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

Journal Article


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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.

Publication Date


  • 2015

Citation


  • Treweek, T. M., Meehan, S., Ecroyd, H. & Carver, J. A. (2015). Small heat-shock proteins: important players in regulating cellular proteostasis. Cellular and Molecular Life Sciences, 72 (3), 429-451.

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=3582&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/2563

Number Of Pages


  • 22

Start Page


  • 429

End Page


  • 451

Volume


  • 72

Issue


  • 3

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.

Publication Date


  • 2015

Citation


  • Treweek, T. M., Meehan, S., Ecroyd, H. & Carver, J. A. (2015). Small heat-shock proteins: important players in regulating cellular proteostasis. Cellular and Molecular Life Sciences, 72 (3), 429-451.

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=3582&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/2563

Number Of Pages


  • 22

Start Page


  • 429

End Page


  • 451

Volume


  • 72

Issue


  • 3