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Mechanisms of Hsp90 regulation
journal contribution
posted on 2023-06-09, 00:00 authored by Chrisostomos ProdromouChrisostomos ProdromouHeat shock protein 90 (Hsp90) is a molecular chaperone that is involved in the activation of disparate client proteins. This implicates Hsp90 in diverse biological processes that require a variety of co-ordinated regulatory mechanisms to control its activity. Perhaps the most important regulator is heat shock factor 1 (HSF1), which is primarily responsible for upregulating Hsp90 by binding heat shock elements (HSEs) within Hsp90 promoters. HSF1 is itself subject to a variety of regulatory processes and can directly respond to stress. HSF1 also interacts with a variety of transcriptional factors that help integrate biological signals, which in turn regulate Hsp90 appropriately. Because of the diverse clientele of Hsp90 a whole variety of co-chaperones also regulate its activity and some are directly responsible for delivery of client protein. Consequently, co-chaperones themselves, like Hsp90, are also subject to regulatory mechanisms such as post translational modification. This review, looks at the many different levels by which Hsp90 activity is ultimately regulated.
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Publication status
- Published
File Version
- Published version
Journal
Biochemical JournalISSN
1470-8728Publisher
Portland PressExternal DOI
Issue
16Volume
473Page range
2439-2452Department affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2016-08-18First Open Access (FOA) Date
2016-08-18First Compliant Deposit (FCD) Date
2016-08-18Usage metrics
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