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Hsp90 的机体角色。

Organismal Roles of Hsp90.

机构信息

Department of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC 28223, USA.

出版信息

Biomolecules. 2023 Jan 29;13(2):251. doi: 10.3390/biom13020251.

DOI:10.3390/biom13020251
PMID:36830620
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9952938/
Abstract

Heat shock protein 90 (Hsp90) is a highly conserved molecular chaperone that assists in the maturation of many client proteins involved in cellular signal transduction. As a regulator of cellular signaling processes, it is vital for the maintenance of cellular proteostasis and adaptation to environmental stresses. Emerging research shows that Hsp90 function in an organism goes well beyond intracellular proteostasis. In metazoans, Hsp90, as an environmentally responsive chaperone, is involved in inter-tissue stress signaling responses that coordinate and safeguard cell nonautonomous proteostasis and organismal health. In this way, Hsp90 has the capacity to influence evolution and aging, and effect behavioral responses to facilitate tissue-defense systems that ensure organismal survival. In this review, I summarize the literature on the organismal roles of Hsp90 uncovered in multicellular organisms, from plants to invertebrates and mammals.

摘要

热休克蛋白 90(Hsp90)是一种高度保守的分子伴侣,可协助细胞信号转导中许多客户蛋白的成熟。作为细胞信号转导过程的调节剂,它对于维持细胞蛋白稳态和适应环境压力至关重要。新兴的研究表明,Hsp90 在生物体中的功能远不止于细胞内蛋白稳态。在后生动物中,Hsp90 作为一种对环境有反应的伴侣蛋白,参与组织间应激信号反应,协调和保护细胞非自主性蛋白稳态和生物体健康。通过这种方式,Hsp90 有能力影响进化和衰老,并影响行为反应,以促进组织防御系统,确保生物体的生存。在这篇综述中,我总结了多细胞生物(从植物到无脊椎动物和哺乳动物)中发现的 Hsp90 的生物体作用的文献。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ff8/9952938/dcc9a7607406/biomolecules-13-00251-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ff8/9952938/6a5f971bba6b/biomolecules-13-00251-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ff8/9952938/dcc9a7607406/biomolecules-13-00251-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ff8/9952938/6a5f971bba6b/biomolecules-13-00251-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ff8/9952938/dcc9a7607406/biomolecules-13-00251-g002.jpg

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Sci Adv. 2022 Dec 9;8(49):eabq3970. doi: 10.1126/sciadv.abq3970.
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