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Role of Small Heat Shock Proteins in the Remodeling of Actin Microfilaments

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Abstract

Small heat shock proteins (sHsps) play an important role in the maintenance of proteome stability and, particularly, in stabilization of the cytoskeleton and cell contractile apparatus. Cell exposure to different types of stress is accompanied by the translocation of sHsps onto actin filaments; therefore, it is commonly believed that the sHsps are true actin-binding proteins. Investigations of last years have shown that this assumption is incorrect. Stress-induced translocation of sHsp to actin filaments is not the result of direct interaction of these proteins with intact actin, but results from the chaperone-like activity of sHsps and their interaction with various actin-binding proteins. HspB1 and HspB5 interact with giant elastic proteins titin and filamin thus providing an integrity of the contractile apparatus and its proper localization in the cell. HspB6 binds to the universal adapter protein 14-3-3 and only indirectly affects the structure of actin filament. HspB7 interacts with filamin C and controls actin filament assembly. HspB8 forms tight complex with the universal regulatory and adapter protein Bag3 and participates in the chaperone-assisted selective autophagy (CASA) of actin-binding proteins (e.g., filamin), as well as in the actin-depending processes taking place in mitoses. Hence, the mechanisms of sHsp participation in the maintenance of the contractile apparatus and cytoskeleton are much more complicated and diverse than it has been postulated earlier and are not limited to direct interactions of sHsps with actin. The old hypothesis on the direct binding of sHsps to intact actin should be revised and further detailed investigation on the sHsp interaction with minor proteins participating in the formation and remodeling of actin filaments is required.

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Acknowledgments

Year 2022 would be an 80-year anniversary of Andrei Dmitrievich Vinogradov, one of the leaders of national bioenergetics, brilliant lecturer, and critically thinking scientist. For 10 years, A. D. Vinogradov had been the Head of Department of Biochemistry and promoted investigations in the field of muscle biochemistry and proteostasis. The authors dedicate this review to the memory of this brilliant scientist.

Funding

This investigation was financially supported by the Russian Science Foundation (project no. 20-74-00013, L.K.M) and Interdisciplinary Scientific and Educational School of Moscow State University “Molecular Technologies of Living Systems and Synthetic Biology” (N.B.G.).

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Authors and Affiliations

  1. Faculty of Biology, Lomonosov Moscow State University, 119991, Moscow, Russia

    Lydia K. Muranova, Vladislav M. Shatov & Nikolai B. Gusev

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  1. Lydia K. Muranova
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  2. Vladislav M. Shatov
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  3. Nikolai B. Gusev
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L.K.M. drafted manuscript, V.M.S. drafted manuscript and prepared all figures, N.B.G. prepared and edited manuscript.

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Correspondence to Nikolai B. Gusev.

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The authors declare no conflict of interests in financial or any other sphere. This article does not contain description of studies with human participants or animals performed by any of the authors.

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Muranova, L.K., Shatov, V.M. & Gusev, N.B. Role of Small Heat Shock Proteins in the Remodeling of Actin Microfilaments. Biochemistry Moscow 87, 800–811 (2022). https://doi.org/10.1134/S0006297922080119

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  • DOI: https://doi.org/10.1134/S0006297922080119

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