminal N-acetyl hexosamines</td>
<td align="left">Sandhoff Disease and Gm2 Gangliosidosis</td>
<td align="left">1.3787</td>
<td align="left">6.82E-04</td>
</tr>
<tr>
<td align="left">IDUA</td>
<td align="left">Alpha-L-Iduronidase</td>
<td align="left">Hydrolyzes the terminal alpha-L-iduronic acid residues of two glycosaminoglycans, dermatan sulfate and heparan sulfate</td>
<td align="left">Hurler Syndrome and Scheie Syndrome</td>
<td align="left">0.6527</td>
<td align="left">3.27E-02</td>
</tr>
<tr>
<td align="left">LGMN</td>
<td align="left">Legumain</td>
<td align="left">A cysteine protease that degrades internalized EGFR</td>
<td align="left">Aneruptive Fever and Cerebral Amyloid Angiopathy, Cst3-Related</td>
<td align="left">0.7823</td>
<td align="left">1.68E-02</td>
</tr>
<tr>
<td align="left">MAN2B1</td>
<td align="left">Mannosidase Alpha Class 2B Member 1</td>
<td align="left">Hydrolyzes terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides</td>
<td align="left">Mannosidosis, Alpha B, Lysosomal and Methylmalonic Aciduria Due To Methylmalonyl-Coa Mutase Deficiency</td>
<td align="left">0.4447</td>
<td align="left">8.58E-02</td>
</tr>
<tr>
<td align="left">MAN2B2</td>
<td align="left">Mannosidase Alpha Class 2B Member 2</td>
<td align="left">Involved in mannose metabolic process</td>
<td align="left">Mannosidosis, Beta A, Lysosomal and Mannosidosis, Alpha B, Lysosomal</td>
<td align="left">1.0883</td>
<td align="left">1.98E-03</td>
</tr>
<tr>
<td align="left">MANBA</td>
<td align="left">Mannosidase Beta</td>
<td align="left">A lysosomal glycosyl hydrolase that degrades N-linked oligosaccharide</td>
<td align="left">Mannosidosis, Beta A, Lysosomal and Angiokeratoma</td>
<td align="left">0.9397</td>
<td align="left">6.16E-03</td>
</tr>
<tr>
<td align="left">NAGA</td>
<td align="left">Alpha-N-Acetylgalactosaminidase</td>
<td align="left">A lysosomal enzyme that cleaves alpha-N-acetylgalactosaminyl moieties from glycoconjugates</td>
<td align="left">Kanzaki Disease and Schindler Disease, Type I</td>
<td align="left">1.0667</td>
<td align="left">7.18E-03</td>
</tr>
<tr>
<td align="left">NAGLU</td>
<td align="left">N-Acetyl-Alpha-Glucosaminidase</td>
<td align="left">A lysosomal enzyme that degrades heparan sulfate</td>
<td align="left">Charcot-Marie-Tooth Disease, Axonal, Type 2V and Mucopolysaccharidosis, Type Iiib</td>
<td align="left">0.8983</td>
<td align="left">9.05E-03</td>
</tr>
<tr>
<td align="left">PLA2G15</td>
<td align="left">Phospholipase A2 Group XV</td>
<td align="left">Hydrolyzes lysophosphatidylcholine to glycerophosphorylcholine and a free fatty acid</td>
<td align="left"/>
<td align="left">1.0920</td>
<td align="left">5.25E-04</td>
</tr>
</tbody>
</table>
</table-wrap>
<p>These enzymes are crucial for various cellular processes, and their misplacement can lead to aberrant extracellular activity. For instance, cathepsins are involved in protein degradation, and their uncontrolled release may contribute to aberrant extracellular proteolysis. Hexosaminidases, such as HEXA and HEXB, are essential for the breakdown of glycolipids, and their mislocalization may disrupt normal cellular processes and cause Tay-Sachs disease (<xref ref-type="bibr" rid="B23">Barritt et al., 2017</xref>; <xref ref-type="bibr" rid="B174">Ramani and Parayil Sankaran, 2023</xref>). Additionally, the extracellular presence of lysosomal enzymes could lead to altered interactions with the extracellular matrix and neighboring cells, potentially impacting tissue homeostasis and contributing to pathological conditions (<xref ref-type="bibr" rid="B1">Abbott et al., 2010</xref>; <xref ref-type="bibr" rid="B98">Ibata and Yuzaki, 2021</xref>; <xref ref-type="bibr" rid="B206">Stoka et al., 2023</xref>). This holistic analysis provides novel insights into how GRASP55 and the Golgi structure influence the secretome, shedding light on its role in lysosomal protein trafficking and secretion. Understanding the consequences of the extracellular secretion of these enzymes is crucial for unraveling the broader implications of Golgi defects in lysosomal enzyme trafficking.</p>
</sec>
<sec id="s4-3">
<title>4.3 The role of GRASP55 in autophagosome-lysosome fusion and unconventional secretion</title>
<p>In addition to the function of the Golgi in lysosome biogenesis, the Golgi stacking protein GRASP55 also plays a role in stress-induced autophagy and unconventional secretion (<xref ref-type="bibr" rid="B278">Zhang and Wang, 2020b</xref>). Under conditions of glucose and amino acid starvation, there is a significant increase in the expression levels of the GRASP55 protein (<xref ref-type="bibr" rid="B270">Zhang et al., 2019b</xref>), with a subset of the GRASP55 protein localized to autophagosomes (<xref ref-type="bibr" rid="B271">Zhang et al., 2018</xref>). This process is regulated by O-GlcNAcylation, a form of glycosylation that serves as a marker for glucose levels. Under growth condition, GRASP55 is O-GlcNAcylated by the O-GlcNAc transferase (OGT). Upon glucose starvation, GRASP55 is de-O-GlcNAcylated and targeted to autophagosomes (<xref ref-type="fig" rid="F3">Figure 3</xref>) (<xref ref-type="bibr" rid="B267">Zhang, 2023</xref>).</p>
<p>Interestingly, this autophagosome localization of GRASP55 is accompanied by an enhanced fusion between autophagosomes and lysosomes. This phenomenon was observed through the increased colocalization of LC3 and LAMP2 (<xref ref-type="bibr" rid="B271">Zhang et al., 2018</xref>). Conversely, autophagosome-lysosome fusion was notably reduced in cells where GRASP55 was depleted, as evidenced by a significant decrease in LC3 and LAMP2 colocalization (<xref ref-type="bibr" rid="B271">Zhang et al., 2018</xref>). In contrast, the expression levels of LC3 and the protein Sequestosome one (p62/SQSTM1), classical selective autophagy receptors, were significantly elevated (<xref ref-type="bibr" rid="B271">Zhang et al., 2018</xref>), indicating a reduced autophagic flow.</p>
<p>Mechanistically, GRASP55 interacts with and stimulates the assembly of the Beclin-1-Phosphoinositide 3-kinases (PI3K)-UVRAG complex, which is crucial for the fusion of autophagosomes with lysosomes (<xref ref-type="fig" rid="F3">Figure 3</xref>) (<xref ref-type="bibr" rid="B270">Zhang et al., 2019b</xref>). Subsequent studies demonstrated that adding recombinant GRASP55 into cell lysates increased LC3 and LAMP2 complex formation assessed by co-immunoprecipitation (<xref ref-type="bibr" rid="B271">Zhang et al., 2018</xref>). Like its role in Golgi stacking, GRASP55 oligomers act as membrane tethers, facilitating fusion by physically connecting autophagosomes and lysosomes via interactions with LC3 (autophagosomes) and LAMP2 (late endosomes/lysosomes) (<xref ref-type="fig" rid="F3">Figure 3</xref>) (<xref ref-type="bibr" rid="B276">Zhang and Wang, 2018b</xref>; <xref ref-type="bibr" rid="B275">a</xref>).</p>
<p>Initially, GRASPs were found to be associated with the unconventional secretion of acyl-CoA binding protein (AcbA/Acb1) in <italic>Dictyostelium discoideum</italic> and <italic>Saccharomyces cerevisiae</italic> (<xref ref-type="bibr" rid="B119">Kinseth et al., 2007</xref>; <xref ref-type="bibr" rid="B144">Manjithaya et al., 2010</xref>). Subsequently, cytosolic proteins without ER signal sequences (leaderless proteins), such as the cytokine interleukin one beta (IL-1&#x3b2;) (<xref ref-type="bibr" rid="B45">Chiritoiu et al., 2019</xref>), growth factors including fibroblast growth factor 2 (FGF2), as well as some integral membrane proteins (<xref ref-type="bibr" rid="B119">Kinseth et al., 2007</xref>; <xref ref-type="bibr" rid="B77">Gee et al., 2011</xref>), were all found to be secreted in a Golgi-independent but GRASP-dependent manner (<xref ref-type="bibr" rid="B278">Zhang and Wang, 2020b</xref>). In <italic>Drosophila</italic>, the singular GRASP protein was found to be involved in the unconventional trafficking of &#x3b1;-integrin during specific stages of fly development (<xref ref-type="bibr" rid="B189">Schotman et al., 2008</xref>). In <italic>Drosophila</italic> adult fat body cells Unpaired 2 (Upd2), analogous to the primary human adipokine leptin, is also secreted through GRASP unconventional secretion pathway (<xref ref-type="bibr" rid="B172">Rajan et al., 2017</xref>).</p>
<p>Interestingly, a recent study has shown that GRASP55 is a direct substrate of mTORC1. When mTOR1 is active, it phosphorylates GRASP55 proteins at the Golgi cisternae, where they maintain their cellular localization. Conversely, reduced mTORC1 activity, due to various stresses or inhibitors, results in GRASP55 dephosphorylation, prompting its relocation from the Golgi to autophagosomes and multivesicular bodies (MVBs), leading to the stimulation of unconventional secretion of proteins. This suggests that the mTORC1-GRASP55 signaling axis plays an essential role in controlling the section of extracellular proteome (<xref ref-type="bibr" rid="B156">Nuchel et al., 2021</xref>).</p>
<p>Recent studies demonstrated that more cytosolic proteins, including neurodegenerative proteopathic proteins &#x3b1;-synuclein, TDP-43, SOD1, and tau (<xref ref-type="bibr" rid="B61">El-Agnaf et al., 2003</xref>; <xref ref-type="bibr" rid="B126">Lee et al., 2005</xref>; <xref ref-type="bibr" rid="B62">El-Agnaf et al., 2006</xref>; <xref ref-type="bibr" rid="B83">Gomes et al., 2007</xref>; <xref ref-type="bibr" rid="B63">Emmanouilidou et al., 2010</xref>; <xref ref-type="bibr" rid="B9">Alvarez-Erviti et al., 2011</xref>; <xref ref-type="bibr" rid="B85">Grey et al., 2015</xref>; <xref ref-type="bibr" rid="B99">Iguchi et al., 2016</xref>; <xref ref-type="bibr" rid="B50">Cruz-Garcia et al., 2017</xref>; <xref ref-type="bibr" rid="B134">Liu et al., 2017</xref>; <xref ref-type="bibr" rid="B184">Ruan and Ikezu, 2019</xref>), can be secreted. Studies utilizing mutant huntingtin (mHtt) as a model protein have revealed the potential mechanism for cytoplasmic proteolytic proteins to be secreted through a Golgi-independent, autophagy-dependent, and stress-induced unconventional protein secretion pathway (<xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>). GRASP55 regulates the secretion and aggregation of mHtt by controlling this pathway (<xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>). This process involves transporting cargo proteins from the cytosol to autophagosomes and, ultimately, to the extracellular space (<xref ref-type="fig" rid="F3">Figure 3</xref>) (<xref ref-type="bibr" rid="B278">Zhang and Wang, 2020b</xref>). Healthy cells can internalize these secreted proteopathic proteins, leading to the spread of disease proteins between cells, resulting in cell death (<xref ref-type="bibr" rid="B209">Sung et al., 2001</xref>; <xref ref-type="bibr" rid="B139">Luk et al., 2009</xref>; <xref ref-type="bibr" rid="B184">Ruan and Ikezu, 2019</xref>; <xref ref-type="bibr" rid="B108">Jo et al., 2020</xref>).</p>
<p>The secretome analysis comparing WT and 55KO cells has identified new candidates involved in GRASP55-dependent unconventional secretion (<xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>). Among the 445 proteins affected significantly by 55KO, 196 (71%) of the 276 proteins lacking ER signal sequences showed decreased secretion in 55KO, underscoring the significance of GRASP55 in unconventional protein secretion. Gene Ontology analysis revealed numerous pathways affected by 55KO, including lysosomal enzymes, extracellular matrix organization, glycosaminoglycan metabolism, and stress response, thereby reinforcing the connection between GRASP55, lysosomal function, and stress response (<xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>).</p>
<p>Moreover, the secretome analysis has confirmed the secretion of proteins lacking ER signal sequences through a GRASP55-dependent mechanism. Studies of specific candidates such as transgelin 1 (TAGLN), multifunctional protein ADE2 (PAICS), and peroxiredoxin-1 (PRDX1) have demonstrated their secretion dependency on GRASP55 (<xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>). Furthermore, these studies have underscored the vital roles played by GRASP55 in unconventional protein secretion, providing insights into its effects on cellular processes and emphasizing its connection to lysosomal function and stress response. Despite the identification of numerous substrates in GRASP55-dependent unconventional secretion, a direct interaction between GRASP55 and cargo molecules has not been documented. The mechanisms through which GRASP55 detects cellular stresses, recruits cytosolic proteins, and facilitates their extracellular release remain largely unresolved questions.</p>
</sec>
<sec id="s4-4">
<title>4.4 Non-classical LSDs, neurodegenerative disorders, and their association with Golgi defects</title>
<p>While classical LSDs are usually associated with inherited mutations in lysosomal enzymes, non-classical LSDs may involve abnormalities in lysosomal function, lysosomal membrane proteins, or other processes related to lysosomal biology. Non-classical LSDs often present with a broad spectrum of symptoms and may not follow the well-defined patterns seen in classical cases. These disorders may result from genetic mutations affecting various aspects of lysosomal physiology, such as lysosomal membrane stability, membrane transporters, or regulatory proteins (<xref ref-type="bibr" rid="B68">Ferreira and Gahl, 2017</xref>; <xref ref-type="bibr" rid="B165">Platt et al., 2018</xref>). These so called non-classical LSDs represent a diverse group of disorders characterized by the abnormal accumulation of substances within lysosomes, leading to cellular dysfunction (<xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>; <xref ref-type="bibr" rid="B29">Bonam et al., 2019</xref>). The atypical nature of non-classical LSDs poses challenges in their diagnosis and classification, as they may exhibit overlapping features with other metabolic or neurodegenerative disorders (<xref ref-type="bibr" rid="B142">Machtel et al., 2023</xref>).</p>
<p>An intriguing connection has been observed between some non-classical LSDs and Golgi defects. These disorders often involve disruptions in cellular trafficking and sorting mechanisms, impacting the proper functioning of the Golgi apparatus (<xref ref-type="bibr" rid="B180">Robenek and Schmitz, 1991</xref>; <xref ref-type="bibr" rid="B17">Bajaj et al., 2019</xref>). Due to its pivotal role in protein modification, sorting, and transport, any compromise in Golgi function can result in abnormalities in the processing and trafficking of lysosomal enzymes (<xref ref-type="fig" rid="F3">Figure 3</xref>) (<xref ref-type="bibr" rid="B173">Rajkumar and Dumpa, 2023</xref>).</p>
<p>One example of non-classical LSDs associated with trafficking defects within the Golgi is sialic acid storage diseases, such as Salla disease and infantile sialic acid storage disease (ISSD) (<xref ref-type="bibr" rid="B68">Ferreira and Gahl, 2017</xref>). These disorders are characterized by the accumulation of sialic acid in lysosomes, leading to neurodevelopmental abnormalities. Studies have shown that mutations in the SLC17A5 gene, which encodes sialin, a lysosomal sialic acid transporter, result in the trapping of these proteins in the Golgi, preventing their delivery to lysosomes (<xref ref-type="bibr" rid="B15">Aula et al., 2002</xref>). This disruption in SLC17A5 trafficking contributes to the lysosomal storage phenotype observed in these diseases.</p>
<p>Although neurodegenerative diseases are generally not considered classical LSDs, many of them are characterized by protein aggregations and lysosomal dysfunction (<xref ref-type="bibr" rid="B54">Darios and Stevanin, 2020</xref>; <xref ref-type="bibr" rid="B182">Root et al., 2021</xref>; <xref ref-type="bibr" rid="B228">Udayar et al., 2022</xref>). In AD, intracellular NFTs formed by hyperphosphorylated tau are strongly linked to neuronal loss and cognitive decline (<xref ref-type="bibr" rid="B229">Umeda et al., 2014</xref>). In Parkinson&#x2019;s disease (PD) and Lewy body dementia (DLB), &#x3b1;-synuclein forms aggregates known as Lewy bodies (<xref ref-type="bibr" rid="B204">Stefanis, 2012</xref>). In ALS and frontotemporal dementia (FTD), TDP-43 protein undergoes abnormal cellular localization and aggregation in the nucleus and cytoplasm (<xref ref-type="bibr" rid="B183">Ross and Poirier, 2004</xref>; <xref ref-type="bibr" rid="B110">Johnson et al., 2009</xref>; <xref ref-type="bibr" rid="B227">Udan-Johns et al., 2014</xref>; <xref ref-type="bibr" rid="B102">Ishii et al., 2017</xref>). The aggregation of these proteopathic proteins disrupts normal cellular processes, including protein homeostasis, intracellular signaling, and neuronal function, ultimately leading to neuronal cell death. As discussed above, all these aggregative proteins are released by GRASP55-dependent unconventional secretion.</p>
<p>Neurons maintain high basal autophagy for survival (<xref ref-type="bibr" rid="B66">Feng et al., 2014</xref>; <xref ref-type="bibr" rid="B76">Galluzzi et al., 2014</xref>; <xref ref-type="bibr" rid="B253">Yin et al., 2016</xref>). Autophagy-lysosome defects occur in early AD pathogenesis (<xref ref-type="bibr" rid="B152">Nixon et al., 2005</xref>; <xref ref-type="bibr" rid="B130">Levine and Kroemer, 2008</xref>) and likely contribute to the formation of amyloid plaques and NFTs (<xref ref-type="bibr" rid="B28">Boland et al., 2008</xref>). The A&#x3b2; peptide is produced during the autophagic turnover of organelles rich in APP, supplied by autophagy and endocytosis (<xref ref-type="bibr" rid="B150">Nilsson et al., 2013</xref>). In CA1 pyramidal hippocampus neurons from subjects with early and late-stage AD, there is a notable increase in autophagosome formation and a progressive impairment in autophagy flux (<xref ref-type="bibr" rid="B151">Nixon, 2007</xref>). The combination of increased autophagosome formation and defective clearance of A&#x3b2;-generating autophagic vacuoles creates conditions favorable for A&#x3b2; accumulation in AD (<xref ref-type="bibr" rid="B151">Nixon, 2007</xref>). The sustained activation of autophagy amid declining lysosomal clearance accounts for the unusually robust autophagic pathology implicated in AD pathogenesis (<xref ref-type="bibr" rid="B31">Bordi et al., 2016</xref>; <xref ref-type="bibr" rid="B128">Leeman et al., 2018</xref>).</p>
<p>AD is frequently associated with type 2 diabetes mellitus (T2DM) and decreased brain O-GlcNAc levels (<xref ref-type="bibr" rid="B70">Franco and Bronson, 2005</xref>; <xref ref-type="bibr" rid="B2">Accardi et al., 2012</xref>; <xref ref-type="bibr" rid="B176">Rasool et al., 2014</xref>; <xref ref-type="bibr" rid="B14">Arnold et al., 2018</xref>); Inhibition of O-GlcNAcase (OGA) has been shown to reduce tau aggregation and A&#x3b2; production (<xref ref-type="bibr" rid="B257">Yuzwa et al., 2012</xref>; <xref ref-type="bibr" rid="B117">Kim et al., 2013</xref>; <xref ref-type="bibr" rid="B255">Yuzwa et al., 2014a</xref>; <xref ref-type="bibr" rid="B256">Yuzwa et al., 2014b</xref>). O-GlcNAcylation is considered an energy-sensing mechanism and part of a protective stress response (<xref ref-type="bibr" rid="B258">Zachara et al., 2004</xref>; <xref ref-type="bibr" rid="B262">Zeidan and Hart, 2010</xref>; <xref ref-type="bibr" rid="B30">Bond and Hanover, 2015</xref>). Furthermore, studies have indicated that de-O-GlcNAcylated GRASP55 facilitates autophagosome maturation (<xref ref-type="bibr" rid="B271">Zhang et al., 2018</xref>) and secretion of mHtt (<xref ref-type="bibr" rid="B5">Ahat et al., 2022a</xref>), suggesting an important role for GRASP55 and its O-GlcNAcylation in neurodegeneration (<xref ref-type="fig" rid="F3">Figure 3</xref>). The interplay between Golgi fragmentation, APP processing, A&#x3b2; production, lysosomal dysfunction, and GRASP55-mediated unconventional tau secretion represents a significant area for future investigation (<xref ref-type="bibr" rid="B264">Zhang and Wang, 2024</xref>).</p>
<p>While the connection between Golgi defects and LSDs has not been extensively studied, Golgi defects are more commonly associated with certain neurodegenerative disorders and conditions affecting cellular trafficking rather than classical or non-classical LSDs. The Golgi is abnormally fragmented in AD, PD, and ALS (<xref ref-type="bibr" rid="B13">Aridor and Balch, 1999</xref>; <xref ref-type="bibr" rid="B146">Mizuno et al., 2001</xref>; <xref ref-type="bibr" rid="B74">Fujita et al., 2002</xref>; <xref ref-type="bibr" rid="B73">Fujita and Okamoto, 2005</xref>; <xref ref-type="bibr" rid="B112">Joshi et al., 2014</xref>; <xref ref-type="bibr" rid="B229">Umeda et al., 2014</xref>; <xref ref-type="bibr" rid="B64">Evin, 2015</xref>; <xref ref-type="bibr" rid="B111">Joshi et al., 2015</xref>; <xref ref-type="bibr" rid="B113">Joshi and Wang, 2015</xref>), whereas disturbances in lysosomal function contribute to synaptic and cognitive decline (<xref ref-type="bibr" rid="B97">Hwang et al., 2019</xref>). This suggests impaired Golgi apparatus function may lead to lysosomal dysfunction, resulting in neurodegeneration (<xref ref-type="fig" rid="F3">Figure 3</xref>). Understanding the link between lysosomal dysfunction and Golgi defects provides valuable insights into the underlying cellular mechanisms of these disorders. Targeting the Golgi-related pathways may offer potential therapeutic strategies for managing non-classical LSDs or neurodegenerative disease by addressing the aberrant lysosomal enzyme trafficking and sorting associated with Golgi dysfunction. Further research into the molecular basis of these connections holds promise for developing targeted interventions to alleviate the symptoms and progression of non-classical LSDs, neurodegenerative disorders, and other proteopathies.</p>
</sec>
</sec>
<sec id="s5">
<title>5 Conclusion and perspectives</title>
<p>In conclusion, this review underscores the pivotal role of the Golgi apparatus in orchestrating lysosome biogenesis and maintaining cellular homeostasis through the precise delivery of lysosomal enzymes. Our focused examination of Golgi Reassembly Stacking Proteins (GRASPs) provides key insights into their impact on Golgi apparatus formation and function, elucidating their critical role in maintaining lysosomal homeostasis. The intricate association between Golgi structure, lysosomes, and the onset of LSDs and neurodegenerative disorders emphasizes the importance of understanding Golgi-related pathways. Notably, neurodegenerative disorders, including Alzheimer&#x2019;s and Huntington&#x2019;s, serve as illustrative examples, highlighting the profound consequences of Golgi dysfunction on crucial cellular processes such as protein aggregation and lysosomal dysfunction.</p>
<p>Moreover, the identification of aggregative proteins, secreted through GRASP55-dependent unconventional secretion, sheds light on novel pathways and mechanisms underlying these complex disorders. The interplay between Golgi fragmentation, APP processing, A&#x3b2; production, lysosomal dysfunction, and GRASP55-mediated unconventional secretion of tau represents a promising avenue for future research.</p>
<p>Furthermore, the exploration of Golgi dysfunction-induced secretion of lysosomal enzymes adds a new layer of complexity to the cellular processes involved in disease pathogenesis. This review aims to serve as a concise yet comprehensive resource, offering insights into Golgi structure, function, and the implications of disease-related defects. By highlighting Golgi defects as an often-underappreciated contributor to lysosomal dysfunction across various diseases, we seek to enhance comprehension of the intricate interplay between these cellular components.</p>
<p>As we continue to unravel the molecular intricacies of Golgi-related pathways, potential therapeutic strategies for managing LSDs and neurodegenerative conditions may emerge, providing new avenues for targeted interventions to mitigate the impact of these complex disorders. Understanding the nexus between lysosomal dysfunction and Golgi defects provides valuable insights into the cellular mechanisms of these disorders. Targeting Golgi-related pathways emerges as a potential therapeutic strategy for managing non-classical LSDs and neurodegenerative conditions. As research progresses, unraveling the molecular basis of these connections holds promise for developing targeted interventions to alleviate symptoms and impede the progression of these intricate diseases.</p>
</sec>
</body>
<back>
<sec id="s6">
<title>Author contributions</title>
<p>SA: Conceptualization, Data curation, Writing&#x2013;original draft, Writing&#x2013;review and editing, Validation. YW: Conceptualization, Data curation, Writing&#x2013;original draft, Writing&#x2013;review and editing, Funding acquisition.</p>
</sec>
<sec sec-type="funding-information" id="s7">
<title>Funding</title>
<p>The author(s) declare that financial support was received for the research, authorship, and/or publication of this article. This work is supported by National Institutes of Health (Grant R35GM130331) to YW. SA is an undergraduate at the University of Michigan whose research is supported by National Institutes of Health (Grant 3R35GM130331-05S1). This review is part of her honors thesis.</p>
</sec>
<ack>
<p>We thank Dr. Jianchao Zhang for help with the figures and members of the YW lab for suggestions and stimulative discussion.</p>
</ack>
<sec sec-type="COI-statement" id="s8">
<title>Conflict of interest</title>
<p>The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.</p>
<p>The author(s) declared that they were an editorial board member of Frontiers, at the time of submission. This had no impact on the peer review process and the final decision.</p>
</sec>
<sec sec-type="disclaimer" id="s9">
<title>Publisher&#x2019;s note</title>
<p>All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article, or claim that may be made by its manufacturer, is not guaranteed or endorsed by the publisher.</p>
</sec>
<ref-list>
<title>References</title>
<ref id="B1">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Abbott</surname>
<given-names>D. E.</given-names>
</name>
<name>
<surname>Margaryan</surname>
<given-names>N. V.</given-names>
</name>
<name>
<surname>Jeruss</surname>
<given-names>J. S.</given-names>
</name>
<name>
<surname>Khan</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Kaklamani</surname>
<given-names>V.</given-names>
</name>
<name>
<surname>Winchester</surname>
<given-names>D. J.</given-names>
</name>
<etal/>
</person-group> (<year>2010</year>). <article-title>Reevaluating cathepsin D as a biomarker for breast cancer: serum activity levels versus histopathology</article-title>. <source>Cancer Biol. Ther.</source> <volume>9</volume>, <fpage>23</fpage>&#x2013;<lpage>30</lpage>. <pub-id pub-id-type="doi">10.4161/cbt.9.1.10378</pub-id>
</citation>
</ref>
<ref id="B2">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Accardi</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Caruso</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Colonna-Romano</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Camarda</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Monastero</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Candore</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2012</year>). <article-title>Can Alzheimer disease be a form of type 3 diabetes?</article-title> <source>Rejuvenation Res.</source> <volume>15</volume>, <fpage>217</fpage>&#x2013;<lpage>221</lpage>. <pub-id pub-id-type="doi">10.1089/rej.2011.1289</pub-id>
</citation>
</ref>
<ref id="B3">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Aerts</surname>
<given-names>J. M.</given-names>
</name>
<name>
<surname>Schram</surname>
<given-names>A. W.</given-names>
</name>
<name>
<surname>Strijland</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Van Weely</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Jonsson</surname>
<given-names>L. M.</given-names>
</name>
<name>
<surname>Tager</surname>
<given-names>J. M.</given-names>
</name>
<etal/>
</person-group> (<year>1988</year>). <article-title>Glucocerebrosidase, a lysosomal enzyme that does not undergo oligosaccharide phosphorylation</article-title>. <source>Biochim. Biophys. Acta</source> <volume>964</volume>, <fpage>303</fpage>&#x2013;<lpage>308</lpage>. <pub-id pub-id-type="doi">10.1016/0304-4165(88)90030-x</pub-id>
</citation>
</ref>
<ref id="B4">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Agliarulo</surname>
<given-names>I.</given-names>
</name>
<name>
<surname>Parashuraman</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>2022</year>). <article-title>Golgi apparatus regulates plasma membrane composition and function</article-title>. <source>Cells</source> <volume>11</volume>, <fpage>368</fpage>. <pub-id pub-id-type="doi">10.3390/cells11030368</pub-id>
</citation>
</ref>
<ref id="B5">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ahat</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Bui</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Da Veiga Leprevost</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Sharkey</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Reid</surname>
<given-names>W.</given-names>
</name>
<etal/>
</person-group> (<year>2022a</year>). <article-title>GRASP55 regulates the unconventional secretion and aggregation of mutant huntingtin</article-title>. <source>J. Biol. Chem.</source> <volume>298</volume>, <fpage>102219</fpage>. <pub-id pub-id-type="doi">10.1016/j.jbc.2022.102219</pub-id>
</citation>
</ref>
<ref id="B6">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ahat</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2019a</year>). <article-title>New insights into the golgi stacking proteins</article-title>. <source>Front. Cell Dev. Biol.</source> <volume>7</volume>, <fpage>131</fpage>. <pub-id pub-id-type="doi">10.3389/fcell.2019.00131</pub-id>
</citation>
</ref>
<ref id="B7">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ahat</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Song</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Xia</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Reid</surname>
<given-names>W.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Bui</surname>
<given-names>S.</given-names>
</name>
<etal/>
</person-group> (<year>2022b</year>). <article-title>GRASP depletion-mediated Golgi fragmentation impairs glycosaminoglycan synthesis, sulfation, and secretion</article-title>. <source>Cell Mol. Life Sci.</source> <volume>79</volume>, <fpage>199</fpage>. <pub-id pub-id-type="doi">10.1007/s00018-022-04223-3</pub-id>
</citation>
</ref>
<ref id="B8">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ahat</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Xiang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Bekier</surname>
<given-names>M. E.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2019b</year>). <article-title>GRASP depletion-mediated Golgi destruction decreases cell adhesion and migration via the reduction of &#x3b1;5&#x3b2;1 integrin</article-title>. <source>Mol. Biol. Cell</source> <volume>30</volume>, <fpage>766</fpage>&#x2013;<lpage>777</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.E18-07-0462</pub-id>
</citation>
</ref>
<ref id="B9">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Alvarez-Erviti</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Seow</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Schapira</surname>
<given-names>A. H.</given-names>
</name>
<name>
<surname>Gardiner</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Sargent</surname>
<given-names>I. L.</given-names>
</name>
<name>
<surname>Wood</surname>
<given-names>M. J.</given-names>
</name>
<etal/>
</person-group> (<year>2011</year>). <article-title>Lysosomal dysfunction increases exosome-mediated alpha-synuclein release and transmission</article-title>. <source>Neurobiol. Dis.</source> <volume>42</volume>, <fpage>360</fpage>&#x2013;<lpage>367</lpage>. <pub-id pub-id-type="doi">10.1016/j.nbd.2011.01.029</pub-id>
</citation>
</ref>
<ref id="B10">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Amaral</surname>
<given-names>O.</given-names>
</name>
<name>
<surname>Martins</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Oliveira</surname>
<given-names>A. R.</given-names>
</name>
<name>
<surname>Duarte</surname>
<given-names>A. J.</given-names>
</name>
<name>
<surname>Mondragao-Rodrigues</surname>
<given-names>I.</given-names>
</name>
<name>
<surname>Macedo</surname>
<given-names>M. F.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>The biology of lysosomes: from order to disorder</article-title>. <source>Biomedicines</source> <volume>11</volume>, <fpage>213</fpage>. <pub-id pub-id-type="doi">10.3390/biomedicines11010213</pub-id>
</citation>
</ref>
<ref id="B11">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Angelini</surname>
<given-names>M. M.</given-names>
</name>
<name>
<surname>Akhlaghpour</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Neuman</surname>
<given-names>B. W.</given-names>
</name>
<name>
<surname>Buchmeier</surname>
<given-names>M. J.</given-names>
</name>
</person-group> (<year>2013</year>). <article-title>Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 induce double-membrane vesicles</article-title>. <source>mBio</source> <volume>4</volume>, <fpage>e00524</fpage>. <pub-id pub-id-type="doi">10.1128/mBio.00524-13</pub-id>
</citation>
</ref>
<ref id="B12">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Arad</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Maron</surname>
<given-names>B. J.</given-names>
</name>
<name>
<surname>Gorham</surname>
<given-names>J. M.</given-names>
</name>
<name>
<surname>Johnson</surname>
<given-names>W. H.</given-names>
<suffix>Jr.</suffix>
</name>
<name>
<surname>Saul</surname>
<given-names>J. P.</given-names>
</name>
<name>
<surname>Perez-Atayde</surname>
<given-names>A. R.</given-names>
</name>
<etal/>
</person-group> (<year>2005</year>). <article-title>Glycogen storage diseases presenting as hypertrophic cardiomyopathy</article-title>. <source>N. Engl. J. Med.</source> <volume>352</volume>, <fpage>362</fpage>&#x2013;<lpage>372</lpage>. <pub-id pub-id-type="doi">10.1056/NEJMoa033349</pub-id>
</citation>
</ref>
<ref id="B13">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Aridor</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Balch</surname>
<given-names>W. E.</given-names>
</name>
</person-group> (<year>1999</year>). <article-title>Integration of endoplasmic reticulum signaling in health and disease</article-title>. <source>Nat. Med.</source> <volume>5</volume>, <fpage>745</fpage>&#x2013;<lpage>751</lpage>. <pub-id pub-id-type="doi">10.1038/10466</pub-id>
</citation>
</ref>
<ref id="B14">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Arnold</surname>
<given-names>S. E.</given-names>
</name>
<name>
<surname>Arvanitakis</surname>
<given-names>Z.</given-names>
</name>
<name>
<surname>Macauley-Rambach</surname>
<given-names>S. L.</given-names>
</name>
<name>
<surname>Koenig</surname>
<given-names>A. M.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>H. Y.</given-names>
</name>
<name>
<surname>Ahima</surname>
<given-names>R. S.</given-names>
</name>
<etal/>
</person-group> (<year>2018</year>). <article-title>Brain insulin resistance in type 2 diabetes and Alzheimer disease: concepts and conundrums</article-title>. <source>Nat. Rev. Neurol.</source> <volume>14</volume>, <fpage>168</fpage>&#x2013;<lpage>181</lpage>. <pub-id pub-id-type="doi">10.1038/nrneurol.2017.185</pub-id>
</citation>
</ref>
<ref id="B15">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Aula</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Jalanko</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Aula</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Peltonen</surname>
<given-names>L.</given-names>
</name>
</person-group> (<year>2002</year>). <article-title>Unraveling the molecular pathogenesis of free sialic acid storage disorders: altered targeting of mutant sialin</article-title>. <source>Mol. Genet. Metab.</source> <volume>77</volume>, <fpage>99</fpage>&#x2013;<lpage>107</lpage>. <pub-id pub-id-type="doi">10.1016/s1096-7192(02)00124-5</pub-id>
</citation>
</ref>
<ref id="B16">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ayala</surname>
<given-names>I.</given-names>
</name>
<name>
<surname>Colanzi</surname>
<given-names>A.</given-names>
</name>
</person-group> (<year>2017</year>). <article-title>Alterations of Golgi organization in Alzheimer&#x27;s disease: a cause or a consequence?</article-title> <source>Tissue Cell</source> <volume>49</volume>, <fpage>133</fpage>&#x2013;<lpage>140</lpage>. <pub-id pub-id-type="doi">10.1016/j.tice.2016.11.007</pub-id>
</citation>
</ref>
<ref id="B17">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bajaj</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Lotfi</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Pal</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Ronza</surname>
<given-names>A. D.</given-names>
</name>
<name>
<surname>Sharma</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Sardiello</surname>
<given-names>M.</given-names>
</name>
</person-group> (<year>2019</year>). <article-title>Lysosome biogenesis in health and disease</article-title>. <source>J. Neurochem.</source> <volume>148</volume>, <fpage>573</fpage>&#x2013;<lpage>589</lpage>. <pub-id pub-id-type="doi">10.1111/jnc.14564</pub-id>
</citation>
</ref>
<ref id="B18">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Baloyannis</surname>
<given-names>S. J.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>Golgi apparatus and protein trafficking in Alzheimer&#x27;s disease</article-title>. <source>J. Alzheimers Dis.</source> <volume>42</volume> (<issue>Suppl. 3</issue>), <fpage>S153</fpage>&#x2013;<lpage>S162</lpage>. <pub-id pub-id-type="doi">10.3233/JAD-132660</pub-id>
</citation>
</ref>
<ref id="B19">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bankaitis</surname>
<given-names>V. A.</given-names>
</name>
<name>
<surname>Garcia-Mata</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Mousley</surname>
<given-names>C. J.</given-names>
</name>
</person-group> (<year>2012</year>). <article-title>Golgi membrane dynamics and lipid metabolism</article-title>. <source>Curr. Biol.</source> <volume>22</volume>, <fpage>R414</fpage>&#x2013;<lpage>R424</lpage>. <pub-id pub-id-type="doi">10.1016/j.cub.2012.03.004</pub-id>
</citation>
</ref>
<ref id="B20">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Barbagallo</surname>
<given-names>A. P.</given-names>
</name>
<name>
<surname>Weldon</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Tamayev</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Zhou</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Giliberto</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Foreman</surname>
<given-names>O.</given-names>
</name>
<etal/>
</person-group> (<year>2010</year>). <article-title>Tyr(682) in the intracellular domain of APP regulates amyloidogenic APP processing <italic>in vivo</italic>
</article-title>. <source>PLoS One</source> <volume>5</volume>, <fpage>e15503</fpage>. <pub-id pub-id-type="doi">10.1371/journal.pone.0015503</pub-id>
</citation>
</ref>
<ref id="B21">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Barlowe</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Orci</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Yeung</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Hosobuchi</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Hamamoto</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Salama</surname>
<given-names>N.</given-names>
</name>
<etal/>
</person-group> (<year>1994</year>). <article-title>COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum</article-title>. <source>Cell</source> <volume>77</volume>, <fpage>895</fpage>&#x2013;<lpage>907</lpage>. <pub-id pub-id-type="doi">10.1016/0092-8674(94)90138-4</pub-id>
</citation>
</ref>
<ref id="B22">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Barr</surname>
<given-names>F. A.</given-names>
</name>
<name>
<surname>Puype</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Vandekerckhove</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Warren</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>1997</year>). <article-title>GRASP65, a protein involved in the stacking of Golgi cisternae</article-title>. <source>Cell</source> <volume>91</volume>, <fpage>253</fpage>&#x2013;<lpage>262</lpage>. <pub-id pub-id-type="doi">10.1016/s0092-8674(00)80407-9</pub-id>
</citation>
</ref>
<ref id="B23">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Barritt</surname>
<given-names>A. W.</given-names>
</name>
<name>
<surname>Anderson</surname>
<given-names>S. J.</given-names>
</name>
<name>
<surname>Leigh</surname>
<given-names>P. N.</given-names>
</name>
<name>
<surname>Ridha</surname>
<given-names>B. H.</given-names>
</name>
</person-group> (<year>2017</year>). <article-title>Late-onset tay-sachs disease</article-title>. <source>Pract. Neurol.</source> <volume>17</volume>, <fpage>396</fpage>&#x2013;<lpage>399</lpage>. <pub-id pub-id-type="doi">10.1136/practneurol-2017-001665</pub-id>
</citation>
</ref>
<ref id="B24">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bauerfeind</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Huttner</surname>
<given-names>W. B.</given-names>
</name>
</person-group> (<year>1993</year>). <article-title>Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles</article-title>. <source>Curr. Opin. Cell Biol.</source> <volume>5</volume>, <fpage>628</fpage>&#x2013;<lpage>635</lpage>. <pub-id pub-id-type="doi">10.1016/0955-0674(93)90132-a</pub-id>
</citation>
</ref>
<ref id="B25">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bekier</surname>
<given-names>M. E.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Huang</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<etal/>
</person-group> (<year>2017</year>). <article-title>Knockout of the Golgi stacking proteins GRASP55 and GRASP65 impairs Golgi structure and function</article-title>. <source>Mol. Biol. Cell</source> <volume>28</volume>, <fpage>2833</fpage>&#x2013;<lpage>2842</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.E17-02-0112</pub-id>
</citation>
</ref>
<ref id="B26">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bisel</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Wei</surname>
<given-names>J. H.</given-names>
</name>
<name>
<surname>Xiang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Miron-Mendoza</surname>
<given-names>M.</given-names>
</name>
<etal/>
</person-group> (<year>2008</year>). <article-title>ERK regulates Golgi and centrosome orientation towards the leading edge through GRASP65</article-title>. <source>J. Cell Biol.</source> <volume>182</volume>, <fpage>837</fpage>&#x2013;<lpage>843</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.200805045</pub-id>
</citation>
</ref>
<ref id="B27">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bizzaro</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Pasini</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Ghirardello</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Finco</surname>
<given-names>B.</given-names>
</name>
</person-group> (<year>1999</year>). <article-title>High anti-golgi autoantibody levels: an early sign of autoimmune disease?</article-title> <source>Clin. Rheumatol.</source> <volume>18</volume>, <fpage>346</fpage>&#x2013;<lpage>348</lpage>. <pub-id pub-id-type="doi">10.1007/s100670050115</pub-id>
</citation>
</ref>
<ref id="B28">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Boland</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Kumar</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Lee</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Platt</surname>
<given-names>F. M.</given-names>
</name>
<name>
<surname>Wegiel</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Yu</surname>
<given-names>W. H.</given-names>
</name>
<etal/>
</person-group> (<year>2008</year>). <article-title>Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer&#x27;s disease</article-title>. <source>J. Neurosci.</source> <volume>28</volume>, <fpage>6926</fpage>&#x2013;<lpage>6937</lpage>. <pub-id pub-id-type="doi">10.1523/JNEUROSCI.0800-08.2008</pub-id>
</citation>
</ref>
<ref id="B29">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bonam</surname>
<given-names>S. R.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Muller</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>2019</year>). <article-title>Lysosomes as a therapeutic target</article-title>. <source>Nat. Rev. Drug Discov.</source> <volume>18</volume>, <fpage>923</fpage>&#x2013;<lpage>948</lpage>. <pub-id pub-id-type="doi">10.1038/s41573-019-0036-1</pub-id>
</citation>
</ref>
<ref id="B30">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bond</surname>
<given-names>M. R.</given-names>
</name>
<name>
<surname>Hanover</surname>
<given-names>J. A.</given-names>
</name>
</person-group> (<year>2015</year>). <article-title>A little sugar goes a long way: the cell biology of O-GlcNAc</article-title>. <source>J. Cell Biol.</source> <volume>208</volume>, <fpage>869</fpage>&#x2013;<lpage>880</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.201501101</pub-id>
</citation>
</ref>
<ref id="B31">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bordi</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Berg</surname>
<given-names>M. J.</given-names>
</name>
<name>
<surname>Mohan</surname>
<given-names>P. S.</given-names>
</name>
<name>
<surname>Peterhoff</surname>
<given-names>C. M.</given-names>
</name>
<name>
<surname>Alldred</surname>
<given-names>M. J.</given-names>
</name>
<name>
<surname>Che</surname>
<given-names>S.</given-names>
</name>
<etal/>
</person-group> (<year>2016</year>). <article-title>Autophagy flux in CA1 neurons of Alzheimer hippocampus: increased induction overburdens failing lysosomes to propel neuritic dystrophy</article-title>. <source>Autophagy</source> <volume>12</volume>, <fpage>2467</fpage>&#x2013;<lpage>2483</lpage>. <pub-id pub-id-type="doi">10.1080/15548627.2016.1239003</pub-id>
</citation>
</ref>
<ref id="B32">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Brandizzi</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Barlowe</surname>
<given-names>C.</given-names>
</name>
</person-group> (<year>2013</year>). <article-title>Organization of the ER-Golgi interface for membrane traffic control</article-title>. <source>Nat. Rev. Mol. Cell Biol.</source> <volume>14</volume>, <fpage>382</fpage>&#x2013;<lpage>392</lpage>. <pub-id pub-id-type="doi">10.1038/nrm3588</pub-id>
</citation>
</ref>
<ref id="B33">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Braulke</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Carette</surname>
<given-names>J. E.</given-names>
</name>
<name>
<surname>Palm</surname>
<given-names>W.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>Lysosomal enzyme trafficking: from molecular mechanisms to human diseases</article-title>. <source>Trends Cell Biol.</source> <volume>34</volume>, <fpage>P198</fpage>&#x2013;<lpage>P210</lpage>. <pub-id pub-id-type="doi">10.1016/j.tcb.2023.06.005</pub-id>
</citation>
</ref>
<ref id="B34">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Brown</surname>
<given-names>W. J.</given-names>
</name>
<name>
<surname>Farquhar</surname>
<given-names>M. G.</given-names>
</name>
</person-group> (<year>1984</year>). <article-title>The mannose-6-phosphate receptor for lysosomal enzymes is concentrated in cis Golgi cisternae</article-title>. <source>Cell</source> <volume>36</volume>, <fpage>295</fpage>&#x2013;<lpage>307</lpage>. <pub-id pub-id-type="doi">10.1016/0092-8674(84)90223-x</pub-id>
</citation>
</ref>
<ref id="B35">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bucurica</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Gaman</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Jinga</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Popa</surname>
<given-names>A. A.</given-names>
</name>
<name>
<surname>Ionita-Radu</surname>
<given-names>F.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>Golgi apparatus target proteins in gastroenterological cancers: a comprehensive review of GOLPH3 and golga proteins</article-title>. <source>Cells</source> <volume>12</volume>, <fpage>1823</fpage>. <pub-id pub-id-type="doi">10.3390/cells12141823</pub-id>
</citation>
</ref>
<ref id="B36">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Bui</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Mejia</surname>
<given-names>I.</given-names>
</name>
<name>
<surname>Diaz</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2021</year>). <article-title>Adaptation of the golgi apparatus in cancer cell invasion and metastasis</article-title>. <source>Front. Cell Dev. Biol.</source> <volume>9</volume>, <fpage>806482</fpage>. <pub-id pub-id-type="doi">10.3389/fcell.2021.806482</pub-id>
</citation>
</ref>
<ref id="B37">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Burgess</surname>
<given-names>T. L.</given-names>
</name>
<name>
<surname>Kelly</surname>
<given-names>R. B.</given-names>
</name>
</person-group> (<year>1987</year>). <article-title>Constitutive and regulated secretion of proteins</article-title>. <source>Annu. Rev. Cell Biol.</source> <volume>3</volume>, <fpage>243</fpage>&#x2013;<lpage>293</lpage>. <pub-id pub-id-type="doi">10.1146/annurev.cb.03.110187.001331</pub-id>
</citation>
</ref>
<ref id="B38">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Campadelli</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Brandimarti</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Di Lazzaro</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Ward</surname>
<given-names>P. L.</given-names>
</name>
<name>
<surname>Roizman</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Torrisi</surname>
<given-names>M. R.</given-names>
</name>
</person-group> (<year>1993</year>). <article-title>Fragmentation and dispersal of Golgi proteins and redistribution of glycoproteins and glycolipids processed through the Golgi apparatus after infection with herpes simplex virus 1</article-title>. <source>Proc. Natl. Acad. Sci. U. S. A.</source> <volume>90</volume>, <fpage>2798</fpage>&#x2013;<lpage>2802</lpage>. <pub-id pub-id-type="doi">10.1073/pnas.90.7.2798</pub-id>
</citation>
</ref>
<ref id="B39">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Celi</surname>
<given-names>A. B.</given-names>
</name>
<name>
<surname>Goldstein</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Rosato-Siri</surname>
<given-names>M. V.</given-names>
</name>
<name>
<surname>Pinto</surname>
<given-names>A.</given-names>
</name>
</person-group> (<year>2022</year>). <article-title>Role of globotriaosylceramide in physiology and pathology</article-title>. <source>Front. Mol. Biosci.</source> <volume>9</volume>, <fpage>813637</fpage>. <pub-id pub-id-type="doi">10.3389/fmolb.2022.813637</pub-id>
</citation>
</ref>
<ref id="B40">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Cervigni</surname>
<given-names>R. I.</given-names>
</name>
<name>
<surname>Bonavita</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Barretta</surname>
<given-names>M. L.</given-names>
</name>
<name>
<surname>Spano</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Ayala</surname>
<given-names>I.</given-names>
</name>
<name>
<surname>Nakamura</surname>
<given-names>N.</given-names>
</name>
<etal/>
</person-group> (<year>2015</year>). <article-title>JNK2 controls fragmentation of the Golgi complex and the G2/M transition through phosphorylation of GRASP65</article-title>. <source>J. Cell Sci.</source> <volume>128</volume>, <fpage>2249</fpage>&#x2013;<lpage>2260</lpage>. <pub-id pub-id-type="doi">10.1242/jcs.164871</pub-id>
</citation>
</ref>
<ref id="B41">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Chan</surname>
<given-names>Y. A.</given-names>
</name>
<name>
<surname>Zhan</surname>
<given-names>S. H.</given-names>
</name>
</person-group> (<year>2022</year>). <article-title>The emergence of the spike furin cleavage site in SARS-CoV-2</article-title>. <source>Mol. Biol. Evol.</source> <volume>39</volume>, <fpage>msab327</fpage>. <pub-id pub-id-type="doi">10.1093/molbev/msab327</pub-id>
</citation>
</ref>
<ref id="B42">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Chen</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Retzlaff</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Roos</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Frydman</surname>
<given-names>J.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>Cellular strategies of protein quality control</article-title>. <source>Cold Spring Harb. Perspect. Biol.</source> <volume>3</volume>, <fpage>a004374</fpage>. <pub-id pub-id-type="doi">10.1101/cshperspect.a004374</pub-id>
</citation>
</ref>
<ref id="B43">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Chia</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Tham</surname>
<given-names>K. M.</given-names>
</name>
<name>
<surname>Gill</surname>
<given-names>D. J.</given-names>
</name>
<name>
<surname>Bard-Chapeau</surname>
<given-names>E. A.</given-names>
</name>
<name>
<surname>Bard</surname>
<given-names>F. A.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>ERK8 is a negative regulator of O-GalNAc glycosylation and cell migration</article-title>. <source>Elife</source> <volume>3</volume>, <fpage>e01828</fpage>. <pub-id pub-id-type="doi">10.7554/eLife.01828</pub-id>
</citation>
</ref>
<ref id="B44">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ching</surname>
<given-names>Y. P.</given-names>
</name>
<name>
<surname>Leong</surname>
<given-names>V. Y.</given-names>
</name>
<name>
<surname>Lee</surname>
<given-names>M. F.</given-names>
</name>
<name>
<surname>Xu</surname>
<given-names>H. T.</given-names>
</name>
<name>
<surname>Jin</surname>
<given-names>D. Y.</given-names>
</name>
<name>
<surname>Ng</surname>
<given-names>I. O.</given-names>
</name>
</person-group> (<year>2007</year>). <article-title>P21-activated protein kinase is overexpressed in hepatocellular carcinoma and enhances cancer metastasis involving c-Jun NH2-terminal kinase activation and paxillin phosphorylation</article-title>. <source>Cancer Res.</source> <volume>67</volume>, <fpage>3601</fpage>&#x2013;<lpage>3608</lpage>. <pub-id pub-id-type="doi">10.1158/0008-5472.CAN-06-3994</pub-id>
</citation>
</ref>
<ref id="B45">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Chiritoiu</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Brouwers</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Turacchio</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Pirozzi</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Malhotra</surname>
<given-names>V.</given-names>
</name>
</person-group> (<year>2019</year>). <article-title>GRASP55 and UPR control interleukin-1beta aggregation and secretion</article-title>. <source>Dev. Cell</source> <volume>49</volume>, <fpage>145</fpage>&#x2013;<lpage>155 e144</lpage>. <pub-id pub-id-type="doi">10.1016/j.devcel.2019.02.011</pub-id>
</citation>
</ref>
<ref id="B46">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Choy</surname>
<given-names>R. W.</given-names>
</name>
<name>
<surname>Cheng</surname>
<given-names>Z.</given-names>
</name>
<name>
<surname>Schekman</surname>
<given-names>R.</given-names>
</name>
</person-group> (<year>2012</year>). <article-title>Amyloid precursor protein (APP) traffics from the cell surface via endosomes for amyloid &#x3b2; (A&#x3b2;) production in the trans-Golgi network</article-title>. <source>Proc. Natl. Acad. Sci. U. S. A.</source> <volume>109</volume>, <fpage>E2077</fpage>&#x2013;<lpage>E2082</lpage>. <pub-id pub-id-type="doi">10.1073/pnas.1208635109</pub-id>
</citation>
</ref>
<ref id="B47">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Cortese</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Lee</surname>
<given-names>J. Y.</given-names>
</name>
<name>
<surname>Cerikan</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Neufeldt</surname>
<given-names>C. J.</given-names>
</name>
<name>
<surname>Oorschot</surname>
<given-names>V. M. J.</given-names>
</name>
<name>
<surname>Kohrer</surname>
<given-names>S.</given-names>
</name>
<etal/>
</person-group> (<year>2020</year>). <article-title>Integrative imaging reveals SARS-CoV-2-induced reshaping of subcellular morphologies</article-title>. <source>Cell Host Microbe</source> <volume>28</volume>, <fpage>853</fpage>&#x2013;<lpage>866</lpage>. <pub-id pub-id-type="doi">10.1016/j.chom.2020.11.003</pub-id>
</citation>
</ref>
<ref id="B48">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Cortes-Saladelafont</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Fernandez-Martin</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Ortolano</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>Fabry disease and central nervous system involvement: from big to small, from brain to synapse</article-title>. <source>Int. J. Mol. Sci.</source> <volume>24</volume>, <fpage>5246</fpage>. <pub-id pub-id-type="doi">10.3390/ijms24065246</pub-id>
</citation>
</ref>
<ref id="B49">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Coutinho</surname>
<given-names>M. F.</given-names>
</name>
<name>
<surname>Prata</surname>
<given-names>M. J.</given-names>
</name>
<name>
<surname>Alves</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>2012</year>). <article-title>Mannose-6-phosphate pathway: a review on its role in lysosomal function and dysfunction</article-title>. <source>Mol. Genet. Metab.</source> <volume>105</volume>, <fpage>542</fpage>&#x2013;<lpage>550</lpage>. <pub-id pub-id-type="doi">10.1016/j.ymgme.2011.12.012</pub-id>
</citation>
</ref>
<ref id="B50">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Cruz-Garcia</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Brouwers</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Duran</surname>
<given-names>J. M.</given-names>
</name>
<name>
<surname>Mora</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Curwin</surname>
<given-names>A. J.</given-names>
</name>
<name>
<surname>Malhotra</surname>
<given-names>V.</given-names>
</name>
</person-group> (<year>2017</year>). <article-title>A diacidic motif determines unconventional secretion of wild-type and ALS-linked mutant SOD1</article-title>. <source>J. Cell Biol.</source> <volume>216</volume>, <fpage>2691</fpage>&#x2013;<lpage>2700</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.201704056</pub-id>
</citation>
</ref>
<ref id="B51">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Cuozzo</surname>
<given-names>J. W.</given-names>
</name>
<name>
<surname>Sahagian</surname>
<given-names>G. G.</given-names>
</name>
</person-group> (<year>1994</year>). <article-title>Lysine is a common determinant for mannose phosphorylation of lysosomal proteins</article-title>. <source>J. Biol. Chem.</source> <volume>269</volume>, <fpage>14490</fpage>&#x2013;<lpage>14496</lpage>. <pub-id pub-id-type="doi">10.1016/s0021-9258(17)36649-8</pub-id>
</citation>
</ref>
<ref id="B52">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Dal Canto</surname>
<given-names>M. C.</given-names>
</name>
</person-group> (<year>1996</year>). <article-title>The Golgi apparatus and the pathogenesis of Alzheimer&#x27;s disease</article-title>. <source>Am. J. Pathol.</source> <volume>148</volume>, <fpage>355</fpage>&#x2013;<lpage>360</lpage>.</citation>
</ref>
<ref id="B53">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>D&#x27;angelo</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Prencipe</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Iodice</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Beznoussenko</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Savarese</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Marra</surname>
<given-names>P.</given-names>
</name>
<etal/>
</person-group> (<year>2009</year>). <article-title>GRASP65 and GRASP55 sequentially promote the transport of C-terminal valine-bearing cargos to and through the Golgi complex</article-title>. <source>J. Biol. Chem.</source> <volume>284</volume>, <fpage>34849</fpage>&#x2013;<lpage>34860</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M109.068403</pub-id>
</citation>
</ref>
<ref id="B54">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Darios</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Stevanin</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2020</year>). <article-title>Impairment of lysosome function and autophagy in rare neurodegenerative diseases</article-title>. <source>J. Mol. Biol.</source> <volume>432</volume>, <fpage>2714</fpage>&#x2013;<lpage>2734</lpage>. <pub-id pub-id-type="doi">10.1016/j.jmb.2020.02.033</pub-id>
</citation>
</ref>
<ref id="B55">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Dennis</surname>
<given-names>J. W.</given-names>
</name>
<name>
<surname>Granovsky</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Warren</surname>
<given-names>C. E.</given-names>
</name>
</person-group> (<year>1999</year>). <article-title>Glycoprotein glycosylation and cancer progression</article-title>. <source>Biochim. Biophys. Acta</source> <volume>1473</volume>, <fpage>21</fpage>&#x2013;<lpage>34</lpage>. <pub-id pub-id-type="doi">10.1016/s0304-4165(99)00167-1</pub-id>
</citation>
</ref>
<ref id="B56">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Diaz-Corrales</surname>
<given-names>F. J.</given-names>
</name>
<name>
<surname>Asanuma</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Miyazaki</surname>
<given-names>I.</given-names>
</name>
<name>
<surname>Ogawa</surname>
<given-names>N.</given-names>
</name>
</person-group> (<year>2004</year>). <article-title>Rotenone induces disassembly of the Golgi apparatus in the rat dopaminergic neuroblastoma B65 cell line</article-title>. <source>Neurosci. Lett.</source> <volume>354</volume>, <fpage>59</fpage>&#x2013;<lpage>63</lpage>. <pub-id pub-id-type="doi">10.1016/j.neulet.2003.09.059</pub-id>
</citation>
</ref>
<ref id="B57">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Dries</surname>
<given-names>D. R.</given-names>
</name>
<name>
<surname>Yu</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2008</year>). <article-title>Assembly, maturation, and trafficking of the gamma-secretase complex in Alzheimer&#x27;s disease</article-title>. <source>Curr. Alzheimer Res.</source> <volume>5</volume>, <fpage>132</fpage>&#x2013;<lpage>146</lpage>. <pub-id pub-id-type="doi">10.2174/156720508783954695</pub-id>
</citation>
</ref>
<ref id="B58">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Driouich</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Follet-Gueye</surname>
<given-names>M. L.</given-names>
</name>
<name>
<surname>Bernard</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Kousar</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Chevalier</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Vicre-Gibouin</surname>
<given-names>M.</given-names>
</name>
<etal/>
</person-group> (<year>2012</year>). <article-title>Golgi-mediated synthesis and secretion of matrix polysaccharides of the primary cell wall of higher plants</article-title>. <source>Front. Plant Sci.</source> <volume>3</volume>, <fpage>79</fpage>. <pub-id pub-id-type="doi">10.3389/fpls.2012.00079</pub-id>
</citation>
</ref>
<ref id="B59">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Durand</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Seta</surname>
<given-names>N.</given-names>
</name>
</person-group> (<year>2000</year>). <article-title>Protein glycosylation and diseases: blood and urinary oligosaccharides as markers for diagnosis and therapeutic monitoring</article-title>. <source>Clin. Chem.</source> <volume>46</volume>, <fpage>795</fpage>&#x2013;<lpage>805</lpage>. <pub-id pub-id-type="doi">10.1093/clinchem/46.6.795</pub-id>
</citation>
</ref>
<ref id="B60">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Egea</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Franci</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Gambus</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Lesuffleur</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Zweibaum</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Real</surname>
<given-names>F. X.</given-names>
</name>
</person-group> (<year>1993</year>). <article-title>cis-Golgi resident proteins and O-glycans are abnormally compartmentalized in the RER of colon cancer cells</article-title>. <source>J. Cell Sci.</source> <volume>105</volume> (<issue>Pt 3</issue>), <fpage>819</fpage>&#x2013;<lpage>830</lpage>. <pub-id pub-id-type="doi">10.1242/jcs.105.3.819</pub-id>
</citation>
</ref>
<ref id="B61">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>El-Agnaf</surname>
<given-names>O. M.</given-names>
</name>
<name>
<surname>Salem</surname>
<given-names>S. A.</given-names>
</name>
<name>
<surname>Paleologou</surname>
<given-names>K. E.</given-names>
</name>
<name>
<surname>Cooper</surname>
<given-names>L. J.</given-names>
</name>
<name>
<surname>Fullwood</surname>
<given-names>N. J.</given-names>
</name>
<name>
<surname>Gibson</surname>
<given-names>M. J.</given-names>
</name>
<etal/>
</person-group> (<year>2003</year>). <article-title>Alpha-synuclein implicated in Parkinson&#x27;s disease is present in extracellular biological fluids, including human plasma</article-title>. <source>FASEB J.</source> <volume>17</volume>, <fpage>1945</fpage>&#x2013;<lpage>1947</lpage>. <pub-id pub-id-type="doi">10.1096/fj.03-0098fje</pub-id>
</citation>
</ref>
<ref id="B62">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>El-Agnaf</surname>
<given-names>O. M.</given-names>
</name>
<name>
<surname>Salem</surname>
<given-names>S. A.</given-names>
</name>
<name>
<surname>Paleologou</surname>
<given-names>K. E.</given-names>
</name>
<name>
<surname>Curran</surname>
<given-names>M. D.</given-names>
</name>
<name>
<surname>Gibson</surname>
<given-names>M. J.</given-names>
</name>
<name>
<surname>Court</surname>
<given-names>J. A.</given-names>
</name>
<etal/>
</person-group> (<year>2006</year>). <article-title>Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson&#x27;s disease</article-title>. <source>FASEB J.</source> <volume>20</volume>, <fpage>419</fpage>&#x2013;<lpage>425</lpage>. <pub-id pub-id-type="doi">10.1096/fj.03-1449com</pub-id>
</citation>
</ref>
<ref id="B63">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Emmanouilidou</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Melachroinou</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Roumeliotis</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Garbis</surname>
<given-names>S. D.</given-names>
</name>
<name>
<surname>Ntzouni</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Margaritis</surname>
<given-names>L. H.</given-names>
</name>
<etal/>
</person-group> (<year>2010</year>). <article-title>Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival</article-title>. <source>J. Neurosci.</source> <volume>30</volume>, <fpage>6838</fpage>&#x2013;<lpage>6851</lpage>. <pub-id pub-id-type="doi">10.1523/JNEUROSCI.5699-09.2010</pub-id>
</citation>
</ref>
<ref id="B64">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Evin</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2015</year>). <article-title>How accelerated Golgi trafficking may drive Alzheimer&#x27;s disease</article-title>. <source>Bioessays</source> <volume>37</volume>, <fpage>232</fpage>&#x2013;<lpage>233</lpage>. <pub-id pub-id-type="doi">10.1002/bies.201400219</pub-id>
</citation>
</ref>
<ref id="B65">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Farquhar</surname>
<given-names>M. G.</given-names>
</name>
<name>
<surname>Palade</surname>
<given-names>G. E.</given-names>
</name>
</person-group> (<year>1998</year>). <article-title>The Golgi apparatus: 100 years of progress and controversy</article-title>. <source>Trends Cell Biol.</source> <volume>8</volume>, <fpage>2</fpage>&#x2013;<lpage>10</lpage>. <pub-id pub-id-type="doi">10.1016/s0962-8924(97)01187-2</pub-id>
</citation>
</ref>
<ref id="B66">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Feng</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>He</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Yao</surname>
<given-names>Z.</given-names>
</name>
<name>
<surname>Klionsky</surname>
<given-names>D. J.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>The machinery of macroautophagy</article-title>. <source>Cell Res.</source> <volume>24</volume>, <fpage>24</fpage>&#x2013;<lpage>41</lpage>. <pub-id pub-id-type="doi">10.1038/cr.2013.168</pub-id>
</citation>
</ref>
<ref id="B67">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Fernandez-Castaneda</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Lu</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Geraghty</surname>
<given-names>A. C.</given-names>
</name>
<name>
<surname>Song</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Lee</surname>
<given-names>M. H.</given-names>
</name>
<name>
<surname>Wood</surname>
<given-names>J.</given-names>
</name>
<etal/>
</person-group> (<year>2022</year>). <article-title>Mild respiratory COVID can cause multi-lineage neural cell and myelin dysregulation</article-title>. <source>Cell</source> <volume>185</volume>, <fpage>2452</fpage>&#x2013;<lpage>2468.e16</lpage>. <pub-id pub-id-type="doi">10.1016/j.cell.2022.06.008</pub-id>
</citation>
</ref>
<ref id="B68">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ferreira</surname>
<given-names>C. R.</given-names>
</name>
<name>
<surname>Gahl</surname>
<given-names>W. A.</given-names>
</name>
</person-group> (<year>2017</year>). <article-title>Lysosomal storage diseases</article-title>. <source>Transl. Sci. Rare Dis.</source> <volume>2</volume>, <fpage>1</fpage>&#x2013;<lpage>71</lpage>. <pub-id pub-id-type="doi">10.3233/TRD-160005</pub-id>
</citation>
</ref>
<ref id="B69">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Filocamo</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Morrone</surname>
<given-names>A.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>Lysosomal storage disorders: molecular basis and laboratory testing</article-title>. <source>Hum. Genomics</source> <volume>5</volume>, <fpage>156</fpage>&#x2013;<lpage>169</lpage>. <pub-id pub-id-type="doi">10.1186/1479-7364-5-3-156</pub-id>
</citation>
</ref>
<ref id="B70">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Franco</surname>
<given-names>K. S.</given-names>
</name>
<name>
<surname>Bronson</surname>
<given-names>D.</given-names>
</name>
</person-group> (<year>2005</year>). <article-title>Diabetes mellitus and Alzheimer disease</article-title>. <source>Arch. Neurol.</source> <volume>62</volume>, <fpage>330; author reply 330</fpage>&#x2013;<lpage>331</lpage>. <pub-id pub-id-type="doi">10.1001/archneur.62.2.330-a</pub-id>
</citation>
</ref>
<ref id="B71">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Freeze</surname>
<given-names>H. H.</given-names>
</name>
<name>
<surname>Ng</surname>
<given-names>B. G.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>Golgi glycosylation and human inherited diseases</article-title>. <source>Cold Spring Harb. Perspect. Biol.</source> <volume>3</volume>, <fpage>a005371</fpage>. <pub-id pub-id-type="doi">10.1101/cshperspect.a005371</pub-id>
</citation>
</ref>
<ref id="B72">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Fritzler</surname>
<given-names>M. J.</given-names>
</name>
<name>
<surname>Etherington</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Sokoluk</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Kinsella</surname>
<given-names>T. D.</given-names>
</name>
<name>
<surname>Valencia</surname>
<given-names>D. W.</given-names>
</name>
</person-group> (<year>1984</year>). <article-title>Antibodies from patients with autoimmune disease react with a cytoplasmic antigen in the Golgi apparatus</article-title>. <source>J. Immunol.</source> <volume>132</volume>, <fpage>2904</fpage>&#x2013;<lpage>2908</lpage>. <pub-id pub-id-type="doi">10.4049/jimmunol.132.6.2904</pub-id>
</citation>
</ref>
<ref id="B73">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Fujita</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Okamoto</surname>
<given-names>K.</given-names>
</name>
</person-group> (<year>2005</year>). <article-title>Golgi apparatus of the motor neurons in patients with amyotrophic lateral sclerosis and in mice models of amyotrophic lateral sclerosis</article-title>. <source>Neuropathology</source> <volume>25</volume>, <fpage>388</fpage>&#x2013;<lpage>394</lpage>. <pub-id pub-id-type="doi">10.1111/j.1440-1789.2005.00616.x</pub-id>
</citation>
</ref>
<ref id="B74">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Fujita</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Okamoto</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Sakurai</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Kusaka</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Aizawa</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Mihara</surname>
<given-names>B.</given-names>
</name>
<etal/>
</person-group> (<year>2002</year>). <article-title>The Golgi apparatus is fragmented in spinal cord motor neurons of amyotrophic lateral sclerosis with basophilic inclusions</article-title>. <source>Acta Neuropathol.</source> <volume>103</volume>, <fpage>243</fpage>&#x2013;<lpage>247</lpage>. <pub-id pub-id-type="doi">10.1007/s004010100461</pub-id>
</citation>
</ref>
<ref id="B75">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Futerman</surname>
<given-names>A. H.</given-names>
</name>
<name>
<surname>Van Meer</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2004</year>). <article-title>The cell biology of lysosomal storage disorders</article-title>. <source>Nat. Rev. Mol. Cell Biol.</source> <volume>5</volume>, <fpage>554</fpage>&#x2013;<lpage>565</lpage>. <pub-id pub-id-type="doi">10.1038/nrm1423</pub-id>
</citation>
</ref>
<ref id="B76">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Galluzzi</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Pietrocola</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Levine</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Kroemer</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>Metabolic control of autophagy</article-title>. <source>Cell</source> <volume>159</volume>, <fpage>1263</fpage>&#x2013;<lpage>1276</lpage>. <pub-id pub-id-type="doi">10.1016/j.cell.2014.11.006</pub-id>
</citation>
</ref>
<ref id="B77">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Gee</surname>
<given-names>H. Y.</given-names>
</name>
<name>
<surname>Noh</surname>
<given-names>S. H.</given-names>
</name>
<name>
<surname>Tang</surname>
<given-names>B. L.</given-names>
</name>
<name>
<surname>Kim</surname>
<given-names>K. H.</given-names>
</name>
<name>
<surname>Lee</surname>
<given-names>M. G.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>Rescue of &#x394;F508-CFTR trafficking via a GRASP-dependent unconventional secretion pathway</article-title>. <source>Cell</source> <volume>146</volume>, <fpage>746</fpage>&#x2013;<lpage>760</lpage>. <pub-id pub-id-type="doi">10.1016/j.cell.2011.07.021</pub-id>
</citation>
</ref>
<ref id="B78">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Geuze</surname>
<given-names>H. J.</given-names>
</name>
<name>
<surname>Slot</surname>
<given-names>J. W.</given-names>
</name>
<name>
<surname>Strous</surname>
<given-names>G. J.</given-names>
</name>
<name>
<surname>Hasilik</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Von Figura</surname>
<given-names>K.</given-names>
</name>
</person-group> (<year>1984</year>). <article-title>Ultrastructural localization of the mannose 6-phosphate receptor in rat liver</article-title>. <source>J. Cell Biol.</source> <volume>98</volume>, <fpage>2047</fpage>&#x2013;<lpage>2054</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.98.6.2047</pub-id>
</citation>
</ref>
<ref id="B79">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Gieselmann</surname>
<given-names>V.</given-names>
</name>
<name>
<surname>Hasilik</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Von Figura</surname>
<given-names>K.</given-names>
</name>
</person-group> (<year>1985</year>). <article-title>Processing of human cathepsin D in lysosomes <italic>in vitro</italic>
</article-title>. <source>J. Biol. Chem.</source> <volume>260</volume>, <fpage>3215</fpage>&#x2013;<lpage>3220</lpage>. <pub-id pub-id-type="doi">10.1016/s0021-9258(18)89493-5</pub-id>
</citation>
</ref>
<ref id="B80">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Gieselmann</surname>
<given-names>V.</given-names>
</name>
<name>
<surname>Polten</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Kreysing</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Kappler</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Fluharty</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Von Figura</surname>
<given-names>K.</given-names>
</name>
</person-group> (<year>1991</year>). <article-title>Molecular genetics of metachromatic leukodystrophy</article-title>. <source>Dev. Neurosci.</source> <volume>13</volume>, <fpage>222</fpage>&#x2013;<lpage>227</lpage>. <pub-id pub-id-type="doi">10.1159/000112164</pub-id>
</citation>
</ref>
<ref id="B81">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Glick</surname>
<given-names>B. S.</given-names>
</name>
<name>
<surname>Nakano</surname>
<given-names>A.</given-names>
</name>
</person-group> (<year>2009</year>). <article-title>Membrane traffic within the Golgi apparatus</article-title>. <source>Annu. Rev. Cell Dev. Biol.</source> <volume>25</volume>, <fpage>113</fpage>&#x2013;<lpage>132</lpage>. <pub-id pub-id-type="doi">10.1146/annurev.cellbio.24.110707.175421</pub-id>
</citation>
</ref>
<ref id="B82">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Goldfischer</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>1982</year>). <article-title>The internal reticular apparatus of Camillo Golgi: a complex, heterogeneous organelle, enriched in acid, neutral, and alkaline phosphatases, and involved in glycosylation, secretion, membrane flow, lysosome formation, and intracellular digestion</article-title>. <source>J. Histochem Cytochem</source> <volume>30</volume>, <fpage>717</fpage>&#x2013;<lpage>733</lpage>. <pub-id pub-id-type="doi">10.1177/30.7.6286754</pub-id>
</citation>
</ref>
<ref id="B83">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Gomes</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Keller</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Altevogt</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Costa</surname>
<given-names>J.</given-names>
</name>
</person-group> (<year>2007</year>). <article-title>Evidence for secretion of Cu,Zn superoxide dismutase via exosomes from a cell model of amyotrophic lateral sclerosis</article-title>. <source>Neurosci. Lett.</source> <volume>428</volume>, <fpage>43</fpage>&#x2013;<lpage>46</lpage>. <pub-id pub-id-type="doi">10.1016/j.neulet.2007.09.024</pub-id>
</citation>
</ref>
<ref id="B84">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Gonatas</surname>
<given-names>N. K.</given-names>
</name>
<name>
<surname>Gonatas</surname>
<given-names>J. O.</given-names>
</name>
<name>
<surname>Stieber</surname>
<given-names>A.</given-names>
</name>
</person-group> (<year>1998</year>). <article-title>The involvement of the Golgi apparatus in the pathogenesis of amyotrophic lateral sclerosis, Alzheimer&#x27;s disease, and ricin intoxication</article-title>. <source>Histochem Cell Biol.</source> <volume>109</volume>, <fpage>591</fpage>&#x2013;<lpage>600</lpage>. <pub-id pub-id-type="doi">10.1007/s004180050257</pub-id>
</citation>
</ref>
<ref id="B85">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Grey</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Dunning</surname>
<given-names>C. J.</given-names>
</name>
<name>
<surname>Gaspar</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Grey</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Brundin</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Sparr</surname>
<given-names>E.</given-names>
</name>
<etal/>
</person-group> (<year>2015</year>). <article-title>Acceleration of &#x3b1;-synuclein aggregation by exosomes</article-title>. <source>J. Biol. Chem.</source> <volume>290</volume>, <fpage>2969</fpage>&#x2013;<lpage>2982</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M114.585703</pub-id>
</citation>
</ref>
<ref id="B86">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Guo</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Sirkis</surname>
<given-names>D. W.</given-names>
</name>
<name>
<surname>Schekman</surname>
<given-names>R.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>Protein sorting at the trans-Golgi network</article-title>. <source>Annu. Rev. Cell Dev. Biol.</source> <volume>30</volume>, <fpage>169</fpage>&#x2013;<lpage>206</lpage>. <pub-id pub-id-type="doi">10.1146/annurev-cellbio-100913-013012</pub-id>
</citation>
</ref>
<ref id="B87">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Haass</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Kaether</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Thinakaran</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Sisodia</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>2012</year>). <article-title>Trafficking and proteolytic processing of APP</article-title>. <source>Cold Spring Harb. Perspect. Med.</source> <volume>2</volume>, <fpage>a006270</fpage>. <pub-id pub-id-type="doi">10.1101/cshperspect.a006270</pub-id>
</citation>
</ref>
<ref id="B88">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Helenius</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Aebi</surname>
<given-names>M.</given-names>
</name>
</person-group> (<year>2001</year>). <article-title>Intracellular functions of N-linked glycans</article-title>. <source>Science</source> <volume>291</volume>, <fpage>2364</fpage>&#x2013;<lpage>2369</lpage>. <pub-id pub-id-type="doi">10.1126/science.291.5512.2364</pub-id>
</citation>
</ref>
<ref id="B89">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Hilditch-Maguire</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Trettel</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Passani</surname>
<given-names>L. A.</given-names>
</name>
<name>
<surname>Auerbach</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Persichetti</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Macdonald</surname>
<given-names>M. E.</given-names>
</name>
</person-group> (<year>2000</year>). <article-title>Huntingtin: an iron-regulated protein essential for normal nuclear and perinuclear organelles</article-title>. <source>Hum. Mol. Genet.</source> <volume>9</volume>, <fpage>2789</fpage>&#x2013;<lpage>2797</lpage>. <pub-id pub-id-type="doi">10.1093/hmg/9.19.2789</pub-id>
</citation>
</ref>
<ref id="B90">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Hoflack</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Kornfeld</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>1985</year>). <article-title>Purification and characterization of a cation-dependent mannose 6-phosphate receptor from murine P388D1 macrophages and bovine liver</article-title>. <source>J. Biol. Chem.</source> <volume>260</volume>, <fpage>12008</fpage>&#x2013;<lpage>12014</lpage>. <pub-id pub-id-type="doi">10.1016/s0021-9258(17)38977-9</pub-id>
</citation>
</ref>
<ref id="B91">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Hu</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Shi</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Huang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Morelli</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Shi</surname>
<given-names>N.</given-names>
</name>
</person-group> (<year>2015</year>). <article-title>Structural basis for the interaction between the Golgi reassembly-stacking protein GRASP65 and the Golgi matrix protein GM130</article-title>. <source>J. Biol. Chem.</source> <volume>290</volume>, <fpage>26373</fpage>&#x2013;<lpage>26382</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M115.657940</pub-id>
</citation>
</ref>
<ref id="B92">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Huang</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Haga</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Kweon</surname>
<given-names>H. K.</given-names>
</name>
<name>
<surname>Seino</surname>
<given-names>J.</given-names>
</name>
<etal/>
</person-group> (<year>2022</year>). <article-title>Mitotic phosphorylation inhibits the Golgi mannosidase MAN1A1</article-title>. <source>Cell Rep.</source> <volume>41</volume>, <fpage>111679</fpage>. <pub-id pub-id-type="doi">10.1016/j.celrep.2022.111679</pub-id>
</citation>
</ref>
<ref id="B93">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Huang</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2016</year>). <article-title>Monoubiquitination of syntaxin 5 regulates golgi membrane dynamics during the cell cycle</article-title>. <source>Dev. Cell</source> <volume>38</volume>, <fpage>73</fpage>&#x2013;<lpage>85</lpage>. <pub-id pub-id-type="doi">10.1016/j.devcel.2016.06.001</pub-id>
</citation>
</ref>
<ref id="B94">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Huang</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2017</year>). <article-title>Golgi structure formation, function, and post-translational modifications in mammalian cells</article-title>. <source>F1000Res</source> <volume>6</volume>, <fpage>2050</fpage>. <pub-id pub-id-type="doi">10.12688/f1000research.11900.1</pub-id>
</citation>
</ref>
<ref id="B95">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Huse</surname>
<given-names>J. T.</given-names>
</name>
<name>
<surname>Liu</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Pijak</surname>
<given-names>D. S.</given-names>
</name>
<name>
<surname>Carlin</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Lee</surname>
<given-names>V. M.</given-names>
</name>
<name>
<surname>Doms</surname>
<given-names>R. W.</given-names>
</name>
</person-group> (<year>2002</year>). <article-title>Beta-secretase processing in the trans-Golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer&#x27;s disease brain</article-title>. <source>J. Biol. Chem.</source> <volume>277</volume>, <fpage>16278</fpage>&#x2013;<lpage>16284</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M111141200</pub-id>
</citation>
</ref>
<ref id="B96">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Huttner</surname>
<given-names>W. B.</given-names>
</name>
<name>
<surname>Ohashi</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Kehlenbach</surname>
<given-names>R. H.</given-names>
</name>
<name>
<surname>Barr</surname>
<given-names>F. A.</given-names>
</name>
<name>
<surname>Bauerfeind</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Braunling</surname>
<given-names>O.</given-names>
</name>
<etal/>
</person-group> (<year>1995</year>). <article-title>Biogenesis of neurosecretory vesicles</article-title>. <source>Cold Spring Harb. Symp. Quant. Biol.</source> <volume>60</volume>, <fpage>315</fpage>&#x2013;<lpage>327</lpage>. <pub-id pub-id-type="doi">10.1101/sqb.1995.060.01.036</pub-id>
</citation>
</ref>
<ref id="B97">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Hwang</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Estick</surname>
<given-names>C. M.</given-names>
</name>
<name>
<surname>Ikonne</surname>
<given-names>U. S.</given-names>
</name>
<name>
<surname>Butler</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Pait</surname>
<given-names>M. C.</given-names>
</name>
<name>
<surname>Elliott</surname>
<given-names>L. H.</given-names>
</name>
<etal/>
</person-group> (<year>2019</year>). <article-title>The role of lysosomes in a broad disease-modifying approach evaluated across transgenic mouse models of Alzheimer&#x2019;s disease and Parkinson&#x2019;s disease and models of mild cognitive impairment</article-title>. <source>Int. J. Mol. Sci.</source> <volume>20</volume>, <fpage>4432</fpage>. <pub-id pub-id-type="doi">10.3390/ijms20184432</pub-id>
</citation>
</ref>
<ref id="B98">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ibata</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Yuzaki</surname>
<given-names>M.</given-names>
</name>
</person-group> (<year>2021</year>). <article-title>Destroy the old to build the new: activity-dependent lysosomal exocytosis in neurons</article-title>. <source>Neurosci. Res.</source> <volume>167</volume>, <fpage>38</fpage>&#x2013;<lpage>46</lpage>. <pub-id pub-id-type="doi">10.1016/j.neures.2021.03.011</pub-id>
</citation>
</ref>
<ref id="B99">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Iguchi</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Eid</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Parent</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Soucy</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Bareil</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Riku</surname>
<given-names>Y.</given-names>
</name>
<etal/>
</person-group> (<year>2016</year>). <article-title>Exosome secretion is a key pathway for clearance of pathological TDP-43</article-title>. <source>Brain</source> <volume>139</volume>, <fpage>3187</fpage>&#x2013;<lpage>3201</lpage>. <pub-id pub-id-type="doi">10.1093/brain/aww237</pub-id>
</citation>
</ref>
<ref id="B100">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ireland</surname>
<given-names>S. C.</given-names>
</name>
<name>
<surname>Huang</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2020b</year>). <article-title>Hydrogen peroxide induces Arl1 degradation and impairs Golgi-mediated trafficking</article-title>. <source>Mol. Biol. Cell</source> <volume>31</volume>, <fpage>1931</fpage>&#x2013;<lpage>1942</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.E20-01-0063</pub-id>
</citation>
</ref>
<ref id="B101">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ireland</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>S</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Fu</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<etal/>
</person-group> (<year>2020a</year>). <article-title>Cytosolic Ca 2&#x2b; modulates golgi structure through pkc&#x3b1;-mediated GRASP55 phosphorylation</article-title>. <source>iScience</source> <volume>23</volume>, <fpage>100952</fpage>. <pub-id pub-id-type="doi">10.1016/j.isci.2020.100952</pub-id>
</citation>
</ref>
<ref id="B102">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ishii</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Kawakami</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Endo</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Misawa</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Watabe</surname>
<given-names>K.</given-names>
</name>
</person-group> (<year>2017</year>). <article-title>Formation and spreading of TDP-43 aggregates in cultured neuronal and glial cells demonstrated by time-lapse imaging</article-title>. <source>PLoS One</source> <volume>12</volume>, <fpage>e0179375</fpage>. <pub-id pub-id-type="doi">10.1371/journal.pone.0179375</pub-id>
</citation>
</ref>
<ref id="B103">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Janke</surname>
<given-names>C.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>The tubulin code: molecular components, readout mechanisms, and functions</article-title>. <source>J. Cell Biol.</source> <volume>206</volume>, <fpage>461</fpage>&#x2013;<lpage>472</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.201406055</pub-id>
</citation>
</ref>
<ref id="B104">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Jarvela</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Linstedt</surname>
<given-names>A. D.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization</article-title>. <source>Mol. Biol. Cell</source> <volume>25</volume>, <fpage>133</fpage>&#x2013;<lpage>144</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.E13-07-0395</pub-id>
</citation>
</ref>
<ref id="B105">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Jensen</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Schekman</surname>
<given-names>R.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>COPII-mediated vesicle formation at a glance</article-title>. <source>J. Cell Sci.</source> <volume>124</volume>, <fpage>1</fpage>&#x2013;<lpage>4</lpage>. <pub-id pub-id-type="doi">10.1242/jcs.069773</pub-id>
</citation>
</ref>
<ref id="B106">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Jesch</surname>
<given-names>S. A.</given-names>
</name>
<name>
<surname>Lewis</surname>
<given-names>T. S.</given-names>
</name>
<name>
<surname>Ahn</surname>
<given-names>N. G.</given-names>
</name>
<name>
<surname>Linstedt</surname>
<given-names>A. D.</given-names>
</name>
</person-group> (<year>2001</year>). <article-title>Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2</article-title>. <source>Mol. Biol. Cell</source> <volume>12</volume>, <fpage>1811</fpage>&#x2013;<lpage>1817</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.12.6.1811</pub-id>
</citation>
</ref>
<ref id="B107">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Jiang</surname>
<given-names>Z.</given-names>
</name>
<name>
<surname>Kuo</surname>
<given-names>Y. H.</given-names>
</name>
<name>
<surname>Zhong</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Zhou</surname>
<given-names>X. X.</given-names>
</name>
<name>
<surname>Xing</surname>
<given-names>L.</given-names>
</name>
<etal/>
</person-group> (<year>2022</year>). <article-title>Adaptor-specific antibody fragment inhibitors for the intracellular modulation of p97 (VCP) protein-protein interactions</article-title>. <source>J. Am. Chem. Soc.</source> <volume>144</volume>, <fpage>13218</fpage>&#x2013;<lpage>13225</lpage>. <pub-id pub-id-type="doi">10.1021/jacs.2c03665</pub-id>
</citation>
</ref>
<ref id="B108">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Jo</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Lee</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Jeon</surname>
<given-names>Y.-M.</given-names>
</name>
<name>
<surname>Kim</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Kwon</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Kim</surname>
<given-names>H.-J.</given-names>
</name>
</person-group> (<year>2020</year>). <article-title>The role of TDP-43 propagation in neurodegenerative diseases: integrating insights from clinical and experimental studies</article-title>. <source>Exp. Mol. Med.</source> <volume>52</volume>, <fpage>1652</fpage>&#x2013;<lpage>1662</lpage>. <pub-id pub-id-type="doi">10.1038/s12276-020-00513-7</pub-id>
</citation>
</ref>
<ref id="B109">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Joazeiro</surname>
<given-names>C. A.</given-names>
</name>
<name>
<surname>Weissman</surname>
<given-names>A. M.</given-names>
</name>
</person-group> (<year>2000</year>). <article-title>RING finger proteins: mediators of ubiquitin ligase activity</article-title>. <source>Cell</source> <volume>102</volume>, <fpage>549</fpage>&#x2013;<lpage>552</lpage>. <pub-id pub-id-type="doi">10.1016/s0092-8674(00)00077-5</pub-id>
</citation>
</ref>
<ref id="B110">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Johnson</surname>
<given-names>B. S.</given-names>
</name>
<name>
<surname>Snead</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Lee</surname>
<given-names>J. J.</given-names>
</name>
<name>
<surname>Mccaffery</surname>
<given-names>J. M.</given-names>
</name>
<name>
<surname>Shorter</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Gitler</surname>
<given-names>A. D.</given-names>
</name>
</person-group> (<year>2009</year>). <article-title>TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity</article-title>. <source>J. Biol. Chem.</source> <volume>284</volume>, <fpage>20329</fpage>&#x2013;<lpage>20339</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M109.010264</pub-id>
</citation>
</ref>
<ref id="B111">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Joshi</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Bekier</surname>
<given-names>M. E.</given-names>
<suffix>2nd</suffix>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2015</year>). <article-title>Golgi fragmentation in Alzheimer&#x27;s disease</article-title>. <source>Front. Neurosci.</source> <volume>9</volume>, <fpage>340</fpage>. <pub-id pub-id-type="doi">10.3389/fnins.2015.00340</pub-id>
</citation>
</ref>
<ref id="B112">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Joshi</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Chi</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Huang</surname>
<given-names>Z.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>A&#x3b2;-induced Golgi fragmentation in Alzheimer&#x27;s disease enhances A&#x3b2; production</article-title>. <source>Proc. Natl. Acad. Sci. U. S. A.</source> <volume>111</volume>, <fpage>E1230</fpage>&#x2013;<lpage>E1239</lpage>. <pub-id pub-id-type="doi">10.1073/pnas.1320192111</pub-id>
</citation>
</ref>
<ref id="B113">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Joshi</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2015</year>). <article-title>Golgi defects enhance APP amyloidogenic processing in Alzheimer&#x27;s disease</article-title>. <source>Bioessays</source> <volume>37</volume>, <fpage>240</fpage>&#x2013;<lpage>247</lpage>. <pub-id pub-id-type="doi">10.1002/bies.201400116</pub-id>
</citation>
</ref>
<ref id="B114">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Kaufmann</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Kukolj</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Brachner</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Beltzung</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Bruno</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Kostrhon</surname>
<given-names>S.</given-names>
</name>
<etal/>
</person-group> (<year>2016</year>). <article-title>SIRT2 regulates nuclear envelope reassembly through ANKLE2 deacetylation</article-title>. <source>J. Cell Sci.</source> <volume>129</volume>, <fpage>4607</fpage>&#x2013;<lpage>4621</lpage>. <pub-id pub-id-type="doi">10.1242/jcs.192633</pub-id>
</citation>
</ref>
<ref id="B115">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Kellokumpu</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Sormunen</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Kellokumpu</surname>
<given-names>I.</given-names>
</name>
</person-group> (<year>2002</year>). <article-title>Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra-Golgi pH</article-title>. <source>FEBS Lett.</source> <volume>516</volume>, <fpage>217</fpage>&#x2013;<lpage>224</lpage>. <pub-id pub-id-type="doi">10.1016/s0014-5793(02)02535-8</pub-id>
</citation>
</ref>
<ref id="B116">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Khan</surname>
<given-names>S. A.</given-names>
</name>
<name>
<surname>Tomatsu</surname>
<given-names>S. C.</given-names>
</name>
</person-group> (<year>2020</year>). <article-title>Mucolipidoses overview: past, present, and future</article-title>. <source>Int. J. Mol. Sci.</source> <volume>21</volume>, <fpage>6812</fpage>. <pub-id pub-id-type="doi">10.3390/ijms21186812</pub-id>
</citation>
</ref>
<ref id="B117">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Kim</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Nam</surname>
<given-names>D. W.</given-names>
</name>
<name>
<surname>Park</surname>
<given-names>S. Y.</given-names>
</name>
<name>
<surname>Song</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Hong</surname>
<given-names>H. S.</given-names>
</name>
<name>
<surname>Boo</surname>
<given-names>J. H.</given-names>
</name>
<etal/>
</person-group> (<year>2013</year>). <article-title>O-linked &#x3b2;-N-acetylglucosaminidase inhibitor attenuates &#x3b2;-amyloid plaque and rescues memory impairment</article-title>. <source>Neurobiol. Aging</source> <volume>34</volume>, <fpage>275</fpage>&#x2013;<lpage>285</lpage>. <pub-id pub-id-type="doi">10.1016/j.neurobiolaging.2012.03.001</pub-id>
</citation>
</ref>
<ref id="B118">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Kim</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Kim</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Noh</surname>
<given-names>S. H.</given-names>
</name>
<name>
<surname>Jang</surname>
<given-names>D. G.</given-names>
</name>
<name>
<surname>Park</surname>
<given-names>S. Y.</given-names>
</name>
<name>
<surname>Min</surname>
<given-names>D.</given-names>
</name>
<etal/>
</person-group> (<year>2020</year>). <article-title>Grasp55(-/-) mice display impaired fat absorption and resistance to high-fat diet-induced obesity</article-title>. <source>Nat. Commun.</source> <volume>11</volume>, <fpage>1418</fpage>. <pub-id pub-id-type="doi">10.1038/s41467-020-14912-x</pub-id>
</citation>
</ref>
<ref id="B119">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Kinseth</surname>
<given-names>M. A.</given-names>
</name>
<name>
<surname>Anjard</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Fuller</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Guizzunti</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Loomis</surname>
<given-names>W. F.</given-names>
</name>
<name>
<surname>Malhotra</surname>
<given-names>V.</given-names>
</name>
</person-group> (<year>2007</year>). <article-title>The Golgi-associated protein GRASP is required for unconventional protein secretion during development</article-title>. <source>Cell</source> <volume>130</volume>, <fpage>524</fpage>&#x2013;<lpage>534</lpage>. <pub-id pub-id-type="doi">10.1016/j.cell.2007.06.029</pub-id>
</citation>
</ref>
<ref id="B120">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Klumperman</surname>
<given-names>J.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>Architecture of the mammalian golgi</article-title>. <source>Cold Spring Harb. Perspect. Biol.</source> <volume>3</volume>, <fpage>0051811</fpage>&#x2013;<lpage>a5219</lpage>. <pub-id pub-id-type="doi">10.1101/cshperspect.a005181</pub-id>
</citation>
</ref>
<ref id="B121">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Kodani</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Sutterlin</surname>
<given-names>C.</given-names>
</name>
</person-group> (<year>2008</year>). <article-title>The Golgi protein GM130 regulates centrosome morphology and function</article-title>. <source>Mol. Biol. Cell</source> <volume>19</volume>, <fpage>745</fpage>&#x2013;<lpage>753</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.e07-08-0847</pub-id>
</citation>
</ref>
<ref id="B122">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Kondylis</surname>
<given-names>V.</given-names>
</name>
<name>
<surname>Spoorendonk</surname>
<given-names>K. M.</given-names>
</name>
<name>
<surname>Rabouille</surname>
<given-names>C.</given-names>
</name>
</person-group> (<year>2005</year>). <article-title>dGRASP localization and function in the early exocytic pathway in Drosophila S2 cells</article-title>. <source>Mol. Biol. Cell</source> <volume>16</volume>, <fpage>4061</fpage>&#x2013;<lpage>4072</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.e04-10-0938</pub-id>
</citation>
</ref>
<ref id="B123">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Krishnan</surname>
<given-names>V.</given-names>
</name>
<name>
<surname>Bane</surname>
<given-names>S. M.</given-names>
</name>
<name>
<surname>Kawle</surname>
<given-names>P. D.</given-names>
</name>
<name>
<surname>Naresh</surname>
<given-names>K. N.</given-names>
</name>
<name>
<surname>Kalraiya</surname>
<given-names>R. D.</given-names>
</name>
</person-group> (<year>2005</year>). <article-title>Altered melanoma cell surface glycosylation mediates organ specific adhesion and metastasis via lectin receptors on the lung vascular endothelium</article-title>. <source>Clin. Exp. Metastasis</source> <volume>22</volume>, <fpage>11</fpage>&#x2013;<lpage>24</lpage>. <pub-id pub-id-type="doi">10.1007/s10585-005-2036-2</pub-id>
</citation>
</ref>
<ref id="B124">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Kweon</surname>
<given-names>H. K.</given-names>
</name>
<name>
<surname>Kong</surname>
<given-names>A. T.</given-names>
</name>
<name>
<surname>Hersberger</surname>
<given-names>K. E.</given-names>
</name>
<name>
<surname>Huang</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Nesvizhskii</surname>
<given-names>A. I.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
<etal/>
</person-group> (<year>2024</year>). <article-title>Sulfoproteomics workflow with precursor ion accurate mass shift analysis reveals novel tyrosine sulfoproteins in the golgi</article-title>. <source>J. Proteome Res.</source> <volume>23</volume>, <fpage>71</fpage>&#x2013;<lpage>83</lpage>. <pub-id pub-id-type="doi">10.1021/acs.jproteome.3c00323</pub-id>
</citation>
</ref>
<ref id="B125">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Lamichhane</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Rocha Cabrero</surname>
<given-names>F.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>Metachromatic leukodystrophy</article-title>. <source>StatPearls. (Treasure Isl. (FL))</source>.</citation>
</ref>
<ref id="B126">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Lee</surname>
<given-names>H. J.</given-names>
</name>
<name>
<surname>Patel</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Lee</surname>
<given-names>S. J.</given-names>
</name>
</person-group> (<year>2005</year>). <article-title>Intravesicular localization and exocytosis of alpha-synuclein and its aggregates</article-title>. <source>J. Neurosci.</source> <volume>25</volume>, <fpage>6016</fpage>&#x2013;<lpage>6024</lpage>. <pub-id pub-id-type="doi">10.1523/JNEUROSCI.0692-05.2005</pub-id>
</citation>
</ref>
<ref id="B127">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Lee</surname>
<given-names>I.</given-names>
</name>
<name>
<surname>Tiwari</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Dunlop</surname>
<given-names>M. H.</given-names>
</name>
<name>
<surname>Graham</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Liu</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Rothman</surname>
<given-names>J. E.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>Membrane adhesion dictates Golgi stacking and cisternal morphology</article-title>. <source>Proc. Natl. Acad. Sci. U. S. A.</source> <volume>111</volume>, <fpage>1849</fpage>&#x2013;<lpage>1854</lpage>. <pub-id pub-id-type="doi">10.1073/pnas.1323895111</pub-id>
</citation>
</ref>
<ref id="B128">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Leeman</surname>
<given-names>D. S.</given-names>
</name>
<name>
<surname>Hebestreit</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Ruetz</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Webb</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Mckay</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Pollina</surname>
<given-names>E. A.</given-names>
</name>
<etal/>
</person-group> (<year>2018</year>). <article-title>Lysosome activation clears aggregates and enhances quiescent neural stem cell activation during aging</article-title>. <source>Science</source> <volume>359</volume>, <fpage>1277</fpage>&#x2013;<lpage>1283</lpage>. <pub-id pub-id-type="doi">10.1126/science.aag3048</pub-id>
</citation>
</ref>
<ref id="B129">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Lenders</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Brand</surname>
<given-names>E.</given-names>
</name>
</person-group> (<year>2021</year>). <article-title>Fabry disease: the current treatment landscape</article-title>. <source>Drugs</source> <volume>81</volume>, <fpage>635</fpage>&#x2013;<lpage>645</lpage>. <pub-id pub-id-type="doi">10.1007/s40265-021-01486-1</pub-id>
</citation>
</ref>
<ref id="B130">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Levine</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Kroemer</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2008</year>). <article-title>Autophagy in the pathogenesis of disease</article-title>. <source>Cell</source> <volume>132</volume>, <fpage>27</fpage>&#x2013;<lpage>42</lpage>. <pub-id pub-id-type="doi">10.1016/j.cell.2007.12.018</pub-id>
</citation>
</ref>
<ref id="B131">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Ahat</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2019a</year>). <article-title>Golgi structure and function in health, stress, and diseases</article-title>. <source>Results Probl. Cell Differ.</source> <volume>67</volume>, <fpage>441</fpage>&#x2013;<lpage>485</lpage>. <pub-id pub-id-type="doi">10.1007/978-3-030-23173-6_19</pub-id>
</citation>
</ref>
<ref id="B132">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Ireland</surname>
<given-names>S. C.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2019b</year>). <article-title>DjA1 maintains Golgi integrity via interaction with GRASP65</article-title>. <source>Mol. Biol. Cell</source> <volume>30</volume>, <fpage>478</fpage>&#x2013;<lpage>490</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.E18-10-0613</pub-id>
</citation>
</ref>
<ref id="B133">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Lin</surname>
<given-names>C. Y.</given-names>
</name>
<name>
<surname>Madsen</surname>
<given-names>M. L.</given-names>
</name>
<name>
<surname>Yarm</surname>
<given-names>F. R.</given-names>
</name>
<name>
<surname>Jang</surname>
<given-names>Y. J.</given-names>
</name>
<name>
<surname>Liu</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Erikson</surname>
<given-names>R. L.</given-names>
</name>
</person-group> (<year>2000</year>). <article-title>Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2</article-title>. <source>Proc. Natl. Acad. Sci. U. S. A.</source> <volume>97</volume>, <fpage>12589</fpage>&#x2013;<lpage>12594</lpage>. <pub-id pub-id-type="doi">10.1073/pnas.220423497</pub-id>
</citation>
</ref>
<ref id="B134">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Liu</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Coyne</surname>
<given-names>A. N.</given-names>
</name>
<name>
<surname>Pei</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Vaughan</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Chaung</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Zarnescu</surname>
<given-names>D. C.</given-names>
</name>
<etal/>
</person-group> (<year>2017</year>). <article-title>Endocytosis regulates TDP-43 toxicity and turnover</article-title>. <source>Nat. Commun.</source> <volume>8</volume>, <fpage>2092</fpage>. <pub-id pub-id-type="doi">10.1038/s41467-017-02017-x</pub-id>
</citation>
</ref>
<ref id="B135">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Lowe</surname>
<given-names>M.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>Structural organization of the Golgi apparatus</article-title>. <source>Curr. Opin. Cell Biol.</source> <volume>23</volume>, <fpage>85</fpage>&#x2013;<lpage>93</lpage>. <pub-id pub-id-type="doi">10.1016/j.ceb.2010.10.004</pub-id>
</citation>
</ref>
<ref id="B136">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Lowe</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Rabouille</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Nakamura</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Watson</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Jackman</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Jamsa</surname>
<given-names>E.</given-names>
</name>
<etal/>
</person-group> (<year>1998</year>). <article-title>Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis</article-title>. <source>Cell</source> <volume>94</volume>, <fpage>783</fpage>&#x2013;<lpage>793</lpage>. <pub-id pub-id-type="doi">10.1016/s0092-8674(00)81737-7</pub-id>
</citation>
</ref>
<ref id="B137">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Lubbehusen</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Thiel</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Rind</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Ungar</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Prinsen</surname>
<given-names>B. H.</given-names>
</name>
<name>
<surname>De Koning</surname>
<given-names>T. J.</given-names>
</name>
<etal/>
</person-group> (<year>2010</year>). <article-title>Fatal outcome due to deficiency of subunit 6 of the conserved oligomeric Golgi complex leading to a new type of congenital disorders of glycosylation</article-title>. <source>Hum. Mol. Genet.</source> <volume>19</volume>, <fpage>3623</fpage>&#x2013;<lpage>3633</lpage>. <pub-id pub-id-type="doi">10.1093/hmg/ddq278</pub-id>
</citation>
</ref>
<ref id="B138">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ludford</surname>
<given-names>R. J.</given-names>
</name>
</person-group> (<year>1924</year>). <article-title>The distribution of the cytoplasmic organs in transplantable tumour cells, with special reference to dictyokinesis</article-title>. <source>Proc. R. Soc. Lond.</source> <volume>97</volume>, <fpage>50</fpage>&#x2013;<lpage>60</lpage>.</citation>
</ref>
<ref id="B139">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Luk</surname>
<given-names>K. C.</given-names>
</name>
<name>
<surname>Song</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>O&#x27;brien</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Stieber</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Branch</surname>
<given-names>J. R.</given-names>
</name>
<name>
<surname>Brunden</surname>
<given-names>K. R.</given-names>
</name>
<etal/>
</person-group> (<year>2009</year>). <article-title>Exogenous alpha-synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells</article-title>. <source>Proc. Natl. Acad. Sci. U. S. A.</source> <volume>106</volume>, <fpage>20051</fpage>&#x2013;<lpage>20056</lpage>. <pub-id pub-id-type="doi">10.1073/pnas.0908005106</pub-id>
</citation>
</ref>
<ref id="B140">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Luzio</surname>
<given-names>J. P.</given-names>
</name>
<name>
<surname>Hackmann</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Dieckmann</surname>
<given-names>N. M.</given-names>
</name>
<name>
<surname>Griffiths</surname>
<given-names>G. M.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>The biogenesis of lysosomes and lysosome-related organelles</article-title>. <source>Cold Spring Harb. Perspect. Biol.</source> <volume>6</volume>, <fpage>a016840</fpage>. <pub-id pub-id-type="doi">10.1101/cshperspect.a016840</pub-id>
</citation>
</ref>
<ref id="B141">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Maccioni</surname>
<given-names>H. J.</given-names>
</name>
<name>
<surname>Quiroga</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Spessott</surname>
<given-names>W.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>Organization of the synthesis of glycolipid oligosaccharides in the Golgi complex</article-title>. <source>FEBS Lett.</source> <volume>585</volume>, <fpage>1691</fpage>&#x2013;<lpage>1698</lpage>. <pub-id pub-id-type="doi">10.1016/j.febslet.2011.03.030</pub-id>
</citation>
</ref>
<ref id="B142">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Machtel</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Boros</surname>
<given-names>F. A.</given-names>
</name>
<name>
<surname>Dobert</surname>
<given-names>J. P.</given-names>
</name>
<name>
<surname>Arnold</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Zunke</surname>
<given-names>F.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>From lysosomal storage disorders to Parkinson&#x27;s disease - challenges and opportunities</article-title>. <source>J. Mol. Biol.</source> <volume>435</volume>, <fpage>167932</fpage>. <pub-id pub-id-type="doi">10.1016/j.jmb.2022.167932</pub-id>
</citation>
</ref>
<ref id="B143">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Maldonado</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Brown</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Bayrd</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Pease</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>1966</year>). <article-title>Ultrastructure of the myeloma cell</article-title>. <source>Cancer</source> <volume>19</volume>, <fpage>1613</fpage>&#x2013;<lpage>1627</lpage>. <pub-id pub-id-type="doi">10.1002/1097-0142(196611)19:11&#x3c;1613::aid-cncr2820191127&#x3e;3.0.co;2-q</pub-id>
</citation>
</ref>
<ref id="B144">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Manjithaya</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Anjard</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Loomis</surname>
<given-names>W. F.</given-names>
</name>
<name>
<surname>Subramani</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>2010</year>). <article-title>Unconventional secretion of Pichia pastoris Acb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation</article-title>. <source>J. Cell Biol.</source> <volume>188</volume>, <fpage>537</fpage>&#x2013;<lpage>546</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.200911149</pub-id>
</citation>
</ref>
<ref id="B145">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Meena</surname>
<given-names>N. K.</given-names>
</name>
<name>
<surname>Raben</surname>
<given-names>N.</given-names>
</name>
</person-group> (<year>2020</year>). <article-title>Pompe disease: new developments in an old lysosomal storage disorder</article-title>. <source>Biomolecules</source> <volume>10</volume>, <fpage>1339</fpage>. <pub-id pub-id-type="doi">10.3390/biom10091339</pub-id>
</citation>
</ref>
<ref id="B146">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Mizuno</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Hattori</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Kitada</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Matsumine</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Mori</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Shimura</surname>
<given-names>H.</given-names>
</name>
<etal/>
</person-group> (<year>2001</year>). <article-title>Familial Parkinson&#x27;s disease. Alpha-synuclein and parkin</article-title>. <source>Adv. Neurol.</source> <volume>86</volume>, <fpage>13</fpage>&#x2013;<lpage>21</lpage>.</citation>
</ref>
<ref id="B147">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Mourelatos</surname>
<given-names>Z.</given-names>
</name>
<name>
<surname>Gonatas</surname>
<given-names>N. K.</given-names>
</name>
<name>
<surname>Stieber</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Gurney</surname>
<given-names>M. E.</given-names>
</name>
<name>
<surname>Dal Canto</surname>
<given-names>M. C.</given-names>
</name>
</person-group> (<year>1996</year>). <article-title>The Golgi apparatus of spinal cord motor neurons in transgenic mice expressing mutant Cu,Zn superoxide dismutase becomes fragmented in early, preclinical stages of the disease</article-title>. <source>Proc. Natl. Acad. Sci. U. S. A.</source> <volume>93</volume>, <fpage>5472</fpage>&#x2013;<lpage>5477</lpage>. <pub-id pub-id-type="doi">10.1073/pnas.93.11.5472</pub-id>
</citation>
</ref>
<ref id="B148">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Nakamura</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Rabouille</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Watson</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Nilsson</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Hui</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Slusarewicz</surname>
<given-names>P.</given-names>
</name>
<etal/>
</person-group> (<year>1995</year>). <article-title>Characterization of a cis-Golgi matrix protein, GM130</article-title>. <source>J. Cell Biol.</source> <volume>131</volume>, <fpage>1715</fpage>&#x2013;<lpage>1726</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.131.6.1715</pub-id>
</citation>
</ref>
<ref id="B149">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ng</surname>
<given-names>M. L.</given-names>
</name>
<name>
<surname>Tan</surname>
<given-names>S. H.</given-names>
</name>
<name>
<surname>See</surname>
<given-names>E. E.</given-names>
</name>
<name>
<surname>Ooi</surname>
<given-names>E. E.</given-names>
</name>
<name>
<surname>Ling</surname>
<given-names>A. E.</given-names>
</name>
</person-group> (<year>2003</year>). <article-title>Proliferative growth of SARS coronavirus in Vero E6 cells</article-title>. <source>J. Gen. Virol.</source> <volume>84</volume>, <fpage>3291</fpage>&#x2013;<lpage>3303</lpage>. <pub-id pub-id-type="doi">10.1099/vir.0.19505-0</pub-id>
</citation>
</ref>
<ref id="B150">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Nilsson</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Loganathan</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Sekiguchi</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Matsuba</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Hui</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Tsubuki</surname>
<given-names>S.</given-names>
</name>
<etal/>
</person-group> (<year>2013</year>). <article-title>A&#x3b2; secretion and plaque formation depend on autophagy</article-title>. <source>Cell Rep.</source> <volume>5</volume>, <fpage>61</fpage>&#x2013;<lpage>69</lpage>. <pub-id pub-id-type="doi">10.1016/j.celrep.2013.08.042</pub-id>
</citation>
</ref>
<ref id="B151">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Nixon</surname>
<given-names>R. A.</given-names>
</name>
</person-group> (<year>2007</year>). <article-title>Autophagy, amyloidogenesis and Alzheimer disease</article-title>. <source>J. Cell Sci.</source> <volume>120</volume>, <fpage>4081</fpage>&#x2013;<lpage>4091</lpage>. <pub-id pub-id-type="doi">10.1242/jcs.019265</pub-id>
</citation>
</ref>
<ref id="B152">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Nixon</surname>
<given-names>R. A.</given-names>
</name>
<name>
<surname>Wegiel</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Kumar</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Yu</surname>
<given-names>W. H.</given-names>
</name>
<name>
<surname>Peterhoff</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Cataldo</surname>
<given-names>A.</given-names>
</name>
<etal/>
</person-group> (<year>2005</year>). <article-title>Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study</article-title>. <source>J. Neuropathol. Exp. Neurol.</source> <volume>64</volume>, <fpage>113</fpage>&#x2013;<lpage>122</lpage>. <pub-id pub-id-type="doi">10.1093/jnen/64.2.113</pub-id>
</citation>
</ref>
<ref id="B153">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Nolfi</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Capone</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Rosati</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Della</surname>
<given-names>G. C.</given-names>
</name>
</person-group> (<year>2020</year>). <article-title>The alpha-1,2 fucosylated tubule system of DU145 prostate cancer cells is derived from a partially fragmented Golgi complex and its formation is actin-dependent</article-title>. <source>Exp. Cell Res.</source> <volume>396</volume>, <fpage>112324</fpage>. <pub-id pub-id-type="doi">10.1016/j.yexcr.2020.112324</pub-id>
</citation>
</ref>
<ref id="B154">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>North</surname>
<given-names>B. J.</given-names>
</name>
<name>
<surname>Marshall</surname>
<given-names>B. L.</given-names>
</name>
<name>
<surname>Borra</surname>
<given-names>M. T.</given-names>
</name>
<name>
<surname>Denu</surname>
<given-names>J. M.</given-names>
</name>
<name>
<surname>Verdin</surname>
<given-names>E.</given-names>
</name>
</person-group> (<year>2003</year>). <article-title>The human Sir2 ortholog, SIRT2, is an NAD&#x2b;-dependent tubulin deacetylase</article-title>. <source>Mol. Cell</source> <volume>11</volume>, <fpage>437</fpage>&#x2013;<lpage>444</lpage>. <pub-id pub-id-type="doi">10.1016/s1097-2765(03)00038-8</pub-id>
</citation>
</ref>
<ref id="B155">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Nuchel</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Ghatak</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Zuk</surname>
<given-names>A. V.</given-names>
</name>
<name>
<surname>Illerhaus</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Morgelin</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Schonborn</surname>
<given-names>K.</given-names>
</name>
<etal/>
</person-group> (<year>2018</year>). <article-title>TGFB1 is secreted through an unconventional pathway dependent on the autophagic machinery and cytoskeletal regulators</article-title>. <source>Autophagy</source> <volume>14</volume>, <fpage>465</fpage>&#x2013;<lpage>486</lpage>. <pub-id pub-id-type="doi">10.1080/15548627.2017.1422850</pub-id>
</citation>
</ref>
<ref id="B156">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Nuchel</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Tauber</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Nolte</surname>
<given-names>J. L.</given-names>
</name>
<name>
<surname>Morgelin</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Turk</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Eckes</surname>
<given-names>B.</given-names>
</name>
<etal/>
</person-group> (<year>2021</year>). <article-title>An mTORC1-GRASP55 signaling axis controls unconventional secretion to reshape the extracellular proteome upon stress</article-title>. <source>Mol. Cell</source> <volume>81</volume>, <fpage>3275</fpage>&#x2013;<lpage>3293.e12</lpage>. <pub-id pub-id-type="doi">10.1016/j.molcel.2021.06.017</pub-id>
</citation>
</ref>
<ref id="B157">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ono</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Hakomori</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>2004</year>). <article-title>Glycosylation defining cancer cell motility and invasiveness</article-title>. <source>Glycoconj J.</source> <volume>20</volume>, <fpage>71</fpage>&#x2013;<lpage>78</lpage>. <pub-id pub-id-type="doi">10.1023/B:GLYC.0000018019.22070.7d</pub-id>
</citation>
</ref>
<ref id="B158">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Oudshoorn</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Rijs</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Limpens</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Groen</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Koster</surname>
<given-names>A. J.</given-names>
</name>
<name>
<surname>Snijder</surname>
<given-names>E. J.</given-names>
</name>
<etal/>
</person-group> (<year>2017</year>). <article-title>Expression and cleavage of Middle East respiratory syndrome coronavirus nsp3-4 polyprotein induce the formation of double-membrane vesicles that mimic those associated with coronaviral RNA replication</article-title>. <source>mBio</source> <volume>8</volume>, <fpage>e01658</fpage>. <pub-id pub-id-type="doi">10.1128/mBio.01658-17</pub-id>
</citation>
</ref>
<ref id="B159">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Oussoren</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Van Eerd</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Murphy</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Lachmann</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Van Der Meijden</surname>
<given-names>J. C.</given-names>
</name>
<name>
<surname>Hoefsloot</surname>
<given-names>L. H.</given-names>
</name>
<etal/>
</person-group> (<year>2018</year>). <article-title>Mucolipidosis type III, a series of adult patients</article-title>. <source>J. Inherit. Metab. Dis.</source> <volume>41</volume>, <fpage>839</fpage>&#x2013;<lpage>848</lpage>. <pub-id pub-id-type="doi">10.1007/s10545-018-0186-z</pub-id>
</citation>
</ref>
<ref id="B160">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Palade</surname>
<given-names>G. E.</given-names>
</name>
<name>
<surname>Claude</surname>
<given-names>A.</given-names>
</name>
</person-group> (<year>1949</year>). <article-title>The nature of the Golgi apparatus; identification of the Golgi apparatus with a complex of myelin figures</article-title>. <source>J. Morphol.</source> <volume>85</volume>, <fpage>71</fpage>&#x2013;<lpage>111</lpage>. <pub-id pub-id-type="doi">10.1002/jmor.1050850104</pub-id>
</citation>
</ref>
<ref id="B161">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Pandithage</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Lilischkis</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Harting</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Wolf</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Jedamzik</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Luscher-Firzlaff</surname>
<given-names>J.</given-names>
</name>
<etal/>
</person-group> (<year>2008</year>). <article-title>The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility</article-title>. <source>J. Cell Biol.</source> <volume>180</volume>, <fpage>915</fpage>&#x2013;<lpage>929</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.200707126</pub-id>
</citation>
</ref>
<ref id="B162">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Parenti</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2009</year>). <article-title>Treating lysosomal storage diseases with pharmacological chaperones: from concept to clinics</article-title>. <source>EMBO Mol. Med.</source> <volume>1</volume>, <fpage>268</fpage>&#x2013;<lpage>279</lpage>. <pub-id pub-id-type="doi">10.1002/emmm.200900036</pub-id>
</citation>
</ref>
<ref id="B163">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Pechincha</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Groessl</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Kalis</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>De Almeida</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Zanotti</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Wittmann</surname>
<given-names>M.</given-names>
</name>
<etal/>
</person-group> (<year>2022</year>). <article-title>Lysosomal enzyme trafficking factor LYSET enables nutritional usage of extracellular proteins</article-title>. <source>Science</source> <volume>378</volume>, <fpage>eabn5637</fpage>. <pub-id pub-id-type="doi">10.1126/science.abn5637</pub-id>
</citation>
</ref>
<ref id="B164">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Petrosyan</surname>
<given-names>A.</given-names>
</name>
</person-group> (<year>2015</year>). <article-title>Onco-Golgi: is fragmentation a gate to cancer progression?</article-title> <source>Biochem. Mol. Biol. J.</source> <volume>1</volume>, <fpage>16</fpage>. <pub-id pub-id-type="doi">10.21767/2471-8084.100006</pub-id>
</citation>
</ref>
<ref id="B165">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Platt</surname>
<given-names>F. M.</given-names>
</name>
<name>
<surname>D&#x27;azzo</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Davidson</surname>
<given-names>B. L.</given-names>
</name>
<name>
<surname>Neufeld</surname>
<given-names>E. F.</given-names>
</name>
<name>
<surname>Tifft</surname>
<given-names>C. J.</given-names>
</name>
</person-group> (<year>2018</year>). <article-title>Lysosomal storage diseases</article-title>. <source>Nat. Rev. Dis. Prim.</source> <volume>4</volume>, <fpage>27</fpage>. <pub-id pub-id-type="doi">10.1038/s41572-018-0025-4</pub-id>
</citation>
</ref>
<ref id="B166">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Pohlmann</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Nagel</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Hille</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Wendland</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Waheed</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Braulke</surname>
<given-names>T.</given-names>
</name>
<etal/>
</person-group> (<year>1989</year>). <article-title>Mannose 6-phosphate specific receptors: structure and function</article-title>. <source>Biochem. Soc. Trans.</source> <volume>17</volume>, <fpage>15</fpage>&#x2013;<lpage>16</lpage>. <pub-id pub-id-type="doi">10.1042/bst0170015</pub-id>
</citation>
</ref>
<ref id="B167">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Pothukuchi</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Agliarulo</surname>
<given-names>I.</given-names>
</name>
<name>
<surname>Pirozzi</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Rizzo</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Russo</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Turacchio</surname>
<given-names>G.</given-names>
</name>
<etal/>
</person-group> (<year>2021</year>). <article-title>GRASP55 regulates intra-Golgi localization of glycosylation enzymes to control glycosphingolipid biosynthesis</article-title>. <source>EMBO J.</source> <volume>40</volume>, <fpage>e107766</fpage>. <pub-id pub-id-type="doi">10.15252/embj.2021107766</pub-id>
</citation>
</ref>
<ref id="B168">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Prabhu</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Burgos</surname>
<given-names>P. V.</given-names>
</name>
<name>
<surname>Schindler</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Farias</surname>
<given-names>G. G.</given-names>
</name>
<name>
<surname>Magadan</surname>
<given-names>J. G.</given-names>
</name>
<name>
<surname>Bonifacino</surname>
<given-names>J. S.</given-names>
</name>
</person-group> (<year>2012</year>). <article-title>Adaptor protein 2-mediated endocytosis of the &#x3b2;-secretase BACE1 is dispensable for amyloid precursor protein processing</article-title>. <source>Mol. Biol. Cell</source> <volume>23</volume>, <fpage>2339</fpage>&#x2013;<lpage>2351</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.E11-11-0944</pub-id>
</citation>
</ref>
<ref id="B169">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Quinville</surname>
<given-names>B. M.</given-names>
</name>
<name>
<surname>Deschenes</surname>
<given-names>N. M.</given-names>
</name>
<name>
<surname>Ryckman</surname>
<given-names>A. E.</given-names>
</name>
<name>
<surname>Walia</surname>
<given-names>J. S.</given-names>
</name>
</person-group> (<year>2021</year>). <article-title>A comprehensive review: sphingolipid metabolism and implications of disruption in sphingolipid homeostasis</article-title>. <source>Int. J. Mol. Sci.</source> <volume>22</volume>, <fpage>5793</fpage>. <pub-id pub-id-type="doi">10.3390/ijms22115793</pub-id>
</citation>
</ref>
<ref id="B170">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Rabouille</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Levine</surname>
<given-names>T. P.</given-names>
</name>
<name>
<surname>Peters</surname>
<given-names>J. M.</given-names>
</name>
<name>
<surname>Warren</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>1995</year>). <article-title>An NSF-like ATPase, p97, and NSF mediate cisternal regrowth from mitotic Golgi fragments</article-title>. <source>Cell</source> <volume>82</volume>, <fpage>905</fpage>&#x2013;<lpage>914</lpage>. <pub-id pub-id-type="doi">10.1016/0092-8674(95)90270-8</pub-id>
</citation>
</ref>
<ref id="B171">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Rabouille</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Linstedt</surname>
<given-names>A. D.</given-names>
</name>
</person-group> (<year>2016</year>). <article-title>GRASP: a multitasking tether</article-title>. <source>Front. Cell Dev. Biol.</source> <volume>4</volume>, <fpage>1</fpage>. <pub-id pub-id-type="doi">10.3389/fcell.2016.00001</pub-id>
</citation>
</ref>
<ref id="B172">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Rajan</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Housden</surname>
<given-names>B. E.</given-names>
</name>
<name>
<surname>Wirtz-Peitz</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Holderbaum</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Perrimon</surname>
<given-names>N.</given-names>
</name>
</person-group> (<year>2017</year>). <article-title>A mechanism coupling systemic energy sensing to adipokine secretion</article-title>. <source>Dev. Cell</source> <volume>43</volume>, <fpage>83</fpage>&#x2013;<lpage>98</lpage>. <pub-id pub-id-type="doi">10.1016/j.devcel.2017.09.007</pub-id>
</citation>
</ref>
<ref id="B173">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Rajkumar</surname>
<given-names>V.</given-names>
</name>
<name>
<surname>Dumpa</surname>
<given-names>V.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>Lysosomal storage disease</article-title>. <source>StatPearls. (Treasure Isl. (FL))</source>.</citation>
</ref>
<ref id="B174">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ramani</surname>
<given-names>P. K.</given-names>
</name>
<name>
<surname>Parayil Sankaran</surname>
<given-names>B.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>Tay-sachs disease</article-title>. <source>StatPearls. (Treasure Isl. (FL))</source>.</citation>
</ref>
<ref id="B175">
<citation citation-type="book">
<person-group person-group-type="author">
<name>
<surname>Rambourg</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Clermont</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>1997</year>). &#x201c;<article-title>Three-dimensional structure of the Golgi apparatus in mammalian cells</article-title>,&#x201d; in <source>The Golgi apparatus</source>. Editors <person-group person-group-type="editor">
<name>
<surname>Berger</surname>
<given-names>E. G.</given-names>
</name>
<name>
<surname>Roth</surname>
<given-names>J.</given-names>
</name>
</person-group> (<publisher-loc>Basel, Switzerland</publisher-loc>: <publisher-name>Birkhauser Verlag</publisher-name>), <fpage>37</fpage>&#x2013;<lpage>61</lpage>.</citation>
</ref>
<ref id="B176">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Rasool</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Malik</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Qazi</surname>
<given-names>A. M.</given-names>
</name>
<name>
<surname>Sheikh</surname>
<given-names>I. A.</given-names>
</name>
<name>
<surname>Manan</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Shaheen</surname>
<given-names>S.</given-names>
</name>
<etal/>
</person-group> (<year>2014</year>). <article-title>Current view from Alzheimer disease to type 2 diabetes mellitus</article-title>. <source>CNS Neurol. Disord. Drug Targets</source> <volume>13</volume>, <fpage>533</fpage>&#x2013;<lpage>542</lpage>. <pub-id pub-id-type="doi">10.2174/18715273113126660167</pub-id>
</citation>
</ref>
<ref id="B177">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ren</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2020</year>). <article-title>Autophagy and lysosome storage disorders</article-title>. <source>Adv. Exp. Med. Biol.</source> <volume>1207</volume>, <fpage>87</fpage>&#x2013;<lpage>102</lpage>. <pub-id pub-id-type="doi">10.1007/978-981-15-4272-5_5</pub-id>
</citation>
</ref>
<ref id="B178">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Reuser</surname>
<given-names>A. J.</given-names>
</name>
<name>
<surname>Kroos</surname>
<given-names>M. A.</given-names>
</name>
<name>
<surname>Hermans</surname>
<given-names>M. M.</given-names>
</name>
<name>
<surname>Bijvoet</surname>
<given-names>A. G.</given-names>
</name>
<name>
<surname>Verbeet</surname>
<given-names>M. P.</given-names>
</name>
<name>
<surname>Van Diggelen</surname>
<given-names>O. P.</given-names>
</name>
<etal/>
</person-group> (<year>1995</year>). <article-title>Glycogenosis type II (acid maltase deficiency)</article-title>. <source>Muscle Nerve Suppl.</source> <volume>3</volume>, <fpage>S61</fpage>&#x2013;<lpage>S69</lpage>. <pub-id pub-id-type="doi">10.1002/mus.880181414</pub-id>
</citation>
</ref>
<ref id="B179">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Richards</surname>
<given-names>C. M.</given-names>
</name>
<name>
<surname>Jabs</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Qiao</surname>
<given-names>W.</given-names>
</name>
<name>
<surname>Varanese</surname>
<given-names>L. D.</given-names>
</name>
<name>
<surname>Schweizer</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Mosen</surname>
<given-names>P. R.</given-names>
</name>
<etal/>
</person-group> (<year>2022</year>). <article-title>The human disease gene LYSET is essential for lysosomal enzyme transport and viral infection</article-title>. <source>Science</source> <volume>378</volume>, <fpage>eabn5648</fpage>. <pub-id pub-id-type="doi">10.1126/science.abn5648</pub-id>
</citation>
</ref>
<ref id="B180">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Robenek</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Schmitz</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>1991</year>). <article-title>Abnormal processing of Golgi elements and lysosomes in Tangier disease</article-title>. <source>Arterioscler. Thromb.</source> <volume>11</volume>, <fpage>1007</fpage>&#x2013;<lpage>1020</lpage>. <pub-id pub-id-type="doi">10.1161/01.atv.11.4.1007</pub-id>
</citation>
</ref>
<ref id="B181">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Roberts</surname>
<given-names>J. D.</given-names>
</name>
<name>
<surname>Klein</surname>
<given-names>J. L.</given-names>
</name>
<name>
<surname>Palmantier</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Dhume</surname>
<given-names>S. T.</given-names>
</name>
<name>
<surname>George</surname>
<given-names>M. D.</given-names>
</name>
<name>
<surname>Olden</surname>
<given-names>K.</given-names>
</name>
</person-group> (<year>1998</year>). <article-title>The role of protein glycosylation inhibitors in the prevention of metastasis and therapy of cancer</article-title>. <source>Cancer Detect Prev.</source> <volume>22</volume>, <fpage>455</fpage>&#x2013;<lpage>462</lpage>. <pub-id pub-id-type="doi">10.1046/j.1525-1500.1998.00054.x</pub-id>
</citation>
</ref>
<ref id="B182">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Root</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Merino</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Nuckols</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Johnson</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Kukar</surname>
<given-names>T.</given-names>
</name>
</person-group> (<year>2021</year>). <article-title>Lysosome dysfunction as a cause of neurodegenerative diseases: lessons from frontotemporal dementia and amyotrophic lateral sclerosis</article-title>. <source>Neurobiol. Dis.</source> <volume>154</volume>, <fpage>105360</fpage>. <pub-id pub-id-type="doi">10.1016/j.nbd.2021.105360</pub-id>
</citation>
</ref>
<ref id="B183">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ross</surname>
<given-names>C. A.</given-names>
</name>
<name>
<surname>Poirier</surname>
<given-names>M. A.</given-names>
</name>
</person-group> (<year>2004</year>). <article-title>Protein aggregation and neurodegenerative disease</article-title>. <source>Nat. Med.</source> <volume>10</volume> (<issue>Suppl. l</issue>), <fpage>S10</fpage>&#x2013;<lpage>S17</lpage>. <pub-id pub-id-type="doi">10.1038/nm1066</pub-id>
</citation>
</ref>
<ref id="B184">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Ruan</surname>
<given-names>Z.</given-names>
</name>
<name>
<surname>Ikezu</surname>
<given-names>T.</given-names>
</name>
</person-group> (<year>2019</year>). <article-title>Tau secretion</article-title>. <source>Adv. Exp. Med. Biol.</source> <volume>1184</volume>, <fpage>123</fpage>&#x2013;<lpage>134</lpage>. <pub-id pub-id-type="doi">10.1007/978-981-32-9358-8_11</pub-id>
</citation>
</ref>
<ref id="B185">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Rudolph</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Tsai</surname>
<given-names>M. C.</given-names>
</name>
<name>
<surname>Von Gersdorff</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Wadiche</surname>
<given-names>J. I.</given-names>
</name>
</person-group> (<year>2015</year>). <article-title>The ubiquitous nature of multivesicular release</article-title>. <source>Trends Neurosci.</source> <volume>38</volume>, <fpage>428</fpage>&#x2013;<lpage>438</lpage>. <pub-id pub-id-type="doi">10.1016/j.tins.2015.05.008</pub-id>
</citation>
</ref>
<ref id="B186">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Samie</surname>
<given-names>M. A.</given-names>
</name>
<name>
<surname>Xu</surname>
<given-names>H.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>Lysosomal exocytosis and lipid storage disorders</article-title>. <source>J. Lipid Res.</source> <volume>55</volume>, <fpage>995</fpage>&#x2013;<lpage>1009</lpage>. <pub-id pub-id-type="doi">10.1194/jlr.R046896</pub-id>
</citation>
</ref>
<ref id="B187">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Sanda</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Morrison</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Goldman</surname>
<given-names>R.</given-names>
</name>
</person-group> (<year>2021</year>). <article-title>N- and O-glycosylation of the SARS-CoV-2 spike protein</article-title>. <source>Anal. Chem.</source> <volume>93</volume>, <fpage>2003</fpage>&#x2013;<lpage>2009</lpage>. <pub-id pub-id-type="doi">10.1021/acs.analchem.0c03173</pub-id>
</citation>
</ref>
<ref id="B188">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Santos</surname>
<given-names>T. C.</given-names>
</name>
<name>
<surname>Wierda</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Broeke</surname>
<given-names>J. H.</given-names>
</name>
<name>
<surname>Toonen</surname>
<given-names>R. F.</given-names>
</name>
<name>
<surname>Verhage</surname>
<given-names>M.</given-names>
</name>
</person-group> (<year>2017</year>). <article-title>Early golgi abnormalities and neurodegeneration upon loss of presynaptic proteins munc18-1, syntaxin-1, or SNAP-25</article-title>. <source>J. Neurosci.</source> <volume>37</volume>, <fpage>4525</fpage>&#x2013;<lpage>4539</lpage>. <pub-id pub-id-type="doi">10.1523/JNEUROSCI.3352-16.2017</pub-id>
</citation>
</ref>
<ref id="B189">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Schotman</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Karhinen</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Rabouille</surname>
<given-names>C.</given-names>
</name>
</person-group> (<year>2008</year>). <article-title>dGRASP-mediated noncanonical integrin secretion is required for Drosophila epithelial remodeling</article-title>. <source>Dev. Cell</source> <volume>14</volume>, <fpage>171</fpage>&#x2013;<lpage>182</lpage>. <pub-id pub-id-type="doi">10.1016/j.devcel.2007.12.006</pub-id>
</citation>
</ref>
<ref id="B190">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Schulze</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Sandhoff</surname>
<given-names>K.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>Lysosomal lipid storage diseases</article-title>. <source>Cold Spring Harb. Perspect. Biol.</source> <volume>3</volume>, <fpage>a004804</fpage>. <pub-id pub-id-type="doi">10.1101/cshperspect.a004804</pub-id>
</citation>
</ref>
<ref id="B191">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Sewell</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Backstrom</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Dalziel</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Gschmeissner</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Karlsson</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Noll</surname>
<given-names>T.</given-names>
</name>
<etal/>
</person-group> (<year>2006</year>). <article-title>The ST6GalNAc-I sialyltransferase localizes throughout the Golgi and is responsible for the synthesis of the tumor-associated sialyl-Tn O-glycan in human breast cancer</article-title>. <source>J. Biol. Chem.</source> <volume>281</volume>, <fpage>3586</fpage>&#x2013;<lpage>3594</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M511826200</pub-id>
</citation>
</ref>
<ref id="B192">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Shang</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Wan</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Luo</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Ye</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Geng</surname>
<given-names>Q.</given-names>
</name>
<name>
<surname>Auerbach</surname>
<given-names>A.</given-names>
</name>
<etal/>
</person-group> (<year>2020</year>). <article-title>Cell entry mechanisms of SARS-CoV-2</article-title>. <source>Proc. Natl. Acad. Sci. U. S. A.</source> <volume>117</volume>, <fpage>11727</fpage>&#x2013;<lpage>11734</lpage>. <pub-id pub-id-type="doi">10.1073/pnas.2003138117</pub-id>
</citation>
</ref>
<ref id="B193">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Sheth</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Nair</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Jee</surname>
<given-names>B.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>Lysosomal storage disorders: from biology to the clinic with reference to India</article-title>. <source>Lancet Reg. Health Southeast Asia</source> <volume>9</volume>, <fpage>100108</fpage>. <pub-id pub-id-type="doi">10.1016/j.lansea.2022.100108</pub-id>
</citation>
</ref>
<ref id="B194">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Short</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Haas</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Barr</surname>
<given-names>F. A.</given-names>
</name>
</person-group> (<year>2005</year>). <article-title>Golgins and GTPases, giving identity and structure to the Golgi apparatus</article-title>. <source>Biochim. Biophys. Acta</source> <volume>1744</volume>, <fpage>383</fpage>&#x2013;<lpage>395</lpage>. <pub-id pub-id-type="doi">10.1016/j.bbamcr.2005.02.001</pub-id>
</citation>
</ref>
<ref id="B195">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Shorter</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Warren</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2002</year>). <article-title>Golgi architecture and inheritance</article-title>. <source>Annu. Rev. Cell Dev. Biol.</source> <volume>18</volume>, <fpage>379</fpage>&#x2013;<lpage>420</lpage>. <pub-id pub-id-type="doi">10.1146/annurev.cellbio.18.030602.133733</pub-id>
</citation>
</ref>
<ref id="B196">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Shorter</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Watson</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Giannakou</surname>
<given-names>M. E.</given-names>
</name>
<name>
<surname>Clarke</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Warren</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Barr</surname>
<given-names>F. A.</given-names>
</name>
</person-group> (<year>1999</year>). <article-title>GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system</article-title>. <source>EMBO J.</source> <volume>18</volume>, <fpage>4949</fpage>&#x2013;<lpage>4960</lpage>. <pub-id pub-id-type="doi">10.1093/emboj/18.18.4949</pub-id>
</citation>
</ref>
<ref id="B197">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Simons</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Ikonen</surname>
<given-names>E.</given-names>
</name>
</person-group> (<year>1997</year>). <article-title>Functional rafts in cell membranes</article-title>. <source>Nature</source> <volume>387</volume>, <fpage>569</fpage>&#x2013;<lpage>572</lpage>. <pub-id pub-id-type="doi">10.1038/42408</pub-id>
</citation>
</ref>
<ref id="B198">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Sipione</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Monyror</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Galleguillos</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Steinberg</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Kadam</surname>
<given-names>V.</given-names>
</name>
</person-group> (<year>2020</year>). <article-title>Gangliosides in the brain: physiology, pathophysiology and therapeutic applications</article-title>. <source>Front. Neurosci.</source> <volume>14</volume>, <fpage>572965</fpage>. <pub-id pub-id-type="doi">10.3389/fnins.2020.572965</pub-id>
</citation>
</ref>
<ref id="B199">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Slusarewicz</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Nilsson</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Hui</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Watson</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Warren</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>1994</year>). <article-title>Isolation of a matrix that binds medial Golgi enzymes</article-title>. <source>J. Cell Biol.</source> <volume>124</volume>, <fpage>405</fpage>&#x2013;<lpage>413</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.124.4.405</pub-id>
</citation>
</ref>
<ref id="B200">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Sly</surname>
<given-names>W. S.</given-names>
</name>
</person-group> (<year>2000</year>). <article-title>The missing link in lysosomal enzyme targeting</article-title>. <source>J. Clin. Invest.</source> <volume>105</volume>, <fpage>563</fpage>&#x2013;<lpage>564</lpage>. <pub-id pub-id-type="doi">10.1172/JCI9479</pub-id>
</citation>
</ref>
<ref id="B201">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Small</surname>
<given-names>S. A.</given-names>
</name>
<name>
<surname>Gandy</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>2006</year>). <article-title>Sorting through the cell biology of Alzheimer&#x27;s disease: intracellular pathways to pathogenesis</article-title>. <source>Neuron</source> <volume>52</volume>, <fpage>15</fpage>&#x2013;<lpage>31</lpage>. <pub-id pub-id-type="doi">10.1016/j.neuron.2006.09.001</pub-id>
</citation>
</ref>
<ref id="B202">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Stanley</surname>
<given-names>P.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>Golgi glycosylation</article-title>. <source>Cold Spring Harb. Perspect. Biol.</source> <volume>3</volume>, <fpage>a005199</fpage>. <pub-id pub-id-type="doi">10.1101/cshperspect.a005199</pub-id>
</citation>
</ref>
<ref id="B203">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Staudt</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Puissant</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Boonen</surname>
<given-names>M.</given-names>
</name>
</person-group> (<year>2016</year>). <article-title>Subcellular trafficking of mammalian lysosomal proteins: an extended view</article-title>. <source>Int. J. Mol. Sci.</source> <volume>18</volume>, <fpage>47</fpage>. <pub-id pub-id-type="doi">10.3390/ijms18010047</pub-id>
</citation>
</ref>
<ref id="B204">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Stefanis</surname>
<given-names>L.</given-names>
</name>
</person-group> (<year>2012</year>). <article-title>&#x3b1;-Synuclein in Parkinson&#x27;s disease</article-title>. <source>Cold Spring Harb. Perspect. Med.</source> <volume>2</volume>, <fpage>a009399</fpage>. <pub-id pub-id-type="doi">10.1101/cshperspect.a009399</pub-id>
</citation>
</ref>
<ref id="B205">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Stieber</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Mourelatos</surname>
<given-names>Z.</given-names>
</name>
<name>
<surname>Gonatas</surname>
<given-names>N. K.</given-names>
</name>
</person-group> (<year>1996</year>). <article-title>In Alzheimer&#x27;s disease the Golgi apparatus of a population of neurons without neurofibrillary tangles is fragmented and atrophic</article-title>. <source>Am. J. Pathol.</source> <volume>148</volume>, <fpage>415</fpage>&#x2013;<lpage>426</lpage>.</citation>
</ref>
<ref id="B206">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Stoka</surname>
<given-names>V.</given-names>
</name>
<name>
<surname>Vasiljeva</surname>
<given-names>O.</given-names>
</name>
<name>
<surname>Nakanishi</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Turk</surname>
<given-names>V.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>The role of cysteine protease cathepsins B, H, C, and X/Z in neurodegenerative diseases and cancer</article-title>. <source>Int. J. Mol. Sci.</source> <volume>24</volume>, <fpage>15613</fpage>. <pub-id pub-id-type="doi">10.3390/ijms242115613</pub-id>
</citation>
</ref>
<ref id="B207">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Suh</surname>
<given-names>Y. H.</given-names>
</name>
<name>
<surname>Checler</surname>
<given-names>F.</given-names>
</name>
</person-group> (<year>2002</year>). <article-title>Amyloid precursor protein, presenilins, and alpha-synuclein: molecular pathogenesis and pharmacological applications in Alzheimer&#x27;s disease</article-title>. <source>Pharmacol. Rev.</source> <volume>54</volume>, <fpage>469</fpage>&#x2013;<lpage>525</lpage>. <pub-id pub-id-type="doi">10.1124/pr.54.3.469</pub-id>
</citation>
</ref>
<ref id="B208">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Sun</surname>
<given-names>A.</given-names>
</name>
</person-group> (<year>2018</year>). <article-title>Lysosomal storage disease overview</article-title>. <source>Ann. Transl. Med.</source> <volume>6</volume>, <fpage>476</fpage>. <pub-id pub-id-type="doi">10.21037/atm.2018.11.39</pub-id>
</citation>
</ref>
<ref id="B209">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Sung</surname>
<given-names>J. Y.</given-names>
</name>
<name>
<surname>Kim</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Paik</surname>
<given-names>S. R.</given-names>
</name>
<name>
<surname>Park</surname>
<given-names>J. H.</given-names>
</name>
<name>
<surname>Ahn</surname>
<given-names>Y. S.</given-names>
</name>
<name>
<surname>Chung</surname>
<given-names>K. C.</given-names>
</name>
</person-group> (<year>2001</year>). <article-title>Induction of neuronal cell death by Rab5A-dependent endocytosis of alpha-synuclein</article-title>. <source>J. Biol. Chem.</source> <volume>276</volume>, <fpage>27441</fpage>&#x2013;<lpage>27448</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M101318200</pub-id>
</citation>
</ref>
<ref id="B210">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Sutterlin</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Polishchuk</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Pecot</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Malhotra</surname>
<given-names>V.</given-names>
</name>
</person-group> (<year>2005</year>). <article-title>The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division</article-title>. <source>Mol. Biol. Cell</source> <volume>16</volume>, <fpage>3211</fpage>&#x2013;<lpage>3222</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.e04-12-1065</pub-id>
</citation>
</ref>
<ref id="B211">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Takasugi</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Tomita</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Hayashi</surname>
<given-names>I.</given-names>
</name>
<name>
<surname>Tsuruoka</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Niimura</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Takahashi</surname>
<given-names>Y.</given-names>
</name>
<etal/>
</person-group> (<year>2003</year>). <article-title>The role of presenilin cofactors in the gamma-secretase complex</article-title>. <source>Nature</source> <volume>422</volume>, <fpage>438</fpage>&#x2013;<lpage>441</lpage>. <pub-id pub-id-type="doi">10.1038/nature01506</pub-id>
</citation>
</ref>
<ref id="B212">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tan</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Banerjee</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Guo</surname>
<given-names>H. F.</given-names>
</name>
<name>
<surname>Ireland</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Pankova</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Ahn</surname>
<given-names>Y. H.</given-names>
</name>
<etal/>
</person-group> (<year>2017a</year>). <article-title>Epithelial-to-mesenchymal transition drives a pro-metastatic Golgi compaction process through scaffolding protein PAQR11</article-title>. <source>J. Clin. Invest.</source> <volume>127</volume>, <fpage>117</fpage>&#x2013;<lpage>131</lpage>. <pub-id pub-id-type="doi">10.1172/JCI88736</pub-id>
</citation>
</ref>
<ref id="B213">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tan</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Shi</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Banerjee</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Liu</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Guo</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Yu</surname>
<given-names>J.</given-names>
</name>
<etal/>
</person-group> (<year>2021</year>). <article-title>A protumorigenic secretory pathway activated by p53 deficiency in lung adenocarcinoma</article-title>. <source>J. Clin. investigation</source> <volume>131</volume>, <fpage>e137186</fpage>. <pub-id pub-id-type="doi">10.1172/JCI137186</pub-id>
</citation>
</ref>
<ref id="B214">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tan</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>P</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Guo</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Ireland</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Pankova</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Ahn</surname>
<given-names>Y.</given-names>
</name>
<etal/>
</person-group> (<year>2017b</year>). <article-title>Epithelial-to-mesenchymal transition drives a pro-metastatic Golgi compaction process through scaffolding protein PAQR11</article-title>. <source>J. Clin. investigation</source> <volume>127</volume>, <fpage>117</fpage>&#x2013;<lpage>131</lpage>. <pub-id pub-id-type="doi">10.1172/JCI88736</pub-id>
</citation>
</ref>
<ref id="B215">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2013</year>). <article-title>Cell cycle regulation of Golgi membrane dynamics</article-title>. <source>Trends Cell Biol.</source> <volume>23</volume>, <fpage>296</fpage>&#x2013;<lpage>304</lpage>. <pub-id pub-id-type="doi">10.1016/j.tcb.2013.01.008</pub-id>
</citation>
</ref>
<ref id="B216">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Xiang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>De Renzis</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Rink</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Zheng</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Zerial</surname>
<given-names>M.</given-names>
</name>
<etal/>
</person-group> (<year>2011</year>). <article-title>The ubiquitin ligase HACE1 regulates Golgi membrane dynamics during the cell cycle</article-title>. <source>Nat. Commun.</source> <volume>2</volume>, <fpage>501</fpage>. <pub-id pub-id-type="doi">10.1038/ncomms1509</pub-id>
</citation>
</ref>
<ref id="B217">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Xiang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2010a</year>). <article-title>Reconstitution of the cell cycle-regulated Golgi disassembly and reassembly in a cell-free system</article-title>. <source>Nat. Protoc.</source> <volume>5</volume>, <fpage>758</fpage>&#x2013;<lpage>772</lpage>. <pub-id pub-id-type="doi">10.1038/nprot.2010.38</pub-id>
</citation>
</ref>
<ref id="B218">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Yuan</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Vielemeyer</surname>
<given-names>O.</given-names>
</name>
<name>
<surname>Perez</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2012</year>). <article-title>Sequential phosphorylation of GRASP65 during mitotic Golgi disassembly</article-title>. <source>Biol. Open</source> <volume>1</volume>, <fpage>1204</fpage>&#x2013;<lpage>1214</lpage>. <pub-id pub-id-type="doi">10.1242/bio.20122659</pub-id>
</citation>
</ref>
<ref id="B219">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Yuan</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2010b</year>). <article-title>The role of GRASP65 in Golgi cisternal stacking and cell cycle progression</article-title>. <source>Traffic</source> <volume>11</volume>, <fpage>827</fpage>&#x2013;<lpage>842</lpage>. <pub-id pub-id-type="doi">10.1111/j.1600-0854.2010.01055.x</pub-id>
</citation>
</ref>
<ref id="B220">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Huang</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Yuan</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2016</year>). <article-title>Mena-GRASP65 interaction couples actin polymerization to Golgi ribbon linking</article-title>. <source>Mol. Biol. Cell</source> <volume>27</volume>, <fpage>137</fpage>&#x2013;<lpage>152</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.E15-09-0650</pub-id>
</citation>
</ref>
<ref id="B221">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Taverna</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Cammarata</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Colomba</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Sciarrino</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Zizzo</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Francofonte</surname>
<given-names>D.</given-names>
</name>
<etal/>
</person-group> (<year>2020</year>). <article-title>Pompe disease: pathogenesis, molecular genetics and diagnosis</article-title>. <source>Aging (Albany NY)</source> <volume>12</volume>, <fpage>15856</fpage>&#x2013;<lpage>15874</lpage>. <pub-id pub-id-type="doi">10.18632/aging.103794</pub-id>
</citation>
</ref>
<ref id="B222">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Thinakaran</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Teplow</surname>
<given-names>D. B.</given-names>
</name>
<name>
<surname>Siman</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Greenberg</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Sisodia</surname>
<given-names>S. S.</given-names>
</name>
</person-group> (<year>1996</year>). <article-title>Metabolism of the "Swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "beta-secretase" site occurs in the golgi apparatus</article-title>. <source>J. Biol. Chem.</source> <volume>271</volume>, <fpage>9390</fpage>&#x2013;<lpage>9397</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.271.16.9390</pub-id>
</citation>
</ref>
<ref id="B223">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tian</surname>
<given-names>W.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Bai</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Yuan</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Xiao</surname>
<given-names>H.</given-names>
</name>
<etal/>
</person-group> (<year>2021</year>). <article-title>O-glycosylation pattern of the SARS-CoV-2 spike protein reveals an "O-Follow-N" rule</article-title>. <source>Cell Res.</source> <volume>31</volume>, <fpage>1123</fpage>&#x2013;<lpage>1125</lpage>. <pub-id pub-id-type="doi">10.1038/s41422-021-00545-2</pub-id>
</citation>
</ref>
<ref id="B224">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tomita</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Kirino</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Suzuki</surname>
<given-names>T.</given-names>
</name>
</person-group> (<year>1998</year>). <article-title>Cleavage of Alzheimer&#x27;s amyloid precursor protein (APP) by secretases occurs after O-glycosylation of APP in the protein secretory pathway. Identification of intracellular compartments in which APP cleavage occurs without using toxic agents that interfere with protein metabolism</article-title>. <source>J. Biol. Chem.</source> <volume>273</volume>, <fpage>6277</fpage>&#x2013;<lpage>6284</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.273.11.6277</pub-id>
</citation>
</ref>
<ref id="B225">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Tyler</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Johansson</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Karlsson</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Gudey</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Br&#xe4;nnstr&#xf6;m</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Grankvist</surname>
<given-names>K.</given-names>
</name>
<etal/>
</person-group> (<year>2015</year>). <article-title>Targeting glucosylceramide synthase induction of cell surface globotriaosylceramide (Gb3) in acquired cisplatin-resistance of lung cancer and malignant pleural mesothelioma cells</article-title>. <source>Exp. Cell Res.</source> <volume>336</volume>, <fpage>23</fpage>&#x2013;<lpage>32</lpage>. <pub-id pub-id-type="doi">10.1016/j.yexcr.2015.05.012</pub-id>
</citation>
</ref>
<ref id="B226">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Uchiyama</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Jokitalo</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Kano</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Murata</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Canas</surname>
<given-names>B.</given-names>
</name>
<etal/>
</person-group> (<year>2002</year>). <article-title>VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly <italic>in vivo</italic>
</article-title>. <source>J. Cell Biol.</source> <volume>159</volume>, <fpage>855</fpage>&#x2013;<lpage>866</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.200208112</pub-id>
</citation>
</ref>
<ref id="B227">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Udan-Johns</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Bengoechea</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Bell</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Shao</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Diamond</surname>
<given-names>M. I.</given-names>
</name>
<name>
<surname>True</surname>
<given-names>H. L.</given-names>
</name>
<etal/>
</person-group> (<year>2014</year>). <article-title>Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones</article-title>. <source>Hum. Mol. Genet.</source> <volume>23</volume>, <fpage>157</fpage>&#x2013;<lpage>170</lpage>. <pub-id pub-id-type="doi">10.1093/hmg/ddt408</pub-id>
</citation>
</ref>
<ref id="B228">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Udayar</surname>
<given-names>V.</given-names>
</name>
<name>
<surname>Chen</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Sidransky</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Jagasia</surname>
<given-names>R.</given-names>
</name>
</person-group> (<year>2022</year>). <article-title>Lysosomal dysfunction in neurodegeneration: emerging concepts and methods</article-title>. <source>Trends Neurosci.</source> <volume>45</volume>, <fpage>184</fpage>&#x2013;<lpage>199</lpage>. <pub-id pub-id-type="doi">10.1016/j.tins.2021.12.004</pub-id>
</citation>
</ref>
<ref id="B229">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Umeda</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Maekawa</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Kimura</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Takashima</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Tomiyama</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Mori</surname>
<given-names>H.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>Neurofibrillary tangle formation by introducing wild-type human tau into APP transgenic mice</article-title>. <source>Acta Neuropathol.</source> <volume>127</volume>, <fpage>685</fpage>&#x2013;<lpage>698</lpage>. <pub-id pub-id-type="doi">10.1007/s00401-014-1259-1</pub-id>
</citation>
</ref>
<ref id="B230">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Van Der Ploeg</surname>
<given-names>A. T.</given-names>
</name>
<name>
<surname>Reuser</surname>
<given-names>A. J.</given-names>
</name>
</person-group> (<year>2008</year>). <article-title>Pompe&#x27;s disease</article-title>. <source>Lancet</source> <volume>372</volume>, <fpage>1342</fpage>&#x2013;<lpage>1353</lpage>. <pub-id pub-id-type="doi">10.1016/S0140-6736(08)61555-X</pub-id>
</citation>
</ref>
<ref id="B231">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Veenendaal</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Jarvela</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Grieve</surname>
<given-names>A. G.</given-names>
</name>
<name>
<surname>Van Es</surname>
<given-names>J. H.</given-names>
</name>
<name>
<surname>Linstedt</surname>
<given-names>A. D.</given-names>
</name>
<name>
<surname>Rabouille</surname>
<given-names>C.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>GRASP65 controls the cis Golgi integrity <italic>in vivo</italic>
</article-title>. <source>Biol. Open</source> <volume>3</volume>, <fpage>431</fpage>&#x2013;<lpage>443</lpage>. <pub-id pub-id-type="doi">10.1242/bio.20147757</pub-id>
</citation>
</ref>
<ref id="B232">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Vellodi</surname>
<given-names>A.</given-names>
</name>
</person-group> (<year>2005</year>). <article-title>Lysosomal storage disorders</article-title>. <source>Br. J. Haematol.</source> <volume>128</volume>, <fpage>413</fpage>&#x2013;<lpage>431</lpage>. <pub-id pub-id-type="doi">10.1111/j.1365-2141.2004.05293.x</pub-id>
</citation>
</ref>
<ref id="B233">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Venkatarangan</surname>
<given-names>V.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>W.</given-names>
</name>
<name>
<surname>Yang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Thoene</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Hahn</surname>
<given-names>S. H.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>M.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>ER-associated degradation in cystinosis pathogenesis and the prospects of precision medicine</article-title>. <source>J. Clin. Invest.</source> <volume>133</volume>, <fpage>e169551</fpage>. <pub-id pub-id-type="doi">10.1172/JCI169551</pub-id>
</citation>
</ref>
<ref id="B234">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Vieira</surname>
<given-names>S. I.</given-names>
</name>
<name>
<surname>Rebelo</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Domingues</surname>
<given-names>S. C.</given-names>
</name>
<name>
<surname>Da Cruz E Silva</surname>
<given-names>E. F.</given-names>
</name>
<name>
<surname>Da Cruz E Silva</surname>
<given-names>O. A.</given-names>
</name>
</person-group> (<year>2009</year>). <article-title>S655 phosphorylation enhances APP secretory traffic</article-title>. <source>Mol. Cell Biochem.</source> <volume>328</volume>, <fpage>145</fpage>&#x2013;<lpage>154</lpage>. <pub-id pub-id-type="doi">10.1007/s11010-009-0084-7</pub-id>
</citation>
</ref>
<ref id="B235">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Vielemeyer</surname>
<given-names>O.</given-names>
</name>
<name>
<surname>Yuan</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Moutel</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Saint-Fort</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Nizak</surname>
<given-names>C.</given-names>
</name>
<etal/>
</person-group> (<year>2009</year>). <article-title>Direct selection of monoclonal phosphospecific antibodies without prior phosphoamino acid mapping</article-title>. <source>J. Biol. Chem.</source> <volume>284</volume>, <fpage>20791</fpage>&#x2013;<lpage>20795</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M109.008730</pub-id>
</citation>
</ref>
<ref id="B236">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>V&#x27;kovski</surname>
<given-names>P.</given-names>
</name>
<name>
<surname>Kratzel</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Steiner</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Stalder</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Thiel</surname>
<given-names>V.</given-names>
</name>
</person-group> (<year>2021</year>). <article-title>Coronavirus biology and replication: implications for SARS-CoV-2</article-title>. <source>Nat. Rev. Microbiol.</source> <volume>19</volume>, <fpage>155</fpage>&#x2013;<lpage>170</lpage>. <pub-id pub-id-type="doi">10.1038/s41579-020-00468-6</pub-id>
</citation>
</ref>
<ref id="B237">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Gandy</surname>
<given-names>S.</given-names>
</name>
</person-group> (<year>2022</year>). <article-title>The Golgi apparatus: site for convergence of COVID-19 brain fog and Alzheimer&#x27;s disease?</article-title> <source>Mol. Neurodegener.</source> <volume>17</volume>, <fpage>67</fpage>. <pub-id pub-id-type="doi">10.1186/s13024-022-00568-2</pub-id>
</citation>
</ref>
<ref id="B238">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Satoh</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Warren</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2005</year>). <article-title>Mapping the functional domains of the Golgi stacking factor GRASP65</article-title>. <source>J. Biol. Chem.</source> <volume>280</volume>, <fpage>4921</fpage>&#x2013;<lpage>4928</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M412407200</pub-id>
</citation>
</ref>
<ref id="B239">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Satoh</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Warren</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Meyer</surname>
<given-names>H. H.</given-names>
</name>
</person-group> (<year>2004</year>). <article-title>VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments</article-title>. <source>J. Cell Biol.</source> <volume>164</volume>, <fpage>973</fpage>&#x2013;<lpage>978</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.200401010</pub-id>
</citation>
</ref>
<ref id="B240">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Seemann</surname>
<given-names>J.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>Golgi biogenesis</article-title>. <source>Cold Spring Harb. Perspect. Biol.</source> <volume>3</volume>, <fpage>a005330</fpage>. <pub-id pub-id-type="doi">10.1101/cshperspect.a005330</pub-id>
</citation>
</ref>
<ref id="B241">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Seemann</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Pypaert</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Shorter</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Warren</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2003</year>). <article-title>A direct role for GRASP65 as a mitotically regulated Golgi stacking factor</article-title>. <source>EMBO J.</source> <volume>22</volume>, <fpage>3279</fpage>&#x2013;<lpage>3290</lpage>. <pub-id pub-id-type="doi">10.1093/emboj/cdg317</pub-id>
</citation>
</ref>
<ref id="B242">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Wei</surname>
<given-names>J. H.</given-names>
</name>
<name>
<surname>Bisel</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Tang</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Seemann</surname>
<given-names>J.</given-names>
</name>
</person-group> (<year>2008</year>). <article-title>Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport</article-title>. <source>PLoS One</source> <volume>3</volume>, <fpage>e1647</fpage>. <pub-id pub-id-type="doi">10.1371/journal.pone.0001647</pub-id>
</citation>
</ref>
<ref id="B243">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Wei</surname>
<given-names>J. H.</given-names>
</name>
<name>
<surname>Seemann</surname>
<given-names>J.</given-names>
</name>
</person-group> (<year>2010</year>). <article-title>Unraveling the golgi ribbon</article-title>. <source>Traffic</source> <volume>11</volume>, <fpage>1391</fpage>&#x2013;<lpage>1400</lpage>. <pub-id pub-id-type="doi">10.1111/j.1600-0854.2010.01114.x</pub-id>
</citation>
</ref>
<ref id="B244">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Wei</surname>
<given-names>J. H.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>Z. C.</given-names>
</name>
<name>
<surname>Wynn</surname>
<given-names>R. M.</given-names>
</name>
<name>
<surname>Seemann</surname>
<given-names>J.</given-names>
</name>
</person-group> (<year>2015</year>). <article-title>GM130 regulates golgi-derived spindle assembly by activating TPX2 and capturing microtubules</article-title>. <source>Cell</source> <volume>162</volume>, <fpage>287</fpage>&#x2013;<lpage>299</lpage>. <pub-id pub-id-type="doi">10.1016/j.cell.2015.06.014</pub-id>
</citation>
</ref>
<ref id="B245">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Wu</surname>
<given-names>C. C.</given-names>
</name>
<name>
<surname>Taylor</surname>
<given-names>R. S.</given-names>
</name>
<name>
<surname>Lane</surname>
<given-names>D. R.</given-names>
</name>
<name>
<surname>Ladinsky</surname>
<given-names>M. S.</given-names>
</name>
<name>
<surname>Weisz</surname>
<given-names>J. A.</given-names>
</name>
<name>
<surname>Howell</surname>
<given-names>K. E.</given-names>
</name>
</person-group> (<year>2000</year>). <article-title>GMx33: a novel family of trans-Golgi proteins identified by proteomics</article-title>. <source>Traffic</source> <volume>1</volume>, <fpage>963</fpage>&#x2013;<lpage>975</lpage>. <pub-id pub-id-type="doi">10.1034/j.1600-0854.2000.011206.x</pub-id>
</citation>
</ref>
<ref id="B246">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Wu</surname>
<given-names>L. G.</given-names>
</name>
<name>
<surname>Hamid</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Shin</surname>
<given-names>W.</given-names>
</name>
<name>
<surname>Chiang</surname>
<given-names>H. C.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>Exocytosis and endocytosis: modes, functions, and coupling mechanisms</article-title>. <source>Annu. Rev. Physiol.</source> <volume>76</volume>, <fpage>301</fpage>&#x2013;<lpage>331</lpage>. <pub-id pub-id-type="doi">10.1146/annurev-physiol-021113-170305</pub-id>
</citation>
</ref>
<ref id="B247">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Xiang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2010</year>). <article-title>GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking</article-title>. <source>J. Cell Biol.</source> <volume>188</volume>, <fpage>237</fpage>&#x2013;<lpage>251</lpage>. <pub-id pub-id-type="doi">10.1083/jcb.200907132</pub-id>
</citation>
</ref>
<ref id="B248">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Xiang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2011</year>). <article-title>New components of the Golgi matrix</article-title>. <source>Cell Tissue Res.</source> <volume>344</volume>, <fpage>365</fpage>&#x2013;<lpage>379</lpage>. <pub-id pub-id-type="doi">10.1007/s00441-011-1166-x</pub-id>
</citation>
</ref>
<ref id="B249">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Xiang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Nix</surname>
<given-names>D. B.</given-names>
</name>
<name>
<surname>Katoh</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Aoki</surname>
<given-names>K.</given-names>
</name>
<name>
<surname>Tiemeyer</surname>
<given-names>M.</given-names>
</name>
<etal/>
</person-group> (<year>2013</year>). <article-title>Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65</article-title>. <source>Nat. Commun.</source> <volume>4</volume>, <fpage>1659</fpage>. <pub-id pub-id-type="doi">10.1038/ncomms2669</pub-id>
</citation>
</ref>
<ref id="B250">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Yang</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>X.</given-names>
</name>
</person-group> (<year>2021</year>). <article-title>Lysosome biogenesis: regulation and functions</article-title>. <source>J. Cell Biol.</source> <volume>220</volume>, <fpage>e202102001</fpage>. <pub-id pub-id-type="doi">10.1083/jcb.202102001</pub-id>
</citation>
</ref>
<ref id="B251">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Yang</surname>
<given-names>D. S.</given-names>
</name>
<name>
<surname>Tandon</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Chen</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Yu</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Yu</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Arawaka</surname>
<given-names>S.</given-names>
</name>
<etal/>
</person-group> (<year>2002</year>). <article-title>Mature glycosylation and trafficking of nicastrin modulate its binding to presenilins</article-title>. <source>J. Biol. Chem.</source> <volume>277</volume>, <fpage>28135</fpage>&#x2013;<lpage>28142</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M110871200</pub-id>
</citation>
</ref>
<ref id="B252">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Yim</surname>
<given-names>W. W.</given-names>
</name>
<name>
<surname>Mizushima</surname>
<given-names>N.</given-names>
</name>
</person-group> (<year>2020</year>). <article-title>Lysosome biology in autophagy</article-title>. <source>Cell Discov.</source> <volume>6</volume>, <fpage>6</fpage>. <pub-id pub-id-type="doi">10.1038/s41421-020-0141-7</pub-id>
</citation>
</ref>
<ref id="B253">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Yin</surname>
<given-names>Z.</given-names>
</name>
<name>
<surname>Pascual</surname>
<given-names>C.</given-names>
</name>
<name>
<surname>Klionsky</surname>
<given-names>D. J.</given-names>
</name>
</person-group> (<year>2016</year>). <article-title>Autophagy: machinery and regulation</article-title>. <source>Microb. Cell</source> <volume>3</volume>, <fpage>588</fpage>&#x2013;<lpage>596</lpage>. <pub-id pub-id-type="doi">10.15698/mic2016.12.546</pub-id>
</citation>
</ref>
<ref id="B254">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Yoshimura</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Ihara</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Matsuzawa</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Taniguchi</surname>
<given-names>N.</given-names>
</name>
</person-group> (<year>1996</year>). <article-title>Aberrant glycosylation of E-cadherin enhances cell-cell binding to suppress metastasis</article-title>. <source>J. Biol. Chem.</source> <volume>271</volume>, <fpage>13811</fpage>&#x2013;<lpage>13815</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.271.23.13811</pub-id>
</citation>
</ref>
<ref id="B255">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Yuzwa</surname>
<given-names>S. A.</given-names>
</name>
<name>
<surname>Cheung</surname>
<given-names>A. H.</given-names>
</name>
<name>
<surname>Okon</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Mcintosh</surname>
<given-names>L. P.</given-names>
</name>
<name>
<surname>Vocadlo</surname>
<given-names>D. J.</given-names>
</name>
</person-group> (<year>2014a</year>). <article-title>O-GlcNAc modification of tau directly inhibits its aggregation without perturbing the conformational properties of tau monomers</article-title>. <source>J. Mol. Biol.</source> <volume>426</volume>, <fpage>1736</fpage>&#x2013;<lpage>1752</lpage>. <pub-id pub-id-type="doi">10.1016/j.jmb.2014.01.004</pub-id>
</citation>
</ref>
<ref id="B256">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Yuzwa</surname>
<given-names>S. A.</given-names>
</name>
<name>
<surname>Shan</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Jones</surname>
<given-names>B. A.</given-names>
</name>
<name>
<surname>Zhao</surname>
<given-names>G.</given-names>
</name>
<name>
<surname>Woodward</surname>
<given-names>M. L.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>X.</given-names>
</name>
<etal/>
</person-group> (<year>2014b</year>). <article-title>Pharmacological inhibition of O-GlcNAcase (OGA) prevents cognitive decline and amyloid plaque formation in bigenic tau/APP mutant mice</article-title>. <source>Mol. Neurodegener.</source> <volume>9</volume>, <fpage>42</fpage>. <pub-id pub-id-type="doi">10.1186/1750-1326-9-42</pub-id>
</citation>
</ref>
<ref id="B257">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Yuzwa</surname>
<given-names>S. A.</given-names>
</name>
<name>
<surname>Shan</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Macauley</surname>
<given-names>M. S.</given-names>
</name>
<name>
<surname>Clark</surname>
<given-names>T.</given-names>
</name>
<name>
<surname>Skorobogatko</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Vosseller</surname>
<given-names>K.</given-names>
</name>
<etal/>
</person-group> (<year>2012</year>). <article-title>Increasing O-GlcNAc slows neurodegeneration and stabilizes tau against aggregation</article-title>. <source>Nat. Chem. Biol.</source> <volume>8</volume>, <fpage>393</fpage>&#x2013;<lpage>399</lpage>. <pub-id pub-id-type="doi">10.1038/nchembio.797</pub-id>
</citation>
</ref>
<ref id="B258">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zachara</surname>
<given-names>N. E.</given-names>
</name>
<name>
<surname>O&#x27;donnell</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Cheung</surname>
<given-names>W. D.</given-names>
</name>
<name>
<surname>Mercer</surname>
<given-names>J. J.</given-names>
</name>
<name>
<surname>Marth</surname>
<given-names>J. D.</given-names>
</name>
<name>
<surname>Hart</surname>
<given-names>G. W.</given-names>
</name>
</person-group> (<year>2004</year>). <article-title>Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress. A survival response of mammalian cells</article-title>. <source>J. Biol. Chem.</source> <volume>279</volume>, <fpage>30133</fpage>&#x2013;<lpage>30142</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M403773200</pub-id>
</citation>
</ref>
<ref id="B259">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zaidi</surname>
<given-names>N.</given-names>
</name>
<name>
<surname>Maurer</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Nieke</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Kalbacher</surname>
<given-names>H.</given-names>
</name>
</person-group> (<year>2008</year>). <article-title>Cathepsin D: a cellular roadmap</article-title>. <source>Biochem. Biophys. Res. Commun.</source> <volume>376</volume>, <fpage>5</fpage>&#x2013;<lpage>9</lpage>. <pub-id pub-id-type="doi">10.1016/j.bbrc.2008.08.099</pub-id>
</citation>
</ref>
<ref id="B260">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zazhytska</surname>
<given-names>M.</given-names>
</name>
<name>
<surname>Kodra</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Hoagland</surname>
<given-names>D. A.</given-names>
</name>
<name>
<surname>Frere</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Fullard</surname>
<given-names>J. F.</given-names>
</name>
<name>
<surname>Shayya</surname>
<given-names>H.</given-names>
</name>
<etal/>
</person-group> (<year>2022</year>). <article-title>Non-cell-autonomous disruption of nuclear architecture as a potential cause of COVID-19-induced anosmia</article-title>. <source>Cell</source> <volume>185</volume>, <fpage>1052</fpage>&#x2013;<lpage>1064.e12</lpage>. <pub-id pub-id-type="doi">10.1016/j.cell.2022.01.024</pub-id>
</citation>
</ref>
<ref id="B261">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zeevaert</surname>
<given-names>R.</given-names>
</name>
<name>
<surname>Foulquier</surname>
<given-names>F.</given-names>
</name>
<name>
<surname>Jaeken</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Matthijs</surname>
<given-names>G.</given-names>
</name>
</person-group> (<year>2008</year>). <article-title>Deficiencies in subunits of the conserved oligomeric golgi (COG) complex define a novel group of congenital disorders of glycosylation</article-title>. <source>Mol. Genet. Metab.</source> <volume>93</volume>, <fpage>15</fpage>&#x2013;<lpage>21</lpage>. <pub-id pub-id-type="doi">10.1016/j.ymgme.2007.08.118</pub-id>
</citation>
</ref>
<ref id="B262">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zeidan</surname>
<given-names>Q.</given-names>
</name>
<name>
<surname>Hart</surname>
<given-names>G. W.</given-names>
</name>
</person-group> (<year>2010</year>). <article-title>The intersections between O-GlcNAcylation and phosphorylation: implications for multiple signaling pathways</article-title>. <source>J. Cell Sci.</source> <volume>123</volume>, <fpage>13</fpage>&#x2013;<lpage>22</lpage>. <pub-id pub-id-type="doi">10.1242/jcs.053678</pub-id>
</citation>
</ref>
<ref id="B263">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Kennedy</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Xing</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Bui</surname>
<given-names>S.</given-names>
</name>
<name>
<surname>Reid</surname>
<given-names>W.</given-names>
</name>
<name>
<surname>Joppich</surname>
<given-names>J.</given-names>
</name>
<etal/>
</person-group> (<year>2022a</year>). <article-title>SARS-CoV-2 triggers Golgi fragmentation via down-regulation of GRASP55 to facilitate viral trafficking</article-title>. <source>bioRxiv deposited</source>.</citation>
</ref>
<ref id="B264">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2024</year>). <article-title>Emerging roles of O-GlcNAcylation in protein trafficking and secretion</article-title>. <source>J. Biol. Chem.</source> <volume>105677</volume>. <pub-id pub-id-type="doi">10.1016/j.jbc.2024.105677</pub-id>
</citation>
</ref>
<ref id="B265">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>W.</given-names>
</name>
<name>
<surname>Yang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Yu</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>J.</given-names>
</name>
<etal/>
</person-group> (<year>2022b</year>). <article-title>GCAF(TMEM251) regulates lysosome biogenesis by activating the mannose-6-phosphate pathway</article-title>. <source>Nat. Commun.</source> <volume>13</volume>, <fpage>5351</fpage>. <pub-id pub-id-type="doi">10.1038/s41467-022-33025-1</pub-id>
</citation>
</ref>
<ref id="B266">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
</person-group> (<year>2021</year>). <article-title>Alterations of golgi structural proteins and glycosylation defects in cancer</article-title>. <source>Front. Cell Dev. Biol.</source> <volume>9</volume>, <fpage>665289</fpage>. <pub-id pub-id-type="doi">10.3389/fcell.2021.665289</pub-id>
</citation>
</ref>
<ref id="B267">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
</person-group> (<year>2023</year>). <article-title>Identification and characterization of GRASP55 O-GlcNAcylation</article-title>. <source>Methods Mol. Biol.</source> <volume>2557</volume>, <fpage>743</fpage>&#x2013;<lpage>753</lpage>. <pub-id pub-id-type="doi">10.1007/978-1-0716-2639-9_44</pub-id>
</citation>
</ref>
<ref id="B268">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Brachner</surname>
<given-names>A.</given-names>
</name>
<name>
<surname>Kukolj</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Slade</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2019a</year>). <article-title>SIRT2 deacetylates GRASP55 to facilitate post-mitotic Golgi assembly</article-title>. <source>J. Cell Sci.</source> <volume>132</volume>, <fpage>jcs232389</fpage>. <pub-id pub-id-type="doi">10.1242/jcs.232389</pub-id>
</citation>
</ref>
<ref id="B269">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Gui</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Bulfer</surname>
<given-names>S. L.</given-names>
</name>
<name>
<surname>Sanghez</surname>
<given-names>V.</given-names>
</name>
<name>
<surname>Wong</surname>
<given-names>D. E.</given-names>
</name>
<etal/>
</person-group> (<year>2015</year>). <article-title>Altered cofactor regulation with disease-associated p97/VCP mutations</article-title>. <source>Proc. Natl. Acad. Sci. U. S. A.</source> <volume>112</volume>, <fpage>E1705</fpage>&#x2013;<lpage>E1714</lpage>. <pub-id pub-id-type="doi">10.1073/pnas.1418820112</pub-id>
</citation>
</ref>
<ref id="B270">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Ireland</surname>
<given-names>S. C.</given-names>
</name>
<name>
<surname>Ahat</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Bekier</surname>
<given-names>M. E.</given-names>
</name>
<etal/>
</person-group> (<year>2019b</year>). <article-title>GORASP2/GRASP55 collaborates with the PtdIns3K UVRAG complex to facilitate autophagosome-lysosome fusion</article-title>. <source>Autophagy</source> <volume>15</volume>, <fpage>1787</fpage>&#x2013;<lpage>1800</lpage>. <pub-id pub-id-type="doi">10.1080/15548627.2019.1596480</pub-id>
</citation>
</ref>
<ref id="B271">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>L.</given-names>
</name>
<name>
<surname>Lak</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Jokitalo</surname>
<given-names>E.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2018</year>). <article-title>GRASP55 senses glucose deprivation through O-GlcNAcylation to promote autophagosome-lysosome fusion</article-title>. <source>Dev. Cell</source> <volume>45</volume>, <fpage>245</fpage>&#x2013;<lpage>261</lpage>. <pub-id pub-id-type="doi">10.1016/j.devcel.2018.03.023</pub-id>
</citation>
</ref>
<ref id="B272">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2015a</year>). <article-title>Cell cycle regulation of VCIP135 deubiquitinase activity and function in p97/p47-mediated Golgi reassembly</article-title>. <source>Mol. Biol. Cell</source> <volume>26</volume>, <fpage>2242</fpage>&#x2013;<lpage>2251</lpage>. <pub-id pub-id-type="doi">10.1091/mbc.E15-01-0041</pub-id>
</citation>
</ref>
<ref id="B273">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2015b</year>). <article-title>GRASPs in golgi structure and function</article-title>. <source>Front. Cell Dev. Biol.</source> <volume>3</volume>, <fpage>84</fpage>. <pub-id pub-id-type="doi">10.3389/fcell.2015.00084</pub-id>
</citation>
</ref>
<ref id="B274">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2016</year>). <article-title>Glycosylation quality control by the golgi structure</article-title>. <source>J. Mol. Biol.</source> <volume>428</volume>, <fpage>3183</fpage>&#x2013;<lpage>3193</lpage>. <pub-id pub-id-type="doi">10.1016/j.jmb.2016.02.030</pub-id>
</citation>
</ref>
<ref id="B275">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2018a</year>). <article-title>The Golgi stacking protein GORASP2/GRASP55 serves as an energy sensor to promote autophagosome maturation under glucose starvation</article-title>. <source>Autophagy</source> <volume>14</volume>, <fpage>1649</fpage>&#x2013;<lpage>1651</lpage>. <pub-id pub-id-type="doi">10.1080/15548627.2018.1491214</pub-id>
</citation>
</ref>
<ref id="B276">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2018b</year>). <article-title>GRASP55 facilitates autophagosome maturation under glucose deprivation</article-title>. <source>Mol. Cell Oncol.</source> <volume>5</volume>, <fpage>e1494948</fpage>. <pub-id pub-id-type="doi">10.1080/23723556.2018.1494948</pub-id>
</citation>
</ref>
<ref id="B277">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2020a</year>). <article-title>Non-redundant roles of GRASP55 and GRASP65 in the Golgi apparatus and beyond</article-title>. <source>Trends Biochem. Sci.</source> <volume>45</volume>, <fpage>1065</fpage>&#x2013;<lpage>1079</lpage>. <pub-id pub-id-type="doi">10.1016/j.tibs.2020.08.001</pub-id>
</citation>
</ref>
<ref id="B278">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2020b</year>). <article-title>Nonredundant roles of GRASP55 and GRASP65 in the golgi apparatus and beyond</article-title>. <source>Trends Biochem. Sci.</source> <volume>45</volume>, <fpage>1065</fpage>&#x2013;<lpage>1079</lpage>. <pub-id pub-id-type="doi">10.1016/j.tibs.2020.08.001</pub-id>
</citation>
</ref>
<ref id="B279">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Zhang</surname>
<given-names>H.</given-names>
</name>
<name>
<surname>Wang</surname>
<given-names>Y.</given-names>
</name>
</person-group> (<year>2014</year>). <article-title>Phosphorylation regulates VCIP135 function in Golgi membrane fusion during the cell cycle</article-title>. <source>J. Cell Sci.</source> <volume>127</volume>, <fpage>172</fpage>&#x2013;<lpage>181</lpage>. <pub-id pub-id-type="doi">10.1242/jcs.134668</pub-id>
</citation>
</ref>
<ref id="B280">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhang</surname>
<given-names>Y.</given-names>
</name>
<name>
<surname>Seemann</surname>
<given-names>J.</given-names>
</name>
</person-group> (<year>2021</year>). <article-title>Rapid degradation of GRASP55 and GRASP65 reveals their immediate impact on the Golgi structure</article-title>. <source>J. Cell Biol.</source> <volume>220</volume>, <fpage>e202007052</fpage>. <pub-id pub-id-type="doi">10.1083/jcb.202007052</pub-id>
</citation>
</ref>
<ref id="B281">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhao</surname>
<given-names>J.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>B.</given-names>
</name>
<name>
<surname>Huang</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Morelli</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Shi</surname>
<given-names>N.</given-names>
</name>
</person-group> (<year>2017</year>). <article-title>Structural basis for the interaction between golgi reassembly-stacking protein GRASP55 and Golgin45</article-title>. <source>J. Biol. Chem.</source> <volume>292</volume>, <fpage>2956</fpage>&#x2013;<lpage>2965</lpage>. <pub-id pub-id-type="doi">10.1074/jbc.M116.765990</pub-id>
</citation>
</ref>
<ref id="B282">
<citation citation-type="journal">
<person-group person-group-type="author">
<name>
<surname>Zhuo</surname>
<given-names>D.</given-names>
</name>
<name>
<surname>Li</surname>
<given-names>X.</given-names>
</name>
<name>
<surname>Guan</surname>
<given-names>F.</given-names>
</name>
</person-group> (<year>2018</year>). <article-title>Biological roles of aberrantly expressed glycosphingolipids and related enzymes in human cancer development and progression</article-title>. <source>Front. Physiol.</source> <volume>9</volume>, <fpage>466</fpage>. <pub-id pub-id-type="doi">10.3389/fphys.2018.00466</pub-id>
</citation>
</ref>
</ref-list>
</back>
</article>