Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 72, Issue 3, Pages 429-451Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-014-1754-5
Keywords
Small heat-shock protein; Protein aggregation; Molecular chaperone; Proteostasis; Cataract; Neurodegenerative disease
Categories
Funding
- Royal Society
- Australian Research Council [FT110100586]
- National Health and Medical Research Council [1068087]
- Australian Research Council [FT110100586] Funding Source: Australian Research Council
- National Health and Medical Research Council of Australia [1068087] Funding Source: NHMRC
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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.
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