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Functional Diversity of Mammalian Small Heat Shock Proteins: A Review

The small heat shock proteins (sHSPs), whose molecular weight ranges from 12∼43 kDa, are members of the heat shock protein (HSP) family that are widely found in all organisms. As intracellular stress resistance molecules, sHSPs play an important role in maintaining the homeostasis of the intracellul...

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Autores principales: Gu, Chaoguang, Fan, Xinyi, Yu, Wei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10417760/
https://www.ncbi.nlm.nih.gov/pubmed/37566026
http://dx.doi.org/10.3390/cells12151947
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author Gu, Chaoguang
Fan, Xinyi
Yu, Wei
author_facet Gu, Chaoguang
Fan, Xinyi
Yu, Wei
author_sort Gu, Chaoguang
collection PubMed
description The small heat shock proteins (sHSPs), whose molecular weight ranges from 12∼43 kDa, are members of the heat shock protein (HSP) family that are widely found in all organisms. As intracellular stress resistance molecules, sHSPs play an important role in maintaining the homeostasis of the intracellular environment under various stressful conditions. A total of 10 sHSPs have been identified in mammals, sharing conserved α-crystal domains combined with variable N-terminal and C-terminal regions. Unlike large-molecular-weight HSP, sHSPs prevent substrate protein aggregation through an ATP-independent mechanism. In addition to chaperone activity, sHSPs were also shown to suppress apoptosis, ferroptosis, and senescence, promote autophagy, regulate cytoskeletal dynamics, maintain membrane stability, control the direction of cellular differentiation, modulate angiogenesis, and spermatogenesis, as well as attenuate the inflammatory response and reduce oxidative damage. Phosphorylation is the most significant post-translational modification of sHSPs and is usually an indicator of their activation. Furthermore, abnormalities in sHSPs often lead to aggregation of substrate proteins and dysfunction of client proteins, resulting in disease. This paper reviews the various biological functions of sHSPs in mammals, emphasizing the roles of different sHSPs in specific cellular activities. In addition, we discuss the effect of phosphorylation on the function of sHSPs and the association between sHSPs and disease.
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spelling pubmed-104177602023-08-12 Functional Diversity of Mammalian Small Heat Shock Proteins: A Review Gu, Chaoguang Fan, Xinyi Yu, Wei Cells Review The small heat shock proteins (sHSPs), whose molecular weight ranges from 12∼43 kDa, are members of the heat shock protein (HSP) family that are widely found in all organisms. As intracellular stress resistance molecules, sHSPs play an important role in maintaining the homeostasis of the intracellular environment under various stressful conditions. A total of 10 sHSPs have been identified in mammals, sharing conserved α-crystal domains combined with variable N-terminal and C-terminal regions. Unlike large-molecular-weight HSP, sHSPs prevent substrate protein aggregation through an ATP-independent mechanism. In addition to chaperone activity, sHSPs were also shown to suppress apoptosis, ferroptosis, and senescence, promote autophagy, regulate cytoskeletal dynamics, maintain membrane stability, control the direction of cellular differentiation, modulate angiogenesis, and spermatogenesis, as well as attenuate the inflammatory response and reduce oxidative damage. Phosphorylation is the most significant post-translational modification of sHSPs and is usually an indicator of their activation. Furthermore, abnormalities in sHSPs often lead to aggregation of substrate proteins and dysfunction of client proteins, resulting in disease. This paper reviews the various biological functions of sHSPs in mammals, emphasizing the roles of different sHSPs in specific cellular activities. In addition, we discuss the effect of phosphorylation on the function of sHSPs and the association between sHSPs and disease. MDPI 2023-07-27 /pmc/articles/PMC10417760/ /pubmed/37566026 http://dx.doi.org/10.3390/cells12151947 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Gu, Chaoguang
Fan, Xinyi
Yu, Wei
Functional Diversity of Mammalian Small Heat Shock Proteins: A Review
title Functional Diversity of Mammalian Small Heat Shock Proteins: A Review
title_full Functional Diversity of Mammalian Small Heat Shock Proteins: A Review
title_fullStr Functional Diversity of Mammalian Small Heat Shock Proteins: A Review
title_full_unstemmed Functional Diversity of Mammalian Small Heat Shock Proteins: A Review
title_short Functional Diversity of Mammalian Small Heat Shock Proteins: A Review
title_sort functional diversity of mammalian small heat shock proteins: a review
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10417760/
https://www.ncbi.nlm.nih.gov/pubmed/37566026
http://dx.doi.org/10.3390/cells12151947
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