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Redefining the Chaperone Mechanism of sHsps: Not Just Holdase Chaperones

  • Chapter
The Big Book on Small Heat Shock Proteins

Part of the book series: Heat Shock Proteins ((HESP,volume 8))

Abstract

The small heat-shock proteins (sHsps) are molecular chaperones that play a fundamental role in maintaining cellular protein homeostasis (proteostasis) by preventing the aggregation of destabilised proteins. They are generally described as ‘holdase’ type chaperones since they have the ability to bind partially folded intermediate states of target proteins, in an ATP-independent manner, and, in doing so, they can form high molecular weight complexes with some of them. However, recent work has shown that the ability of sHsps to interact with target proteins is multi-faceted. This review highlights the mechanisms by which sHsps can interact with aggregation-prone target proteins and proposes that they should be considered as protein ‘stabilisers’ rather than ‘holdase’ chaperones.

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Abbreviations

RCM:

Reduced and carboxymethylated

RCMα-LA:

Reduced and carboxymethylated α-lactalbumin

sHsp(s):

small Heat shock protein(s).

αA-C:

αA-crystallin

αB-C:

αB-crystallin

α-LA:

α-lactalbumin

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  1. Illawarra Health and Medical Research Institute and School of Biological Sciences, University of Wollongong, Wollongong, 2522, NSW, Australia

    Heath Ecroyd

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  1. Department of Molecular Biology, Medical Biochemistry & Pathology Medical School Lab Cell & Developmental Genetics IBIS, Université Laval, Quebec, Québec, Canada

    Robert M. Tanguay

  2. Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut, USA

    Lawrence E. Hightower

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Ecroyd, H. (2015). Redefining the Chaperone Mechanism of sHsps: Not Just Holdase Chaperones. In: Tanguay, R., Hightower, L. (eds) The Big Book on Small Heat Shock Proteins. Heat Shock Proteins, vol 8. Springer, Cham. https://doi.org/10.1007/978-3-319-16077-1_7

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