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<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">790117</article-id>
<article-id pub-id-type="doi">10.3389/fcell.2021.790117</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>A Glimpse of Programmed Cell Death Among Bacteria, Animals, and Plants</article-title>
<alt-title alt-title-type="left-running-head">Zhuang et&#x20;al.</alt-title>
<alt-title alt-title-type="right-running-head">Conserved PCD in Living Organisms</alt-title>
</title-group>
<contrib-group>
<contrib contrib-type="author" corresp="yes">
<name>
<surname>Zhuang</surname>
<given-names>Jun</given-names>
</name>
<xref ref-type="aff" rid="aff1">
<sup>1</sup>
</xref>
<xref ref-type="aff" rid="aff2">
<sup>2</sup>
</xref>
<xref ref-type="corresp" rid="c001">&#x2a;</xref>
<uri xlink:href="https://loop.frontiersin.org/people/599319/overview"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Xie</surname>
<given-names>Li</given-names>
</name>
<xref ref-type="aff" rid="aff1">
<sup>1</sup>
</xref>
<xref ref-type="aff" rid="aff2">
<sup>2</sup>
</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Zheng</surname>
<given-names>Luping</given-names>
</name>
<xref ref-type="aff" rid="aff1">
<sup>1</sup>
</xref>
<xref ref-type="aff" rid="aff2">
<sup>2</sup>
</xref>
</contrib>
</contrib-group>
<aff id="aff1">
<sup>1</sup>
<institution>State Key Laboratory of Ecological Pest Control for Fujian and Taiwan Crops, Fujian Agriculture and Forestry University</institution>, <addr-line>Fuzhou</addr-line>, <country>China</country>
</aff>
<aff id="aff2">
<sup>2</sup>
<institution>Institute of Plant Virology, Fujian Agriculture and Forestry University</institution>, <addr-line>Fuzhou</addr-line>, <country>China</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/439013/overview">Shuai Jiang</ext-link>, Institute of Oceanology, Chinese Academy of Sciences (CAS), China</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/32843/overview">Jens Staal</ext-link>, Ghent University, Belgium</p>
<p>
<ext-link ext-link-type="uri" xlink:href="https://loop.frontiersin.org/people/281630/overview">Faheem Ahmed Khan</ext-link>, Huazhong Agricultural University, China</p>
</fn>
<corresp id="c001">&#x2a;Correspondence: Jun Zhuang, <email>fafuzj@126.com</email>
</corresp>
<fn fn-type="other">
<p>This article was submitted to Cell Death and Survival, a section of the journal Frontiers in Cell and Developmental Biology</p>
</fn>
</author-notes>
<pub-date pub-type="epub">
<day>10</day>
<month>02</month>
<year>2022</year>
</pub-date>
<pub-date pub-type="collection">
<year>2021</year>
</pub-date>
<volume>9</volume>
<elocation-id>790117</elocation-id>
<history>
<date date-type="received">
<day>06</day>
<month>10</month>
<year>2021</year>
</date>
<date date-type="accepted">
<day>24</day>
<month>11</month>
<year>2021</year>
</date>
</history>
<permissions>
<copyright-statement>Copyright &#xa9; 2022 Zhuang, Xie and Zheng.</copyright-statement>
<copyright-year>2022</copyright-year>
<copyright-holder>Zhuang, Xie and Zheng</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&#x20;terms.</p>
</license>
</permissions>
<abstract>
<p>Programmed cell death (PCD) in animals mainly refers to lytic and non-lytic forms. Disruption and integrity of the plasma membrane are considered as hallmarks of lytic and apoptotic cell death, respectively. These lytic cell death programs can prevent the hosts from microbial pathogens. The key to our understanding of these cases is pattern recognition receptors, such as TLRs in animals and LRR-RLKs in plants, and nod-like receptors (NLRs). Herein, we emphatically discuss the biochemical and structural studies that have clarified the anti-apoptotic and pro-apoptotic functions of Bcl-2 family proteins during intrinsic apoptosis and how caspase-8 among apoptosis, necroptosis, and pyroptosis sets the switchable threshold and integrates innate immune signaling, and that have compared the similarity and distinctness of the apoptosome, necroptosome, and inflammasome. We recapitulate that the necroptotic MLKL pore, pyroptotic gasdermin pore, HR-inducing resistosome, and mitochondrial Bcl-2 family all can form ion channels, which all directly boost membrane disruption. Comparing the conservation and unique aspects of PCD including ferrroptosis among bacteria, animals, and plants, the commonly shared immune domains including TIR-like, gasdermin-like, caspase-like, and MLKL/CC-like domains act as arsenal modules to restructure the diverse architecture to commit PCD suicide upon stresses/stimuli for host community.</p>
</abstract>
<kwd-group>
<kwd>pyroptosis</kwd>
<kwd>necroptosis</kwd>
<kwd>apoptosis</kwd>
<kwd>hypersensitive cell death response</kwd>
<kwd>ferroptosis</kwd>
<kwd>bacterial PCD</kwd>
</kwd-group>
</article-meta>
</front>
<body>
<sec id="s1">
<title>Introduction</title>
<p>Programmed cell death (PCD) is clearly characterized in animals and contains several types. Of PCDs, apoptosis is required for tissue development, maintenance of the homeostasis of proliferating cells, and multicellular morphogenesis in plants and animals. The conceptual proposal of apoptosis started from 1965 (<xref ref-type="bibr" rid="B60">Kerr, 1965</xref>). Australian scientists discovered that some scattered dead cells from the liver parenchyma were present when observed under an electron microscope after ligation of the rat portal vein. The lysosomes from these cells seemed not to be damaged and were kept in an intact situation. These cells, featured by morphological shrinkage and chromatin aggregations, fall off from their surrounding tissues and were ultimately engulfed. Kerr and other three scientists formally put forward the concept of apoptosis in 1972&#x20;(<xref ref-type="bibr" rid="B61">Kerr et&#x20;al., 1972</xref>). The molecular progresses on apoptosis <italic>per se</italic> began with a good model organism <italic>Caenorhabditis elegans</italic>. Sydney Brenner first determined the <italic>C. elegans</italic> cell development lineage (<xref ref-type="bibr" rid="B10">Brenner, 1973</xref>). John Sulston discovered the specific cell division and differentiation during the nematode developmental process and identified that nematode apoptosis is dictated by alternate gene expressions. Robert Horvitz found more than 20 genes regulating apoptosis (<xref ref-type="bibr" rid="B64">Lettre and Hengartner, 2006</xref>; <xref ref-type="bibr" rid="B25">Ellis and Horvitz, 1986</xref>). These come in (at least) two distinct flavors, containing either ones responsible for initiating or executing cell death or others involved in inhibition of cell death. The four genes that regulate all somatic cell deaths in <italic>C. elegans</italic> are <italic>CED-3</italic>, <italic>CED-4</italic>, <italic>CED-9</italic>, and <italic>EGL-1</italic> genes. CED-9 is an anti-apoptotic Bcl-2 homolog with four Bcl-2 homology (BH) domains, whereas&#x20;EGL-1 acts as a pro-apoptotic BH3-only domain protein (<xref ref-type="bibr" rid="B39">Hengartner et&#x20;al., 1992</xref>) (<xref ref-type="fig" rid="F1">Figure&#x20;1A</xref>); CED-3 and CED-4 are pro-apoptotic (<xref ref-type="bibr" rid="B64">Lettre and Hengartner, 2006</xref>). CED-3 is homologous to mammalian caspases (cysteinyl aspartic acid&#x2013;specific proteases) formerly known as interleukin-1B&#x2013;converting enzyme in animals (<xref ref-type="bibr" rid="B123">Yuan et&#x20;al., 1993</xref>), and CED-4 is an adaptor protein that is orthologous to mammalian apoptotic protease&#x2013;activating factor-1 (Apaf-1)&#x20;being the main scaffold protein of apoptosome for caspase-9 activation in the intrinsic pathway (<xref ref-type="bibr" rid="B64">Lettre and Hengartner, 2006</xref>) (<xref ref-type="fig" rid="F1">Figure&#x20;1A</xref>). Although the three conserved gene-encoding proteins regulate apoptosis in animals, no corresponding orthologous proteins have been found in plants.</p>
<fig id="F1" position="float">
<label>FIGURE 1</label>
<caption>
<p>Structural features of caspases, Apaf-1, and the Bcl-2 family. <bold>(A)</bold> Master initiator caspases, caspase-2, caspase-8, and caspase-9, are characterized by N-terminal domain(s) including DED or CARD. The effector caspases have caspase-3, caspase-6, and caspase-7 for apoptosis. Apaf-1 is a main scaffold protein for recruitment of Cyt c and caspase-9. Bcl-2 itself plays anti-apoptotic roles whereas the Bax/Bak members of the Bcl-2 family are pro-apoptotic. BH3-only protein is an intrinsic apoptosis initiator. <bold>(B)</bold> Another clade contains inflammatory caspases, including human caspase-1, -4, and -5 and mouse caspase-11, have the N-terminal CARD domains.</p>
</caption>
<graphic xlink:href="fcell-09-790117-g001.tif"/>
</fig>
<sec id="s1-1">
<title>Mammalian Apoptosis Mediated by Caspases</title>
<p>During the process of apoptosis, the central hub is the activation of caspases. Human caspases have 11 members and are categorized into 3 subclasses (<xref ref-type="fig" rid="F1">Figures 1A,B</xref>). Different clades largely correspond to distinct physiological functions. Not all caspases are involved in apoptotic regulation, <italic>albeit</italic> caspases dictate the destiny of apoptotic cells. Caspase-2, -8, -9, and -10 are involved in the initiation of apoptosis (as initiators). Upon dimerization, procaspase-2 becomes active and can process cytosolic Bid to trigger the release of Cyt c (<xref ref-type="bibr" rid="B3">Baliga et&#x20;al., 2004</xref>; <xref ref-type="bibr" rid="B32">Guo et&#x20;al., 2002</xref>); caspase-8 and caspase-9 individually initiate the extrinsic and intrinsic mammalian apoptosis (<xref ref-type="bibr" rid="B14">Chai and Shi, 2014</xref>), or caspase-8 has an N-terminal tandem death effector domain (DED) and is coordinated with the death receptor TNFR for perception of extracellular death signals. Hence, recruitment of caspase-8 forms a death-inducing signaling complex (DISC) and then activates caspase-8 (<xref ref-type="bibr" rid="B90">Schleich et&#x20;al., 2013</xref>). The Apaf-1 apoptosome assembles into a heptameric wheel-like complex with cytochrome c (Cyt c) and caspase-9 having the N-terminal caspase recruitment domain (CARD) (<xref ref-type="bibr" rid="B65">Li et&#x20;al., 1998</xref>). The dome of apoptosome was identified to be the oligomer of CARDs from Apaf-1 and caspase-9 (7:3-4 stoichiometry); then, procaspase-9 undergoes conversion into caspase-9 (<xref ref-type="fig" rid="F2">Figure&#x20;2A</xref>). However, the DARK-DRONC apoptosome (8:8 stoichiometry) complex found in flies and the <italic>C. elegans</italic> octameric CED-4 apoptosome interacting with CED-3 (8:2 stoichiometry) does not require cytochrome c to assemble, as it does in humans. This activating ligand Cyt c for Apaf-1 can be released from the perforated mitochondria by pro-death Bad/Bax, which is being initiated <italic>via</italic> activation of Bid by caspase-8 (<xref ref-type="bibr" rid="B65">Li et&#x20;al., 1998</xref>; <xref ref-type="bibr" rid="B2">Antignani and Youle, 2006</xref>). The plasma membrane of apoptotic cells keeps basically intact; however, the perforated mitochondrial outer membrane by Bax/Bak alternates the mitochondrial outer membrane permeabilization (MOMP) during intrinsic apoptosis. Then, endonuclease G (Endo G) is released from the disrupted mitochondria and enters the nucleus, resulting in DNA cleavage to form DNA ladders, which can also be contributed by DNase <italic>&#x3b3;</italic> (<xref ref-type="bibr" rid="B66">Li et&#x20;al., 2001</xref>; Shiokawa et&#x20;al., 2002). Additionally, the active caspase-8 sequentially activates effector caspase(s) (<xref ref-type="bibr" rid="B99">Stennicke et&#x20;al., 1998</xref>). The activated caspase-3 and -7 have similar cleavage profiles of substrates. The degradations of poly (ADP-ribose) polymerase (PARP) and DNA fragmentation factor-45 (DFF-45) by caspase-3 and caspase-7 give rise to failures in DNA repair and initiation of DNA degradation (<xref ref-type="bibr" rid="B46">J&#xe4;nicke et&#x20;al., 1998</xref>; <xref ref-type="bibr" rid="B105">Tang and Kidd, 1998</xref>; <xref ref-type="bibr" rid="B116">Wride et&#x20;al., 1999</xref>). The lamin A critical for nuclear architecture acts as the substrate of activated caspase-6 (<xref ref-type="bibr" rid="B87">Ruchaud et&#x20;al., 2002</xref>). Degraded lamin A and other cellular skeletal proteins lead to cellular shrinkages and chromatin condensations. However, the cytokines cannot leak out from apoptotic cells to the bystander cells due to the integrity of the plasma membrane during apoptosis genesis. Therefore, apoptosis without the release of cytokines cannot sequentially induce inflammation.</p>
<fig id="F2" position="float">
<label>FIGURE 2</label>
<caption>
<p>Commonality of various PCDs among bacteria, animals, and plants. <bold>(A)</bold> Necroptosis is mediated by RIPK3-phosphorylated MLKL. The oligomerization of the 4-helice bundle in the N-terminal region of MLKL should form a cation channel in the plasma membrane and lead to disruption of membrane integrity. Inflammatory caspases were activated by canonical and/or non-canonical inflammosomes. The active inflammatory caspases can cleave gasdermins. The resulting N-gasdermins insert the plasma membrane and form a membrane pore with 18&#x2013;21&#xa0;nm in inner diameter. The gasdermin pore prefers the release of IL-1&#x3b2; and IL-18. Apoptosis is a non-lytic cell death. In the instinct pathway, the initiator caspase-9 is activated by the apoptosome consisting of apaf-1, Cyt c, and caspase-9; caspase-8 is activated by the death-inducing signaling complex (DISC) for extrinsic apoptosis. Caspase-8 is the molecular switch for apoptosis, for necroptosis, and pyroptosis. Ferroptosis is required for iron and is mediated by LOXs and ROS and POR and Cyt b. The lipid peroxides and lipid radicals are capable of being sequestered by GPX4 and FSP1, respectively. Upon infection, PANoptosis co-featured by pyroptosis, apoptosis, and necroptosis is present as well. <bold>(B)</bold> The bacterial gasdermins are conserved and commit cell death <italic>via</italic> pore-forming as well. cGAMP as the elicitor activates the phospholipase, which perturb membrane integrity and result in cell death. gRAMP, the giant repeat&#x2013;associated mysterious protein from CRISPR-Cas type III effectors; TPR-CHAT, caspase HetF associated with the tetratricopeptide repeat. proteases <bold>(C)</bold> Resistance (R) protein-mediated HR and ferroptosis-like in the plant cell. The R protein ZAR1 (CC-NBS-LRR) with RKS1 and PBL2&#x20;<sup>UMP</sup> ligands form the pentameric complex. The funnel-like channel (&#x223c;0.5&#xa0;nm in narrowest diameter) is a non-selective, Ca<sup>2&#x2b;</sup> influx, cation channel. Likewise, helper NLRs required for TLR (TIR-NB-LRR)-mediated HR constitute a Ca<sup>2&#x2b;</sup> influx, cation channel. But the definitive 3D models of helper NLRs remain elusive; other CNL resistosomes may be cation channels, but their 3D structures are not be determined. And, ferroptosis-like cell death was also observed in plant cells. <bold>(D)</bold> In total, GSDM and MLKL domains directly target the plasma membrane; the Bcl-2 family is responsible for mitochondrial membrane damages; and TIR-like sense and monitor energy deficit to produce a second messenger for downstream signaling.</p>
</caption>
<graphic xlink:href="fcell-09-790117-g002.tif"/>
</fig>
</sec>
<sec id="s1-2">
<title>The Emerging Roles of Mammalian Bcl-2 Family Proteins in Apoptosis</title>
<p>The protein members of the B-cell lymphoma 2 (Bcl-2) family residing at the outer mitochondrial membrane may be classified into three functionally and structurally distinct subgroups, such as BH3 (the Bcl-2 homology 3)-only proteins (which communicate signals to initiate intrinsic apoptosis), the Bcl-2 itself as the pro-survival cell guardian, and the pro-apoptotic effector proteins BAX (Bcl-2&#x2013;associated X protein) and BAK (Bcl-2 antagonist/killer) (<xref ref-type="bibr" rid="B70">Lindsten et&#x20;al., 2000</xref>; <xref ref-type="bibr" rid="B17">Czabotar et&#x20;al., 2014</xref>; <xref ref-type="bibr" rid="B58">Ke et&#x20;al., 2012</xref>; <xref ref-type="bibr" rid="B78">Naim and Kaufmann, 2020</xref>) (<xref ref-type="fig" rid="F1">Figure&#x20;1A</xref>). The anti- and pro-apoptotic ones both balance the mitochondrial membrane potential, and their interplay sets the apoptotic threshold in the mitochondrial outer membrane. With respect to the BH3-only protein, there are activator BH3-only proteins including BIM and the truncated form of BID (tBID) that can directly bind and activate BAX or BAK and sensitizer BH3-only proteins, such as BAD, which indirectly activate BAX or BAK by neutralizing pro-survival Bcl-2 family members (<xref ref-type="bibr" rid="B17">Czabotar et&#x20;al., 2014</xref>). Overexpressed BH3-only proteins, particularly those (BIM, tBID, and PUMA) that target&#x20;all pro-survival Bcl-2 family members, can trigger apoptosis. Diverse cell types from <italic>Bax</italic>
<sup>
<italic>&#x2212;/&#x2212;</italic>
</sup>
<italic>Bak</italic>
<sup>
<italic>&#x2212;/&#x2212;</italic>
</sup> mice are completely resistant to multiple apoptotic stimuli, including the enforced expression of BH3-only proteins (<xref ref-type="bibr" rid="B114">Wei et&#x20;al., 2001</xref>; <xref ref-type="bibr" rid="B15">Cheng et&#x20;al., 2001</xref>; <xref ref-type="bibr" rid="B130">Zong et&#x20;al., 2001</xref>) and are required for normal tissue development (<xref ref-type="bibr" rid="B84">Rathmell et&#x20;al., 2002</xref>; <xref ref-type="bibr" rid="B74">Mason et&#x20;al., 2013</xref>). Thus, the BH3-only proteins function upstream of BAX and BAK (<xref ref-type="bibr" rid="B17">Czabotar et&#x20;al., 2014</xref>) and cannot cause cell death unless BAX or BAK is present. In transgenic mice, all of the pro-survival Bcl-2 family members endow much cell type resistance against diverse apoptotic stimuli. The apoptosis of autoreactive <italic>BIM</italic> <sup>&#x2212;/&#x2212;</sup> B&#x20;cells and T&#x20;cells negatively regulated by Bcl-2 act as one important checkpoint for preventing autoimmune kidney disease that resembles human systemic lupus erythematosus. BH3-only proteins or BH3-mimicking small molecules (BH3 mimetics) might promote apoptosis and improve the cancer therapy effect. Accordingly, the Bcl-2 overexpression in B&#x20;cells of mice, loss of BIM, or loss of both BAX and BAK can provoke a fatal autoimmune kidney disease and might improve the treatment of diverse types of cancer (<xref ref-type="bibr" rid="B1">Adams and Cory, 2018</xref>).</p>
</sec>
<sec id="s1-3">
<title>MLKL-Mediated Necroptosis in Mammalian Cells</title>
<p>As known, non-lytic apoptosis is a non-inflammatory form of cell death. On the contrary, necroptosis and pyroptosis belong to lytic PCDs along with inflammatory exudates but differ for distinguishably lytic phenotypes. The necroptotic feature corresponds to cellular explosion, and pyroptosis is characterized by osmotic swelling/balloon-like protrusions. Necroptotic stimuli (including Z-DNA, Z-DNA binding protein 1 (ZBP1), and TNF-&#x3b1;) initiate a supramolecular organizing center (SMOC), called the necrosome RIPK1-RIPK3 core, as a hetero-amyloid signaling complex to perform autophosphorylations (<xref ref-type="bibr" rid="B126">Zhang, et&#x20;al., 2009</xref>; <xref ref-type="bibr" rid="B101">Sun et&#x20;al., 2012</xref>; <xref ref-type="bibr" rid="B102">Sun and Wang, 2014</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2A</xref>). The activated RIPK3 phosphorylates the necroptosis effector, as a pseudokinase&#x2014;mixed lineage kinase domain-like (MLKL). And, the phosphorylated MLKLs undergo conformational alternation and initiatively bind with IP6 and recognize the anionic phospholipids (such as phosphatidylinositol-4-phosphate (PtIns4P)) of the inner leaflet of the plasma membrane, finally oligomerize and perforate the plasma membrane to form a non-selective cation channel (<xref ref-type="bibr" rid="B43">Huang et&#x20;al., 2017</xref>; <xref ref-type="bibr" rid="B100">Su et&#x20;al., 2014</xref>; <xref ref-type="bibr" rid="B110">Wang et&#x20;al., 2014</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2A</xref>). Necroptosis would occur upon death of stimuli when caspase-8 is inactive after genetic depletion or chemical inhibition by the Z-VAD-FMK inhibitor (<xref ref-type="bibr" rid="B37">He, et&#x20;al., 2009</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2A</xref>). In the more complex necroptotic pathway, tumor necrosis factor receptor 1 (TNFR1), toll-like receptor 3 (TLR3)&#x2013;TRIF, and TLR4&#x2013;TRIF signal <italic>via</italic> RIPK1 to activate NF-&#x3ba;B, but RIPK1 is not required for the TRIF-type I IFN response (<xref ref-type="bibr" rid="B27">Fitzgerald and Kagan, 2020</xref>).</p>
</sec>
<sec id="s1-4">
<title>Gasdermin-Mediated Pyroptosis in Animals and Bacterial Cells</title>
<p>Like apoptosomes and necroptosomes, pyroptotic inflammasomes are responsible for the activation of inflammatory caspase-1 (<xref ref-type="bibr" rid="B19">Ding and Shao, 2017</xref>). How are the other inflammatory caspase-4/5/11 activated upon bacterial infections? Shao Lab identified that caspase-4/5/11 can directly recognize the cytosolic lipopolysaccharides (LPS) to aggregate into non-canonical inflammasomes and commit self-cleavage to form active caspases (<xref ref-type="bibr" rid="B96">Shi et&#x20;al., 2014</xref>). Once activated, caspase-1, 4/5/11 are capable of cleaving gasdermin D (GSDMD), being a bipartite protein whose amino-terminal and carboxy-terminal domains are connected by a linker and the free <italic>N</italic>-terminal fragment of GSDMD to induce 31&#x223c;34-fold symmetry gasdermin pore forming and pyroptosis (<xref ref-type="bibr" rid="B95">Shi et&#x20;al., 2015</xref>; <xref ref-type="bibr" rid="B20">Ding et&#x20;al., 2016</xref>; <xref ref-type="bibr" rid="B19">Ding and Shao, 2017</xref>; <xref ref-type="bibr" rid="B86">Ruan et&#x20;al., 2018</xref>; <xref ref-type="bibr" rid="B119">Xia et&#x20;al., 2021</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2A</xref>). The mature forms of pro&#x2013;interleukin-1&#x3b2; (IL-1&#x3b2;) and pro&#x2013;IL-18 processed by caspase-1 are feasible to outflow through the GSDMD pore (&#x223c;21&#xa0;nm in internal diameter), while large amounts of sodium and water enter, and increasing expansion of pores finally lead to osmotic swelling and cell death (<xref ref-type="bibr" rid="B119">Xia et&#x20;al., 2021</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2A</xref>).</p>
<p>The gasdermin subfamily has six members GSDMA-GASDME and GSDMF (DFNB59, also called PJVK) in humans. GSDMF is highly similar to GSDME, and its mutation is associated with autosomal recessive deafness (<xref ref-type="bibr" rid="B12">Broz et&#x20;al., 2020</xref>). Different gasdermin members are activated by different protease(s) including caspase(s) or other proteases. The activation of GSDME was licensed to caspase-3, and activated gasdermin E assemblies (pore rings) have 26&#x223c;28-fold symmetry and may drive chemotherapy-induced pyroptosis (<xref ref-type="bibr" rid="B113">Wang et&#x20;al., 2017</xref>; <xref ref-type="bibr" rid="B12">Broz et&#x20;al., 2020</xref>; <xref ref-type="bibr" rid="B127">Zhang et&#x20;al., 2020</xref>; <xref ref-type="bibr" rid="B119">Xia et&#x20;al., 2021</xref>). And, gasdermin B can also be functionally cleaved by granzyme(s) from lymphocytes and NK cells for activation (<xref ref-type="bibr" rid="B129">Zhou et&#x20;al., 2020</xref>). Apart from targeting the plasma membrane, active gasdermin B prefers to bind bacterial phospholipids and has strong bactericidal activities rather than cellular toxicity for NK cells (<xref ref-type="bibr" rid="B34">Hansen et&#x20;al., 2021</xref>).</p>
<p>Importantly, oligomerization of the released N-lobe of gasdermins is a requisite for pyroptotic cell death. Pyroptosis is defined as gasdermin-mediated programmed necrotic cell death (<xref ref-type="bibr" rid="B12">Broz et&#x20;al., 2020</xref>). As known, pyroptosis accompanies mitochondrial damages. And, the mitochondrial tricarboxylic acid (TCA) cycle metabolites (namely, fumarate and its derivatives) can modify a reactive cysteine of GSDMD by succination, which results in significantly decreased cleavage and pore formation (<xref ref-type="bibr" rid="B44">Humphries et&#x20;al., 2020</xref>). Nevertheless, GSDMD cleavage by proteases appears to be not equivalent to pore formation. Recent studies identified that the lysosome-locating Ragulator-Rag complex involved in the mTORC1 pathway maintaining metabolic homeostasis may control the pore formation of gasdermins in the plasma membrane and/or serve as a scaffold for the activation of the FADD&#x2013;RIPK1&#x2013;caspase-8 complex to induce pyroptosis (<xref ref-type="bibr" rid="B26">Evavold et&#x20;al., 2021</xref>; <xref ref-type="bibr" rid="B128">Zheng et&#x20;al., 2021</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2A</xref>). The mTORC1 sensitize and control mitochondrial dysfunction and promote mitochondrial ROS generation, which boost gasdermin oligomerization <italic>in vivo</italic> (<xref ref-type="bibr" rid="B26">Evavold et&#x20;al., 2021</xref>). The Rag-Ragulator complex surveils both metabolism and infection to act as a molecular hub dictating the living or death fate of infected cells (<xref ref-type="bibr" rid="B128">Zheng et&#x20;al., 2021</xref>).</p>
<p>During the last stage of pyroptotic cell death, the plasma membrane rupture (PMR) usually occurs in dying cells. PMR previously is considered as a passive process following pore formation. But <xref ref-type="bibr" rid="B57">Kayagaki et&#x20;al. (2021)</xref> recently identified that PMR may be a positive event mediated by the protein NINJ1, which is a 16-kDa protein with two transmembrane motifs and juxtaposed to the plasma membrane with both termini outside the cytoplasm. In addition to pyroptosis, other programmed lytic cell deaths all undergo PMR as well. Therefore, NINJ1 may act downstream of the formations of the GSDMD pore or MLML channel to elicit&#x20;PMR.</p>
<p>Apart from mammalian gasdermins, the only CsGSDME from aquatic teleost <italic>Cynoglossus semilaevis</italic> can be cleaved by Cscaspase-1, -3, and -7 to elicit pyroptosis (<xref ref-type="bibr" rid="B48">Jiang et&#x20;al., 2019</xref>). Additionally, the GSDME homolog also exists in the marine invertebrate coral <italic>Orbicella faveolata</italic>, and Ofcaspase-3 is capable of cleaving OfGSDME to induce pyroptosis upon the infection by the bacterial pathogen <italic>Vibrio coralliilyticus</italic> (<xref ref-type="bibr" rid="B47">Jiang S et&#x20;al., 2020</xref>). These important findings of GSDME-mediated pyroptosis in aquatic animals shed light on the activation mode of gasdermin during pyroptosis and broaden the evolutionary insights into pyroptosis-related immunological stresses upon bacterial invasions. In contrast to animals&#x2019; gasdermins, the uncharacterized proteins with predicted homology to gasdermin domains were identified after bioinformatical analyses of bacterial anti-phage defense islands. The majority are encoded adjacent to one or more genes with a predicted protease domain through examining the genomic neighborhood of bacterial gasdermin-likes (<xref ref-type="bibr" rid="B50">Johnson et&#x20;al., 2022</xref>). Some of the GSDM-associated proteases are fused to repeat domains including leucine-rich repeats, tetratricopeptide repeats, WD40 repeats, or NACHT domains frequently involved in prokaryotic samples. In addition, the gRAMP CRISPR-Cas effector is an RNA endonuclease complex with a caspase-like peptidase (<xref ref-type="bibr" rid="B108">van Beljouw et&#x20;al., 2021</xref>), regardless of the structure and substrate specificity of bacterial caspase-like proteases temporarily named &#x2018;&#x2018;orthocaspases&#x2019;&#x2019; (<xref ref-type="bibr" rid="B75">Minina et&#x20;al., 2020</xref>). While breaking of viral RNAs is inadequate to escape infections, bacteria would switch on suicide as a consequence of activation of caspase-likes by sensing viral RNAs. Another recent report claimed that the activated <italic>Runella</italic> gasdermin-likes after removal of the short C-terminal region (about 20 AAs) by the associated caspase-like protease (or a certain orthocaspase) has the capability to form mesh-like membrane pores (average 28&#xa0;nm in inner diameter) and displays bactericidal activity <italic>via</italic> non-selective leakage (<xref ref-type="bibr" rid="B50">Johnson et&#x20;al., 2022</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2B</xref>), although how caspase-like protease becomes active was not documented. Collectively, it uncovered that the conserved gasdermin-like pore is an ancient conduit for the cellular content efflux in prokaryotes and eukaryotes.</p>
</sec>
<sec id="s1-5">
<title>The Switch of Apoptosis, Necroptosis, and Pyroptosis by Caspase-8</title>
<p>In response to influenza A virus (IAV) infection, the induced pro-death complex encompasses a plethora of proteins: RIPK1, apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC), nucleotide-binding oligomerization domain NOD-like receptor pyrin domain-containing 3 (NLRP3), and caspase-8, RIPK3, ZBP1, and caspase-1 (<xref ref-type="bibr" rid="B88">Samir et&#x20;al., 2020</xref>). In addition, the AIM2 sensitizing dsDNA sense double-stranded DNA (dsDNA) forms the inflammasome being an important sentinel of the innate immune defense and has essential roles in development of infectious diseases. However, AIM2 beyond its canonical role in inflammasome formation and observed pyroptosis cannot explain the outcome resulted from the AIM2 inflammasome. During infections by dsDNA herpes simplex virus 1 (HSV1) and the Gram-negative bacterium <italic>Francisella novicida</italic>, AIM2, pyrin, and ZBP1 were constituents of a large multiplex complex concomitant with ASC,caspase-1, caspase-8, RIPK3, RIPK1, and FADD, that led to PANoptosis, an inflammatory cell death pluralized by apoptosis, pyroptosis, and necroptosis (<xref ref-type="bibr" rid="B63">Lee et&#x20;al., 2021</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2A</xref>). The confluence of critical molecules for apoptosis, pyroptosis, and necroptosis could explain why the different types of cell death can exchange under certain conditions (<xref ref-type="bibr" rid="B91">Schwarzer et&#x20;al., 2020</xref>). Caspase-8 is the initiator caspase of extrinsic apoptosis and cleaves RIPK1/3 to restrict necroptosis (<xref ref-type="bibr" rid="B28">Frank and Vince, 2019</xref>). Therefore, caspase-8 deficiency in mice causes embryonic lethality which can be rescued by deletion of either RIPK3 or MLKL (<xref ref-type="bibr" rid="B29">Fritsch et&#x20;al., 2019</xref>; <xref ref-type="bibr" rid="B79">Newton et&#x20;al., 2019</xref>). MLKL deficiency rescues the cardiovascular defect phenotype but unexpectedly causes necroptosis-independent death. When necroptosis is blocked, the expression of non-catalytic caspase-8 triggered the formation of ASC-associated inflammasomes and resulted in pyroptosis in mice. Genetic analyses confirmed that caspase-8 serves as the molecular switch for hierarchical activation of apoptotic, necroptotic, and pyroptotic signaling pathways (<xref ref-type="bibr" rid="B81">Orning et&#x20;al., 2018</xref>; <xref ref-type="bibr" rid="B29">Fritsch et&#x20;al., 2019</xref>; <xref ref-type="bibr" rid="B79">Newton et&#x20;al., 2019</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2A</xref>).</p>
</sec>
<sec id="s1-6">
<title>Animal and Plant Bcl-2&#x2013;Associated Athanogene Proteins in Cell Death Regulation and Stress Responses</title>
<p>The extrinsic apoptosis pathway and other types of PCD are orchestrated by caspase-8, whereas MOMP during intrinsic apoptosis is positively and negatively regulated by Bcl-2 family proteins. To identify Bcl-2 partner(s), the Bcl-2&#x2013;associated athanogene (BAG) family genes were initially found <italic>via</italic> a yeast two-hybrid screening (<xref ref-type="bibr" rid="B54">Kabbage and Dickman, 2008</xref>). The <italic>BAG1</italic> gene was shown to enhance the anti-apoptotic activity of Bcl-2, which seemed to be indicative of its involvement in the apoptotic pathway(s) (<xref ref-type="bibr" rid="B104">Takayama et&#x20;al., 1995</xref>; <xref ref-type="bibr" rid="B11">Brive et&#x20;al., 2001</xref>; <xref ref-type="bibr" rid="B103">Takayama and Reed, 2001</xref>). The BAG family is a phylogenetically conserved group of proteins with orthologues widely across organisms from plants to metazoans including humans. The C-terminal BAG domain (BD) from all BAG proteins directly interact with the heat shock protein 70 (HSP70) chaperone (<xref ref-type="bibr" rid="B103">Takayama and Reed, 2001</xref>). The BAG proteins serve as co-chaperones that function as molecular switches associating with HSP70 and other substrates and maintain protein homeostasis and modulate cell death. In fact, BAG1 itself functions as a substrate of E3 ligase (i.e.,&#x20;the C terminus of HSC70-interacting protein (CHIP)), and the formation of the BAG1-CHIP ternary complex targets proteins for degradation (<xref ref-type="bibr" rid="B53">Kabbage et&#x20;al., 2017</xref>). Reversely, BAG2 associating with CHIP inhibits the E3 ligase activity. BAG3 has roles in protein quality control to sustain cell survival and was indicative of the antagonistic effect against chemotherapy (<xref ref-type="bibr" rid="B4">Behl 2016</xref>). BAG4 has been considered to act as a negative regulator of the TNF superfamily. BAG5 has been relevant to neurodegeneration (such as Parkinson&#x2019;s disease) and was discovered to suppress both parkin E3 ligase and HSP70 chaperone activities (<xref ref-type="bibr" rid="B55">Kalia et&#x20;al., 2004</xref>). BAG6 ablation might contribute to increased lethality and severe developmental abnormality in various organs (<xref ref-type="bibr" rid="B53">Kabbage et&#x20;al., 2017</xref>).</p>
<p>
<italic>Arabidopsis</italic> BAG proteins may be categorized into two sub-groups according to their featured domain: AtBAG1&#x2013;4 having a UBL motif similar to human BAG1 besides the BD, and AtBAG5&#x2013;7 containing a calmodulin (CaM)&#x2013;binding motif nearby the BD. The AtBAG1&#x2013;3 keeps functionally unknown. BAG4 binds to HSP70 chaperones and is related to cell death inhibition upon abiotic stress. AtBAG5 constitutes a complex with CaM/HSC70 and is involved in plant senescence (<xref ref-type="bibr" rid="B53">Kabbage et&#x20;al., 2017</xref>). AtBAG6 is functionally activated through aspartyl protease processing and coordinates with chitin perception to inducible autophagy (<xref ref-type="bibr" rid="B56">Kang et&#x20;al., 2006</xref>). The ER-locating AtBAG7, as an essential component of the unfolded protein response, recognizes the molecular chaperone BIP2. Upon ER stresses, AtBAG7 can translocate to the nucleus, where it interplays with the transcription factor WRKY29 related to stress response and/or immunity (<xref ref-type="bibr" rid="B68">Li et&#x20;al., 2017</xref>). Due to BAGs&#x2019; association with HSP70 partially and their multiplex targets, the conservation of BAG molecular regulations and contributive properties in immunity-associated cell death was discovered in plants and animals.</p>
</sec>
<sec id="s1-7">
<title>Ferroptosis in Animal and Plant Cells</title>
<p>Along with the discovery of apoptosis, necroptosis, pyroptosis, and immune cell death, ferroptosis dependent of iron was proposed in 2012 (<xref ref-type="bibr" rid="B23">Dixon et&#x20;al., 2012</xref>). Ferroptosis is characterized by the peroxidation of polyunsaturated fatty acids (PUFAs) from membrane lipids by lipoxygenases (LOXs) being non-heme iron oxidases and reactive oxygen species (ROS) from the Fe<sup>2&#x2b;</sup>-directed Fenton reaction (<xref ref-type="bibr" rid="B122">Yang et&#x20;al., 2016</xref>). Recently, lipid peroxidation during ferroptosis may be mainly catalyzed by oxidoreductases POR and cytochrome b5 reductase 1 (CYB5R1) other than LOXs (<xref ref-type="bibr" rid="B121">Yan et&#x20;al., 2021</xref>). Importantly, ferroptosis can be hindered by glutathione peroxidase GPX4 for depletion of lipid peroxide and coenzyme Q oxidoreductase FSP1 and mitochondrial dihydrooratic acid dehydrogenase (DHODH) for neutralization of the lipid peroxide free radical (<xref ref-type="bibr" rid="B6">Bersuker et&#x20;al., 2019</xref>; <xref ref-type="bibr" rid="B72">Mao et&#x20;al., 2021</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2A</xref>). Hence, lipoperoxides cannot be excessively aggregated to disrupt the integrity of the plasma membrane. Due to the prevalence of the conserved cytochromes, LOXs, and other popular oxidoreductases and dehydrogenases in plants, the induced ferroptosis-like cell death may contribute to immune responses in plants upon biotic stresses (<xref ref-type="fig" rid="F2">Figure&#x20;2C</xref>) (<xref ref-type="bibr" rid="B21">Dist&#xe9;fano et&#x20;al., 2017</xref>; <xref ref-type="bibr" rid="B18">Dangol et&#x20;al., 2019</xref>; <xref ref-type="bibr" rid="B22">Dist&#xe9;fano et&#x20;al., 2021</xref>). Also, it has been reported that iron-dependent death regulates conidiospore development of pathogen fungi &#x2014;&#x2014;<italic>Magnaporthe grisea</italic> (<xref ref-type="bibr" rid="B94">Shen et&#x20;al., 2020</xref>). The mechanistic insights into inhibition of ferroptosis in plants remain to be further elucidated by biochemical and genetic analyses.</p>
</sec>
<sec id="s1-8">
<title>CNL Resistosome and Helper Nod-Like Receptors Mediate Ca<sup>2&#x2b;</sup> Influx Required for Programmed Cell Death in Plant Cells</title>
<p>The LRR-NBS domains from R proteins are largely similar to the LRR-NACHT domain in the inflammatory NOD-like receptor protein 3 (NLRP3) for caspase-1 activation. The <italic>N</italic>-terminal domains of R proteins can be divided into three categories: TIR-NBS-LRR (TNLs), CC-NBS-LRR (CNLs), and CC<sub>R</sub>-NB-LRR (RNLs). The three subfamilies are collectively referred to as Nod-like receptors (NLRs). NLRs evolved from a common primordial prokaryotic adenosine triphosphatase (ATPase), which is classified into two distinct derivatives: NACHT and NB-ARC type NBDs. The NB-ARC type is found in plant NLRs and NACHT in animal NLRs (<xref ref-type="bibr" rid="B51">Jones et&#x20;al., 2016</xref>). Animal NLRs with cognate ligands can oligomerize into wheel-like complexes as inflammasomes upon stimuli (<xref ref-type="bibr" rid="B42">Hu et&#x20;al., 2015</xref>). Similarly, the <italic>Arabidopsis</italic> ZAR1 protein (a CNL) initially confers resistance to <italic>P. syringae</italic> carrying the effector protein HopZ1a and sensitizes the alteration of the host sensory protein PBS1-LIKE 2 (PBL2) upon <italic>Xanthomonas campestris</italic> pv. <italic>campestris</italic> (Xcc) effector AvrAC (<xref ref-type="bibr" rid="B8">Bi and Zhou, 2021</xref>). The cryo-EM structures of the ZAR1 resistosome in resting and activated states were reported. ZAR1 interacts with the plant protein pseudokinase RKS1 (a receptor-like cytoplasmic kinase (RLCK), belonging to the RLCK-XII subfamily) and remained at the resting state. Upon infection, AvrAC uridylates PBS1-like protein 2 (a member of RLCK-VII subfamily) to generate PBL2<sup>UMP</sup>, which is recruited to the ZAR1-RKS1 complex to form the ZA1-RKS1- PBL2<sup>UMP</sup> complex in a primed state lacking ATP or dATP (<xref ref-type="bibr" rid="B111">Wang et&#x20;al., 2019a</xref>; <xref ref-type="bibr" rid="B112">Wang et&#x20;al., 2019b</xref>). PBL2<sup>UMP</sup> binding activates the nucleotide exchange factor activity of RKS1. Once activated, RKS1 facilitates ADP release from ZAR1 by inducing conformation changes in the NBD domain of ZAR, which enables ZAR1 to go through the fold switch of its CC domain and leads to the formation of a pentameric ZA1-RKS1- PBL2<sup>UMP</sup> structure (<xref ref-type="bibr" rid="B111">Wang et&#x20;al., 2019a</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2C</xref>). The funnel-shaped architecture constituted by the <italic>N</italic>-terminal alpha-helices of ZAR1 in the resistosome promotes ZAR1 integration into the plasma membrane. It may perturb the membrane integrity or ionic homeostasis. Subsequent studies showed that this funnel-like structure of helices in the N-terminal region is featured by a Ca<sup>2&#x2b;</sup> channel, being responsible for the Ca<sup>2&#x2b;</sup> influx, which is required for resistance (<xref ref-type="bibr" rid="B7">Bi et&#x20;al., 2021</xref>). It is reminiscent that the activation of the inflammasome NLRP3 requires the serine/threonine kinase NEK7, and NLRP3-NEK7 modules constitute a disk-like structure (<xref ref-type="bibr" rid="B38">He et&#x20;al., 2016</xref>; <xref ref-type="bibr" rid="B93">Sharif et&#x20;al., 2019</xref>). This indicated the convergence on activation strategies of diverse varieties of NLRs. NLRs from animals and plants are all capable of being activated by kinase(s), which may possess nucleotide exchange activities and elicit the allosteric effect of NLRs to oligomerize into active resistosomes (<xref ref-type="bibr" rid="B111">Wang et&#x20;al., 2019a</xref>).</p>
<p>TNLs RPP1 and roq1 recognize the bacterial effector ATR1 and <italic>Xanthomonas</italic> effector RPP1 of oomycetes, respectively. The direct binding of ATR1/RPP1 to a <italic>C</italic>-terminal jelly roll/Ig-like domain and LRR domain leads to induce the tetrameric assembly. The two catalytic centers of NADase are composed of asymmetric homodimers in tetrameric TIR domains, which define the formation of active holoenzyme (<xref ref-type="bibr" rid="B73">Martin et&#x20;al., 2020</xref>; <xref ref-type="bibr" rid="B71">Ma et&#x20;al., 2020</xref>). TNLs and CNLs directly or indirectly sensitize pathogen effectors. But RNLs are not conferred to perceive microbial avirulent factors but acts downstream of TNL-mediated signaling. Therefore, it is called helper NLR, which contains two types: NRG1 and ADR1. EDS1 and PAD4 are plant effector proteins with lipase-like domains, which aggregate to promote cell death. Additionally, NRG1 involves the downstream cascade of TNL-mediated cell death. Structural data and electrophysiological experiments also corroborated that the self-activating mutant of NRG1 is a calcium-permeable but non-selective cation channel. <italic>Arabidopsis</italic> NRG1 CC<sub>R</sub> was structurally similar to pseudokinase MLKL as a cationic channel causing cell necrosis in animals (<xref ref-type="bibr" rid="B45">Jacob et&#x20;al., 2021</xref>) (<xref ref-type="fig" rid="F2">Figure&#x20;2C</xref>). Both self-activating mutants expressing NRG1 and ADR1 in tobacco and human cancer cells can give rise to cell death. And, the death phenotype depends on plasma membrane localization of helper NLRs and the Ca<sup>2&#x2b;</sup>influx (<xref ref-type="bibr" rid="B45">Jacob et&#x20;al., 2021</xref>). Collectively, the activation of NLR in CNL and TNL resistosomes both converge on the Ca<sup>2&#x2b;</sup> influx&#x2013;mediated cation channels formed by NLRs. We have not yet understood how to trigger plant cell death after inducing the Ca<sup>2&#x2b;</sup> influx. According to previous reports, the appearance of HR required the plasma membrane fusion with a plant vacuole, in which cysteine proteases (including vacuolar processing enzymes (VPEs), and/or RD19) are required for cytolysis (<xref ref-type="bibr" rid="B35">Hatsugai et&#x20;al., 2004</xref>; <xref ref-type="bibr" rid="B5">Bernoux et&#x20;al., 2008</xref>).</p>
</sec>
<sec id="s1-9">
<title>TIR as NADase for Producing Cyclic ADPR Essential for TNL-Mediated Death Signal Cascading and Activated Myd88-5 Inducing Neuron Death</title>
<p>The plant TNLs RPP1 and ROQ1 recognize their respective cognate effector ATR1. The complexes both individually oligomerize into tetramers, and the tetrameric wheel-like resistosomes have NADase holoenzyme activity through adjacent TIR&#x2013;TIR close contact. The oligomerization of the TIR-domain is essential for its NAD<sup>&#x2b;</sup>-catalyzing activity for variant cADPR (v-cADPR) production (<xref ref-type="bibr" rid="B109">Wan et&#x20;al., 2019</xref>). TIR domains unlike other effector domains (such as Bcl-2, MLKL, and gasdermin) directly target the plasma membrane and perceive and/or amplify signals to trigger downstream immune responses (<xref ref-type="fig" rid="F2">Figure&#x20;2D</xref>). TIR domains from plant TNLs have NADase activities versus TLR-containing TIR domains devoid of catalytic activities and are paralogous to the TIR domain of SARM1 protein, namely MyD88-5 (<xref ref-type="fig" rid="F3">Figures 3A,B</xref>). MyD88 is an adaptor molecule involved in the signaling through the IL-1R and TLR families and is essential for the response to IL-1, IL-18, LPS, and many other bacterial cell-wall components. Otherwise, SARM1/MyD88-5 is the critical mediator of axon degeneration upon energy deficit (<xref ref-type="bibr" rid="B47">Jiang S et&#x20;al., 2020</xref>).</p>
<fig id="F3" position="float">
<label>FIGURE 3</label>
<caption>
<p>Mutual potentiation and regulation of TLR-mediated immunity and NLR-mediated immunity in plants and animals. <bold>(A)</bold> LRR-RLK (receptor-like kinase) confer to pattern-triggered immunity, functionally similar to animal Toll-like on the cell surface. SARM1 has a mitochondria-targeting signal (MTS), AMR, SAM, and C-terminal TIR domain, where there being conserved Asp/Glu residues, which endow the NADase activity. <bold>(B)</bold> Cytosolic CNL and TNL are composed of NBS and LRR domains with a distinct <italic>N</italic>-terminal region (coiled coil or TIR domain). <bold>(C)</bold> The PAD4-EDS1 complex and ADR1 together locate the inner leaflet of the plasma membrane and enhance PRR (LRR-RK)- and RLCK (BIK1)-dependent PTI. <bold>(D)</bold> Cytosolic toll and interleukin 1 receptor (TIR) of TLR4 can interplay with the TIR domain(s) of four adaptor molecules MyD88, TIRAP, TRIF, and TRAM to transmit the cascade reaction and promote the secretion of inflammatory factors and interferons. The capase-8 substrate, N4BP, act as a suppressor of cytokine responses. Asterisk (&#x2a;) represents the catalytic activities of TIR domains.</p>
</caption>
<graphic xlink:href="fcell-09-790117-g003.tif"/>
</fig>
<p>The cryo-EM structure of full-length human SARM1 revealed that it bound NAD<sup>&#x2b;</sup> constitutes, an octamer in its inactive state, which inhibit its TIR NADase activity under high NAD<sup>&#x2b;</sup> levels (<xref ref-type="bibr" rid="B9">Bratkowski et&#x20;al., 2020</xref>; <xref ref-type="bibr" rid="B49">Jiang Y et&#x20;al., 2020</xref>; <xref ref-type="bibr" rid="B98">Sporny et&#x20;al., 2020</xref>). The human SARM1 with a nicotinamide mononucleotide (NMN) octamer undergoes a conformational change disrupting NAD<sup>&#x2b;</sup>binding sites of the ARM domains to enable TIR&#x2013;TIR dimerization. NAD<sup>&#x2b;</sup>deficit upon severe damages of the mitochondria from axons may result in SARM1&#x20;TIR-TIR associations and then produce cADPR to trigger axon death (<xref ref-type="bibr" rid="B49">Jiang Y et&#x20;al., 2020</xref>). The ectopic expression of the TIR domain of human SARM1 in tobacco for cADPR generation may trigger cell death independent of EDS1 (<xref ref-type="bibr" rid="B40">Horsefield et&#x20;al., 2019</xref>). The amount of cADPR dramatically increases upon accumulation of the senescence-related phytohormone ABA in plants and ultimately elicits cell death (<xref ref-type="bibr" rid="B118">Wu et&#x20;al., 1997</xref>). It should be presumed that cADPR as a candidate common second messenger conveys death signal to the cascading pathways in plants and animals. In bacteria, cyclic oligonucleotide sensor(s) conjugated with effectors (such as lipase or transmembrane protein or other effectors) triggers enough bacterial cell disruption in response to phage invasion and results in the abortive infection (<xref ref-type="bibr" rid="B92">Severin et&#x20;al., 2018</xref>; <xref ref-type="bibr" rid="B77">Morehouse et&#x20;al., 2020</xref>). The infected bacterial cells commit suicide prior to the performance of the phage replication cycle. This strategy eliminates infected cells from the bacterial community and protects the bacterial population from a phagic epidemic (<xref ref-type="bibr" rid="B33">Hampton et&#x20;al., 2020</xref>). Some bacteria exploit TIR-STING fusion protein to inhibit phage infections (<xref ref-type="bibr" rid="B16">Cohen et&#x20;al., 2019</xref>; <xref ref-type="bibr" rid="B24">Eaglesham et&#x20;al., 2019</xref>). Bacterial STING coupling cyclic dinucleotide recognition forms filaments to drive TIR oligomerization for cADPR production (<xref ref-type="bibr" rid="B77">Morehouse et&#x20;al., 2020</xref>). This strategy is used to remove infected cells from the bacterial community and protect the population from a phage epidemic.</p>
</sec>
<sec id="s1-10">
<title>Plant Immune Response Coordinated by PTI and ETI Versus TLR- and Nod-Like Receptor-Mediated Immune Responses in Animals</title>
<p>Upon pathogen infection, plants utilize cell-surface pattern-recognition receptors (PRRs) to rapidly recognize pathogen/damage-associated molecular patterns (PAMPs/DAMPs) and then bind and phosphorylate co-receptors&#x2014;receptor-like cytoplasmic kinases (RLCKs) and phosphorylated RLCKs sequentially activate MAPK cascade signaling, Ca<sup>2&#x2b;</sup>-dependent protein kinases (CDPKs), and reactive oxygen species (ROS) burst (<xref ref-type="bibr" rid="B106">Tang et&#x20;al., 2017</xref>; <xref ref-type="bibr" rid="B69">Liang and Zhou, 2018</xref>). For examples, the NO burst was induced in <italic>Arabidopsis</italic> suspension cells in response to bacterial LPS. LPS treatment not only induces the expression of <italic>Arabidopsis</italic> NO synthase (AtNOS1) but also activates the defense genes (<xref ref-type="bibr" rid="B125">Zeidler et&#x20;al., 2004</xref>). Sequentially, the <italic>Arabidopsis</italic> LPS receptor was identified to be lectin S-domain-1 receptor&#x2013;like kinase LORE (<xref ref-type="bibr" rid="B83">Ranf et&#x20;al., 2015</xref>). <italic>AtNOS1</italic>-deficient and LPS-insensitive <italic>LORE</italic> mutants are hypersusceptible to the pathogen <italic>Pseudomonas syringae</italic> (<xref ref-type="bibr" rid="B125">Zeidler et&#x20;al., 2004</xref>; <xref ref-type="bibr" rid="B83">Ranf et&#x20;al., 2015</xref>). Plant LysM domain proteins have been widely implicated in the recognition of GlcNAc-containing glycans. CERK1, a lysin-motif (LysM) receptor kinase (LYK) can recognize fungal MAMP chitin (<xref ref-type="bibr" rid="B76">Miya et&#x20;al., 2007</xref>). LYK5 and LYK4 are also identified to be components of a tripartite chitin receptor complex (<xref ref-type="bibr" rid="B13">Cao et&#x20;al., 2014</xref>; <xref ref-type="bibr" rid="B120">Xue et&#x20;al., 2019</xref>). The glycosylphosphatidylinositol-anchored LysM proteins (LYM1 and LYM3) sense PGNs (<xref ref-type="bibr" rid="B115">Willmann et&#x20;al., 2011</xref>). LRR-RK MIK2 recognizes multiple plant endogenous peptides of SCOOP family members, leading to a series of PTI responses, including the cytosolic Ca<sup>2&#x2b;</sup> influx, ROS burst, MAPK activation, ethylene production, and defense-related gene expression (<xref ref-type="bibr" rid="B41">Hou et&#x20;al., 2021</xref>; <xref ref-type="bibr" rid="B85">Rhodes et&#x20;al., 2021</xref>). The LRR receptor kinase HPCA1(other name CARD1) as the receptor(s) of DAMPs hydrogen peroxide and quinone perceives H<sub>2</sub>O<sub>2</sub> and host-derived quinone DMBQ to activate the Ca<sup>2&#x2b;</sup> influx and MAPK pathway (<xref ref-type="bibr" rid="B62">Laohavisit et&#x20;al., 2020</xref>; <xref ref-type="bibr" rid="B117">Wu et&#x20;al., 2020</xref>).</p>
<p>These responses are collectively called pattern-triggered immunity (PTI), which can impede further invasion at the pre-infection phase. But, successful pathogens exploit secreted effectors dedicates to pathogen virulence to intervene with PTI; this leads to effector-triggered susceptibility (ETS); then, the host continuously evolves the novel NB-LRR protein(s) to specifically recognize/sequester pathogen effector(s), inducing effector-triggered immunity (ETI) (<xref ref-type="bibr" rid="B52">Jones and Dangl, 2006</xref>). R protein-mediated ETI accelerates and amplifies immune responses, leading to resistance against diseases, usually, a hypersensitive cell death response (HR) at infection sites (<xref ref-type="bibr" rid="B52">Jones and Dangl, 2006</xref>). Certainly, ETI has two-branched responses: promotion of the resistance-related gene expression and HR. Recent advances confirmed that ETI also robustly boosted the expression of PTI-involved genes; meanwhile, the sole activation of NLR-mediated resistance in absence of PTI is insufficient to safeguard the host against bacterial infections (<xref ref-type="bibr" rid="B124">Yuan et&#x20;al., 2021</xref>). PTI can enhance resistance from PTI. The PTI and ETI comprising the two-tiered plant immune system that monitors threats from pathogens are not separable and collaboratively contribute to the reciprocal enhancement of plant immunity (<xref ref-type="bibr" rid="B80">Ngou et&#x20;al., 2021</xref>; <xref ref-type="bibr" rid="B82">Pruitt et&#x20;al., 2021</xref>; <xref ref-type="bibr" rid="B124">Yuan et&#x20;al., 2021</xref>; <xref ref-type="bibr" rid="B107">Tian et&#x20;al., 2021</xref>). HR as one canonical type of PCD in plants is beneficial to the host likely by eliminating the intracellular niche for proliferation of certain pathogens. Furthermore, the resulting cellular debris coordinates a systemic immune response to promote the resolution of infection. As known, HR cannot represent the whole resistance in plants. Reprogramming of immune genes enforces resistance. The ADR1-EDS1-PAD4 module can be polymerized with the complex formed by LRR-RP-SOBIR1 and PBL31 of the RLCK family to form a supramolecular complex, which not only binds the inner leaflet of the plasma membrane to mediate the response of PTI but ADR1 is contributive to TNL-directed resistance signaling involved in reprogrammed transcription of pathogenesis-responsive genes (<xref ref-type="bibr" rid="B82">Pruitt et&#x20;al., 2021</xref>) (<xref ref-type="fig" rid="F3">Figure&#x20;3C</xref>).</p>
<p>Likewise, the Toll-like receptor (TLR) families in animals are phylogenetically conserved mediators of innate immunity and are responsible for microbial recognition on cellular surfaces. TLRs consist of a large family with extracellular/ectodomain leucine-rich repeats (LRRs) and a cytoplasmic Toll/interleukin (IL)-1 receptor (TIR) homology domain (<xref ref-type="bibr" rid="B27">Fitzgerald and Kagan, 2020</xref>). TLRs occupy the plasma membranes and detect the microbial&#x20;conserved components present on the host cell surface. TLRs sensitize peptidoglycan (TLR2), dsRNA (TLR3), lipopolysaccharide (LPS) (TLR4), flagellin (TLR5), unmethylated CpG DNAs (TLR9), and other PAMPs. In virtue of the unraveled extracellular receptors for molecular patterns in plants, more diverse motifs present in the extracellular space are used for sensing various molecular patterns including MAMPs and/or other stimuli. Moreover, the commonalities between receptors in plants and animals are single-pass transmembrane proteins which recruit cytosolic kinase(s) to activate phosphorylation-cascading pathway(s) and induce the expression of stress-related genes. In virtue of alien dsRNA or ssDNA being conserved signatures, plant hosts should license PRRs to perceive the immune signal, although the potent extracellular dsDNA/RNA receptors located at the plant cell surface are yet to&#x20;be validated.</p>
<p>Upon recognition of PAMPs, the cytoplasmic TIR domains of dimerized TLRs located at the plasma membrane recruit TIR-containing TIRAP and Myd88 to assembly Myddosome containing TRAF6, which functions to stimulate TBK1 to drive IKK- and MAPK-dependent transcription and cytokine releases (<xref ref-type="bibr" rid="B27">Fitzgerald and Kagan, 2020</xref>). On endosomes, TLR4 and TLR3 are capable of engaging a SMOC called the triffosome. TRIF is present in this complex. TRIF encompasses a pLxIS motif that increases the TBK1-regulated gene expression and an RHIM domain to promote RIPK3-mediated necroptosis (<xref ref-type="bibr" rid="B36">He et&#x20;al., 2011</xref>) (<xref ref-type="fig" rid="F3">Figure&#x20;3D</xref>). Under certain conditions, the TLR3 and TLR4 pair activates caspase-8 through the adaptor TRIF, but generally TLR3/4 signaling does elicit apoptosis. Caspase-8 cleaves N4BP1, which inhibits cytokine responses and suppression of the LPS-stimulated gene expression (<xref ref-type="bibr" rid="B30">Gitlin et&#x20;al., 2020</xref>) (<xref ref-type="fig" rid="F3">Figure&#x20;3D</xref>). Functionally, TLRs from animals may be regarded as the counterpart of LRR-RLKs involved in PTI in plants. The cytoplasmic NOD-like receptors (NLRs) monitored the intracellular environment for an alternative sign upon pathogen infection and then fulfill the assembly of inflammasomes. In parallel, plants have evolved intracellular R proteins to intercept the activities of effector proteins that are delivered inside the host cell and activate defenses, complementing the ETI, which resembles inflammasome-mediated innate immunity in animals. Despite many breakthroughs on the understandings of PTI and ETI from plants and the proposed conceptual resistosome in parallel with the inflammasome, the direct executioners of HR in plants need to be further investigated and explored by the state-of-the-art and maneuverable technology.</p>
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<sec id="s1-11">
<title>Outlook</title>
<p>Mammalian intrinsic apoptosis is marked by the mitochondrial membrane rupture, which resulted from Bax/Bak oligomerization in mitochondrial membranes. The mitochondria branches within alphaproteobacteria. And, the pore-forming domains of bacterial toxins such as colicins A1 and E1 and diphtheria toxin structurally are similar to mitochondrial Bcl-2 (<xref ref-type="bibr" rid="B59">Kelekar and Thompson, 1998</xref>). Like bacterial toxins, Bcl-2, Bcl-xL, and Bax can insert into synthetic lipid vesicles and planar lipid bilayers and form ion-conducting channels (<xref ref-type="bibr" rid="B89">Schendel et&#x20;al., 1997</xref>). This suggested that the Bcl-2 family responsible for mitochondrial &#x201c;suicide&#x201d; might have ancestral origins from bacteria. Why PCD in host cells requires that semi-parasitic mitochondria commit self-death in advance? Apoptosomes sense oxidation&#x2013;reduction potential to activate major initiator caspase-9 for intrinsic apoptosis. Indeed, pyroptosis is also concomitant with damaged mitochondria. The elevated mitochondrial ROS promote gasdermin pore formation for pyroptosis.</p>
<p>Similarly, the plant NLRs activate downstream immune responses, which escalate the expression level of crucial immune proteins, such as BIK1 and NADPH oxidase RBOHD. A plethora of heme-containing RBOHD located in the plasma membrane boost ROS burst (<xref ref-type="bibr" rid="B124">Yuan et&#x20;al., 2021</xref>). R protein-mediated HR coincides with the coexistence of Fe<sup>2&#x2b;</sup> and ROS, which both being requisite for ferroptosis. As aforementioned, NLRs (CC- and CC<sub>R</sub>-types) in plants possess similar structural features of inflammatory NLRs and necroptotic MLKL in animals. These appeared to be indicative of HR in plants as PCD was featured by the chimeric/promiscuous combination of pyroptotic, necroptotic, and ferroptotic forms. According to the above descriptions and comparisons, the PRRs (such as LRR-RK) and R proteins (TNLs and CNLs with LRR motifs) from plants structurally and evolutionarily correspond to TLRs and NLRs (both comprising LRR motifs) in animals. Evidently, the common superhelical conformation of distinct LRR motifs is selected to recognize the diverse molecular patterns derived from pathogens or hosts in plants and animals. Second, ROS act as common inducers for PCD in plants and animals. Third, the serious damage/disruption of biomembranes (the plasma membrane and/or mitochondria/plastid membrane) is essential for PCD in plants and animals. Considering the extreme diversity of bacteriophage species and their tremendous amounts, bacteria hosts exert utmost efforts on the development of immune arsenal including caspase-like,TIR-like, cGAS-like, STING-like, and lipase-like domains shared by prokaryotes and eukaryotes (<xref ref-type="fig" rid="F2">Figure&#x20;2B</xref>). Based on the subsequent discoveries of the primordial signature of bacterial immune proteins orthologous to counterparts in animals, there are grounds to believe that plants have uncharacterized immune effectors which might contribute to conserved PCDs and which might be evolved from the common ancestors/progenitors shared by bacteria and animals.</p>
<p>Relative to the clear mechanistic insights into animal PCDs, in plant PCDs there are many important unsettled problems: 1) the final executioner of plant HR death upon infections; 2) the exact substrates of cysteine proteases or other proteases involved in PCD; 3) the role of the Ca<sup>2&#x2b;</sup> influx. 4) the definite signalings conjugated with the second messengers; 5) the linkage of various types of plant PCDs upon infections; 6) the necessary roles of lipase-like activities in plant HR. Additionally, plant cells have rigid cell walls surrounding the plasma membrane. The question as to whether or not the cell death of plant cells required the degradation of cell wall components such as cellulose, hemicellulose, and pectin remains unknown. We should recapitulate the cellular states including transcriptional and translational profiles through single-cell multi-omic analyses. Collectively, these embodies that the uniform but diversity in all organism PCDs involved in immunity.</p>
</sec>
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</body>
<back>
<sec id="s2">
<title>Author Contributions</title>
<p>JZ wrote this manuscript. LX and LZ collected references specifically related with the Bcl-2 family and discussed the whole manuscript.</p>
</sec>
<sec id="s3">
<title>Funding</title>
<p>This work was supported by the National Natural Science Foundation of China (No. 31301641 to JZ) and the FAFU Science developmental funding (KFA20015A to JZ and CXZX2018094 to&#x20;LZ).</p>
</sec>
<sec sec-type="COI-statement" id="s4">
<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>
</sec>
<sec sec-type="disclaimer" id="s5">
<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>
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