Hsp70 in Redox Homeostasis
Cellular redox homeostasis is precisely balanced by generation and elimination of reactive oxygen species (ROS). ROS are not only capable of causing oxidation of proteins, lipids and DNA to damage cells but can also act as signaling molecules to modulate transcription factors and epigenetic pathways...
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MDPI AG
2022-02-01
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Series: | Cells |
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Online Access: | https://www.mdpi.com/2073-4409/11/5/829 |
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author | Hong Zhang Weibin Gong Si Wu Sarah Perrett |
author_facet | Hong Zhang Weibin Gong Si Wu Sarah Perrett |
author_sort | Hong Zhang |
collection | DOAJ |
description | Cellular redox homeostasis is precisely balanced by generation and elimination of reactive oxygen species (ROS). ROS are not only capable of causing oxidation of proteins, lipids and DNA to damage cells but can also act as signaling molecules to modulate transcription factors and epigenetic pathways that determine cell survival and death. Hsp70 proteins are central hubs for proteostasis and are important factors to ameliorate damage from different kinds of stress including oxidative stress. Hsp70 members often participate in different cellular signaling pathways via their clients and cochaperones. ROS can directly cause oxidative cysteine modifications of Hsp70 members to alter their structure and chaperone activity, resulting in changes in the interactions between Hsp70 and their clients or cochaperones, which can then transfer redox signals to Hsp70-related signaling pathways. On the other hand, ROS also activate some redox-related signaling pathways to indirectly modulate Hsp70 activity and expression. Post-translational modifications including phosphorylation together with elevated Hsp70 expression can expand the capacity of Hsp70 to deal with ROS-damaged proteins and support antioxidant enzymes. Knowledge about the response and role of Hsp70 in redox homeostasis will facilitate our understanding of the cellular knock-on effects of inhibitors targeting Hsp70 and the mechanisms of redox-related diseases and aging. |
first_indexed | 2024-03-09T20:44:13Z |
format | Article |
id | doaj.art-e2c41c31d7864cf6963936890f97a2fd |
institution | Directory Open Access Journal |
issn | 2073-4409 |
language | English |
last_indexed | 2024-03-09T20:44:13Z |
publishDate | 2022-02-01 |
publisher | MDPI AG |
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series | Cells |
spelling | doaj.art-e2c41c31d7864cf6963936890f97a2fd2023-11-23T22:50:54ZengMDPI AGCells2073-44092022-02-0111582910.3390/cells11050829Hsp70 in Redox HomeostasisHong Zhang0Weibin Gong1Si Wu2Sarah Perrett3National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, ChinaNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, ChinaNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, ChinaNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, ChinaCellular redox homeostasis is precisely balanced by generation and elimination of reactive oxygen species (ROS). ROS are not only capable of causing oxidation of proteins, lipids and DNA to damage cells but can also act as signaling molecules to modulate transcription factors and epigenetic pathways that determine cell survival and death. Hsp70 proteins are central hubs for proteostasis and are important factors to ameliorate damage from different kinds of stress including oxidative stress. Hsp70 members often participate in different cellular signaling pathways via their clients and cochaperones. ROS can directly cause oxidative cysteine modifications of Hsp70 members to alter their structure and chaperone activity, resulting in changes in the interactions between Hsp70 and their clients or cochaperones, which can then transfer redox signals to Hsp70-related signaling pathways. On the other hand, ROS also activate some redox-related signaling pathways to indirectly modulate Hsp70 activity and expression. Post-translational modifications including phosphorylation together with elevated Hsp70 expression can expand the capacity of Hsp70 to deal with ROS-damaged proteins and support antioxidant enzymes. Knowledge about the response and role of Hsp70 in redox homeostasis will facilitate our understanding of the cellular knock-on effects of inhibitors targeting Hsp70 and the mechanisms of redox-related diseases and aging.https://www.mdpi.com/2073-4409/11/5/829redox homeostasisoxidative stressROSHsp70cysteine modificationsglutathionylation |
spellingShingle | Hong Zhang Weibin Gong Si Wu Sarah Perrett Hsp70 in Redox Homeostasis Cells redox homeostasis oxidative stress ROS Hsp70 cysteine modifications glutathionylation |
title | Hsp70 in Redox Homeostasis |
title_full | Hsp70 in Redox Homeostasis |
title_fullStr | Hsp70 in Redox Homeostasis |
title_full_unstemmed | Hsp70 in Redox Homeostasis |
title_short | Hsp70 in Redox Homeostasis |
title_sort | hsp70 in redox homeostasis |
topic | redox homeostasis oxidative stress ROS Hsp70 cysteine modifications glutathionylation |
url | https://www.mdpi.com/2073-4409/11/5/829 |
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