Prodromou, Chrisostomos (2016) Mechanisms of Hsp90 regulation. Biochemical Journal, 473 (16). pp. 2439-2452. ISSN 1470-8728

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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.

Item Type:	Article
Schools and Departments:	School of Life Sciences > Biochemistry
Subjects:	Q Science > QP Physiology > QP0501 Animal biochemistry
Depositing User:	Chrisostomos Prodromou
Date Deposited:	18 Aug 2016 10:39
Last Modified:	02 Jul 2019 20:50
URI:	http://sro.sussex.ac.uk/id/eprint/59210

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