Proper protein folding to its 3D structure is essential for cellular homeostasis. Protein misfolding and aggregation are believed to be major driving factors of neurological diseases, diabetes, cancer, and age-associated diseases. Understanding why specific proteins misfold, aggregate, or form biomolecular condensates, and why only certain cell types are vulnerable, is crucial in unraveling the mechanistic basis of these diseases. Most of the protein-folding diseases that have been identified are known for their shared disease-initiating mechanisms. Cell membrane disruption, organellar stress, self-seeding or cross-seeding of protein aggregates, and prion-like cell-to-cell transmission are some of the well-described common pathological mechanisms. Two major questions that remain unaddressed include: What dictates the aggregation of certain proteins in certain cells, and which cellular machineries regulate this process? In order to devise therapeutic measures for proteinopathies, it is necessary to determine the causes of protein folding problems and examine the cellular damage caused by protein oligomers, aggregates, or condensates.This research topic aims to provide an understanding of the causal factors of protein misfolding, aggregation, and/or condensation in cells, how protein misfolding and protein aggregation affect cellular processes and organelles in specific cell types leading to human diseases, and the protective cellular mechanisms that tackle proteotoxicity in proteinopathies.To gather further insights into the cellular contributors and consequences of protein misfolding and aggregation, we welcome articles addressing, but not limited to, the following themes:- Protein misfolding and degenerative diseases- Biomolecular condensates in proteinopathies- Protein folding diseases, ER stress, and calcium homeostasis- Oxidative stress and mitochondrial dysfunction in proteinopathies- Cell type specificity of protein aggregation and toxicity- Autophagy and proteostasis- Protein degradation machineries in diseases- Protein homeostasis failure in aging disorders- Pharmacological enhancement of protein folding and degradation
Proper protein folding to its 3D structure is essential for cellular homeostasis. Protein misfolding and aggregation are believed to be major driving factors of neurological diseases, diabetes, cancer, and age-associated diseases. Understanding why specific proteins misfold, aggregate, or form biomolecular condensates, and why only certain cell types are vulnerable, is crucial in unraveling the mechanistic basis of these diseases. Most of the protein-folding diseases that have been identified are known for their shared disease-initiating mechanisms. Cell membrane disruption, organellar stress, self-seeding or cross-seeding of protein aggregates, and prion-like cell-to-cell transmission are some of the well-described common pathological mechanisms. Two major questions that remain unaddressed include: What dictates the aggregation of certain proteins in certain cells, and which cellular machineries regulate this process? In order to devise therapeutic measures for proteinopathies, it is necessary to determine the causes of protein folding problems and examine the cellular damage caused by protein oligomers, aggregates, or condensates.This research topic aims to provide an understanding of the causal factors of protein misfolding, aggregation, and/or condensation in cells, how protein misfolding and protein aggregation affect cellular processes and organelles in specific cell types leading to human diseases, and the protective cellular mechanisms that tackle proteotoxicity in proteinopathies.To gather further insights into the cellular contributors and consequences of protein misfolding and aggregation, we welcome articles addressing, but not limited to, the following themes:- Protein misfolding and degenerative diseases- Biomolecular condensates in proteinopathies- Protein folding diseases, ER stress, and calcium homeostasis- Oxidative stress and mitochondrial dysfunction in proteinopathies- Cell type specificity of protein aggregation and toxicity- Autophagy and proteostasis- Protein degradation machineries in diseases- Protein homeostasis failure in aging disorders- Pharmacological enhancement of protein folding and degradation