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Regulation of the Chaperone Function of Small Hsps

  • Chapter
The Big Book on Small Heat Shock Proteins

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

Abstract

Small heat shock proteins (sHsps) are ubiquitous molecular chaperones that represent a first line of defense against proteotoxic stress and prevent the aggregation of unfolding proteins. The most striking feature of sHsps is their ability to form higher-order oligomers. Within the last decade, especially the dynamic ensembles with a broad distribution of different oligomers, the diversity of assembly types and the regulation of their activity were in the focus of research. Interestingly, the activity of sHsps directly correlates to these structural features as it is regulated by changes in the composition of the ensembles. In this chapter, we describe the mechanisms known so far which are responsible for the activation of chaperone function and their linkage to changes in the structure of sHsps.

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Acknowledgments

We thank the Deutsche Forschungsgemeinschaft (SFB 1035) and CIPSM for financial support.

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Authors and Affiliations

  1. Department Chemie, Center for Integrated Protein Science, Technische Universität München, 85747, Garching, Germany

    Martin Haslbeck, Sevil Weinkauf & Johannes Buchner

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  1. Martin Haslbeck
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  2. Sevil Weinkauf
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  3. Johannes Buchner
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Correspondence to Martin Haslbeck .

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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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Haslbeck, M., Weinkauf, S., Buchner, J. (2015). Regulation of the Chaperone Function of Small Hsps. 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_6

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