Reversible protein assemblies in the proteostasis network in health and disease

Frontiers in Molecular Biosciences

Molecular Biosciences

Claes Andréasson¹  Verena Kohler² 

[1] Department of Molecular Biosciences, Stockholm University, Stockholm, Sweden;Institute of Molecular Biosciences, University of Graz, Graz, Austria;

关键词: phase separation;    biomolecular condensate;    aggregate;    Hsp70;    Hsp100;    disaggregation;    refolding;    degradation;   

DOI  :  10.3389/fmolb.2023.1155521

 received in 2023-01-31, accepted in 2023-03-09,  发布年份 2023

来源: Frontiers

【 摘 要 】

While proteins populating their native conformations constitute the functional entities of cells, protein aggregates are traditionally associated with cellular dysfunction, stress and disease. During recent years, it has become clear that large aggregate-like protein condensates formed via liquid-liquid phase separation age into more solid aggregate-like particles that harbor misfolded proteins and are decorated by protein quality control factors. The constituent proteins of the condensates/aggregates are disentangled by protein disaggregation systems mainly based on Hsp70 and AAA ATPase Hsp100 chaperones prior to their handover to refolding and degradation systems. Here, we discuss the functional roles that condensate formation/aggregation and disaggregation play in protein quality control to maintain proteostasis and why it matters for understanding health and disease.

【 授权许可】

Unknown   
Copyright © 2023 Kohler and Andréasson.