Small heat-shock proteins: important players in regulating cellular proteostasis.

Abstract

Small heat-shock proteins (sHsps) are a diverse family of intra-cellular molecular chaperone proteins that play a critical role in mitigating and preventing protein aggregation under stress conditions such as elevated temperature, oxidation and infection. In doing so, they assist in the maintenance of protein homeostasis (proteostasis) thereby avoiding the deleterious effects that result from loss of protein function and/or protein aggregation. The chaperone properties of sHsps are therefore employed extensively in many tissues to prevent the development of diseases associated with protein aggregation. Significant progress has been made of late in understanding the structure and chaperone mechanism of sHsps. In this review, we discuss some of these advances, with a focus on mammalian sHsp hetero-oligomerisation, the mechanism by which sHsps act as molecular chaperones to prevent both amorphous and fibrillar protein aggregation, and the role of post-translational modifications in sHsp chaperone function, particularly in the context of disease.

• Authors: Teresa M Treweek, Sarah Meehan, Heath Ecroyd, John A Carver
• Journal: Cellular and molecular life sciences : CMLS (Cell Mol Life Sci) Vol. 72 Issue 3 Pg. 429-451 (Feb 2015) ISSN: 1420-9071 [Electronic] Switzerland
• PMID: 25352169 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Heat-Shock Proteins
• Molecular Chaperones
• alpha-Crystallins

Topics

• Heat-Shock Proteins (chemistry, genetics, physiology)
• Homeostasis (genetics, physiology)
• Humans
• Models, Biological
• Models, Molecular
• Molecular Chaperones (genetics, physiology)
• Multiple Sclerosis (genetics, metabolism)
• Neoplasms (genetics, metabolism)
• Neurodegenerative Diseases (genetics, metabolism)
• Phosphorylation
• Polymerization
• Protein Aggregation, Pathological (metabolism)
• Protein Processing, Post-Translational (genetics, physiology)
• alpha-Crystallins (metabolism)