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| Main Authors: | , , , , , , |
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| Format: | Recurso digital |
| Language: | |
| Published: |
Zenodo
2025
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| Online Access: | https://doi.org/10.5281/zenodo.17115476 |
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Table of Contents:
- <p>Small heat shock proteins (sHSPs; ~12–43 kDa) are ATP-independent molecular chaperones that act as first responders to proteotoxic stress. They bind non-native proteins, prevent irreversible aggregation, and triage clients for refolding or degradation. Their activities emerge from highly dynamic oligomer assemblies regulated by post-translational modification, heterooligomerization, and environmental signals. sHSPs cooperate with ATP-dependent systems— principally Hsp70 (and Hsp100 in bacteria, fungi, and plants)—to disaggregate and refold proteins after stress. Dysregulation of sHSP function is implicated in neurodegeneration, cardiomyopathy, cataract, and cancer. Here, we summarize current understanding of sHSP structure, client recognition and sequestration, interplay with other chaperones, and emerging concepts including phase-separation-like condensates and therapeutic targeting.</p>