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Mechanisms of Hsp90 regulation

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journal contribution
posted on 2023-06-09, 00:00 authored by Chrisostomos ProdromouChrisostomos Prodromou
Heat 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.

History

Publication status

  • Published

File Version

  • Published version

Journal

Biochemical Journal

ISSN

1470-8728

Publisher

Portland Press

Issue

16

Volume

473

Page range

2439-2452

Department affiliated with

  • Biochemistry Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2016-08-18

First Open Access (FOA) Date

2016-08-18

First Compliant Deposit (FCD) Date

2016-08-18

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