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Updated: Jun 13, 2025

Intracellular Refolding Assay
Published on: January 24, 2012
Catchers of folding gone awry: a tale of small heat shock proteins
Carsten Peters1, Martin Haslbeck1, Johannes Buchner1
1School of Natural Sciences, and Department Bioscience, Center for Functional Protein Assemblies, Technical University Munich, Ernst-Otto-Fischer Str. 8, 85748 Garching, Germany.
Abstract:
Small heat shock proteins (sHsps) are an important part of the cellular system maintaining protein homeostasis under physiological and stress conditions. As molecular chaperones, they form complexes with different non-native proteins in an ATP-independent manner. Many sHsps populate ensembles of energetically similar but different-sized oligomers. Regulation of chaperone activity occurs by changing the equilibrium of these ensembles. This makes sHsps a versatile and adaptive system for trapping non-native proteins in complexes, allowing recycling with the help of ATP-dependent chaperones. In this review, we discuss progress in our understanding of the structural principles of sHsp oligomers and their functional principles, as well as their roles in aging and eye lens transparency.
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