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- W2513455229 endingPage "2452" @default.
- W2513455229 startingPage "2439" @default.
- W2513455229 abstract "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." @default.
- W2513455229 created "2016-09-16" @default.
- W2513455229 creator A5050346032 @default.
- W2513455229 date "2016-08-11" @default.
- W2513455229 modified "2023-10-14" @default.
- W2513455229 title "Mechanisms of Hsp90 regulation" @default.
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