With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage

Heat shock proteins (HSPs) are a family of molecular chaperones that regulate essential protein refolding and triage decisions to maintain protein homeostasis. Numerous co-chaperone proteins directly interact and modify the function of HSPs, and these interactions impact the outcome of protein triag...

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Autores principales:	Selin Altinok, Rebekah Sanchez-Hodge, Mariah Stewart, Kaitlan Smith, Jonathan C. Schisler
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	heat shock proteins co-chaperones protein quality control protein folding protein degradation cardioprotection Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/a45b39cdebdc4eadbbfe89c4641cfb01
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spelling	oai:doaj.org-article:a45b39cdebdc4eadbbfe89c4641cfb012021-11-25T17:11:43ZWith or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage10.3390/cells101131212073-4409https://doaj.org/article/a45b39cdebdc4eadbbfe89c4641cfb012021-11-01T00:00:00Zhttps://www.mdpi.com/2073-4409/10/11/3121https://doaj.org/toc/2073-4409Heat shock proteins (HSPs) are a family of molecular chaperones that regulate essential protein refolding and triage decisions to maintain protein homeostasis. Numerous co-chaperone proteins directly interact and modify the function of HSPs, and these interactions impact the outcome of protein triage, impacting everything from structural proteins to cell signaling mediators. The chaperone/co-chaperone machinery protects against various stressors to ensure cellular function in the face of stress. However, coding mutations, expression changes, and post-translational modifications of the chaperone/co-chaperone machinery can alter the cellular stress response. Importantly, these dysfunctions appear to contribute to numerous human diseases. Therapeutic targeting of chaperones is an attractive but challenging approach due to the vast functions of HSPs, likely contributing to the off-target effects of these therapies. Current efforts focus on targeting co-chaperones to develop precise treatments for numerous diseases caused by defects in protein quality control. This review focuses on the recent developments regarding selected HSP70/HSP90 co-chaperones, with a concentration on cardioprotection, neuroprotection, cancer, and autoimmune diseases. We also discuss therapeutic approaches that highlight both the utility and challenges of targeting co-chaperones.Selin AltinokRebekah Sanchez-HodgeMariah StewartKaitlan SmithJonathan C. SchislerMDPI AGarticleheat shock proteinsco-chaperonesprotein quality controlprotein foldingprotein degradationcardioprotectionBiology (General)QH301-705.5ENCells, Vol 10, Iss 3121, p 3121 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	heat shock proteins co-chaperones protein quality control protein folding protein degradation cardioprotection Biology (General) QH301-705.5
spellingShingle	heat shock proteins co-chaperones protein quality control protein folding protein degradation cardioprotection Biology (General) QH301-705.5 Selin Altinok Rebekah Sanchez-Hodge Mariah Stewart Kaitlan Smith Jonathan C. Schisler With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage
description	Heat shock proteins (HSPs) are a family of molecular chaperones that regulate essential protein refolding and triage decisions to maintain protein homeostasis. Numerous co-chaperone proteins directly interact and modify the function of HSPs, and these interactions impact the outcome of protein triage, impacting everything from structural proteins to cell signaling mediators. The chaperone/co-chaperone machinery protects against various stressors to ensure cellular function in the face of stress. However, coding mutations, expression changes, and post-translational modifications of the chaperone/co-chaperone machinery can alter the cellular stress response. Importantly, these dysfunctions appear to contribute to numerous human diseases. Therapeutic targeting of chaperones is an attractive but challenging approach due to the vast functions of HSPs, likely contributing to the off-target effects of these therapies. Current efforts focus on targeting co-chaperones to develop precise treatments for numerous diseases caused by defects in protein quality control. This review focuses on the recent developments regarding selected HSP70/HSP90 co-chaperones, with a concentration on cardioprotection, neuroprotection, cancer, and autoimmune diseases. We also discuss therapeutic approaches that highlight both the utility and challenges of targeting co-chaperones.
format	article
author	Selin Altinok Rebekah Sanchez-Hodge Mariah Stewart Kaitlan Smith Jonathan C. Schisler
author_facet	Selin Altinok Rebekah Sanchez-Hodge Mariah Stewart Kaitlan Smith Jonathan C. Schisler
author_sort	Selin Altinok
title	With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage
title_short	With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage
title_full	With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage
title_fullStr	With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage
title_full_unstemmed	With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage
title_sort	with or without you: co-chaperones mediate health and disease by modifying chaperone function and protein triage
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/a45b39cdebdc4eadbbfe89c4641cfb01
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With or without You: Co-Chaperones Mediate Health and Disease by Modifying Chaperone Function and Protein Triage

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