Small heat shock proteins!
Small heat shock proteins (sHsps) are a ubiquitous family of molecular chaperones with a large substrate range.
In contrast to other molecular chaperones, sHsps function independently of ATP binding or hydrolysis. sHsps form ensembles of different oligomers, which differ in chaperone activity. This is the basis for their regulation via different mechanisms.
Recent advances demonstrating the involvement of sHsps in protein aggregation in the context of condensates, cataract and aging put them in the center of the cellular protein quality control system as a surveying system for the conformational integrity of the proteome under physiological conditions, especially during proteotoxic stress.
https://www.cell.com/trends/biochemical-sciences/fulltext/S0968-0004(24)00190-7
