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Small heat-shock proteins and their role in mechanical stress
The ability of cells to respond to stress is central to health. Stress can damage folded proteins, which are vulnerable to even minor changes in cellular conditions. To maintain proteostasis, cells have developed an intricate network in which molecular chaperones are key players. The small heat-shoc...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7332611/ https://www.ncbi.nlm.nih.gov/pubmed/32253742 http://dx.doi.org/10.1007/s12192-020-01095-z |
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author | Collier, Miranda P. Benesch, Justin L.P. |
author_facet | Collier, Miranda P. Benesch, Justin L.P. |
author_sort | Collier, Miranda P. |
collection | PubMed |
description | The ability of cells to respond to stress is central to health. Stress can damage folded proteins, which are vulnerable to even minor changes in cellular conditions. To maintain proteostasis, cells have developed an intricate network in which molecular chaperones are key players. The small heat-shock proteins (sHSPs) are a widespread family of molecular chaperones, and some sHSPs are prominent in muscle, where cells and proteins must withstand high levels of applied force. sHSPs have long been thought to act as general interceptors of protein aggregation. However, evidence is accumulating that points to a more specific role for sHSPs in protecting proteins from mechanical stress. Here, we briefly introduce the sHSPs and outline the evidence for their role in responses to mechanical stress. We suggest that sHSPs interact with mechanosensitive proteins to regulate physiological extension and contraction cycles. It is likely that further study of these interactions – enabled by the development of experimental methodologies that allow protein contacts to be studied under the application of mechanical force – will expand our understanding of the activity and functions of sHSPs, and of the roles played by chaperones in general. |
format | Online Article Text |
id | pubmed-7332611 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-73326112020-07-09 Small heat-shock proteins and their role in mechanical stress Collier, Miranda P. Benesch, Justin L.P. Cell Stress Chaperones PERSPECTIVES ON sHSPs The ability of cells to respond to stress is central to health. Stress can damage folded proteins, which are vulnerable to even minor changes in cellular conditions. To maintain proteostasis, cells have developed an intricate network in which molecular chaperones are key players. The small heat-shock proteins (sHSPs) are a widespread family of molecular chaperones, and some sHSPs are prominent in muscle, where cells and proteins must withstand high levels of applied force. sHSPs have long been thought to act as general interceptors of protein aggregation. However, evidence is accumulating that points to a more specific role for sHSPs in protecting proteins from mechanical stress. Here, we briefly introduce the sHSPs and outline the evidence for their role in responses to mechanical stress. We suggest that sHSPs interact with mechanosensitive proteins to regulate physiological extension and contraction cycles. It is likely that further study of these interactions – enabled by the development of experimental methodologies that allow protein contacts to be studied under the application of mechanical force – will expand our understanding of the activity and functions of sHSPs, and of the roles played by chaperones in general. Springer Netherlands 2020-04-06 2020-07 /pmc/articles/PMC7332611/ /pubmed/32253742 http://dx.doi.org/10.1007/s12192-020-01095-z Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | PERSPECTIVES ON sHSPs Collier, Miranda P. Benesch, Justin L.P. Small heat-shock proteins and their role in mechanical stress |
title | Small heat-shock proteins and their role in mechanical stress |
title_full | Small heat-shock proteins and their role in mechanical stress |
title_fullStr | Small heat-shock proteins and their role in mechanical stress |
title_full_unstemmed | Small heat-shock proteins and their role in mechanical stress |
title_short | Small heat-shock proteins and their role in mechanical stress |
title_sort | small heat-shock proteins and their role in mechanical stress |
topic | PERSPECTIVES ON sHSPs |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7332611/ https://www.ncbi.nlm.nih.gov/pubmed/32253742 http://dx.doi.org/10.1007/s12192-020-01095-z |
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