AI Article Synopsis
- - Small heat shock proteins (sHsps) help maintain protein balance in cells during normal and stressful situations by acting as molecular chaperones that form complexes with misfolded proteins without using ATP.
- - sHsps exist in various sizes and shapes, and their efficiency as chaperones is regulated by the balance between these different forms, allowing them to effectively trap and manage damaged proteins.
- - The review highlights recent findings on the structure and function of sHsp oligomers, exploring their significance in aging processes and in maintaining transparency in eye lenses.
Article 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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| http://dx.doi.org/10.1016/j.tibs.2024.08.003 | DOI Listing |
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