Abstract
Small heat shock proteins (sHsps) are promiscuous molecular chaperones which form dynamic, spherical oligomers. Besides their main function in balancing proteostasis upon stress, sHsps are implicated in a variety of regulatory cascades especially in eukaryotic cells. The chaperone activity of sHsps is regulated by specific triggers as heat/cold stress, starvation, pH changes, chemical, biomodulators or posttranslational modifications. In this context, switching between activation and inactivation is achieved by modulating the composition of the ensemble of sHsp oligomers. This scheme of regulation allows a tremendous variability in contact sites and, thus, high flexibility in the specific, mechanistically properties of single sHsps. Regarding the evolutionary diversification and high sequence variability of sHsps it is not surprising that their cellular functions seem to be manifold. Here we summarize the current knowledge on the common structural and functional properties of sHsps. Focusing on Drosophila melanogaster as an exemplary model, we especially revisit the expression of sHsps at different stress conditions as well as changes in their expression throughout the development and aging of higher eukaryotes.
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We thank the Deutsche Forschungsgemeinschaft (SFB 1035) for financial support and Oliver Wenisch and Georgie Johnson for critical reading of the manuscript.
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Strauch, A., Haslbeck, M. (2018). Small Heat Shock Proteins in Stress Response of Higher Eukaryotes. In: Asea, A., Kaur, P. (eds) Heat Shock Proteins and Stress. Heat Shock Proteins, vol 15. Springer, Cham. https://doi.org/10.1007/978-3-319-90725-3_14
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