Regulatory mechanisms of Hsp90

Prodromou, Chrisostomos (2017) Regulatory mechanisms of Hsp90. Biochemistry and Molecular Biology Journal, 3 (1). pp. 1-8. ISSN 2471-8084

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The ability of Hsp90 to activate a disparate clientele implicates this chaperone in diverse biological processes. To accommodate such varied roles, Hsp90 requires a variety of regulatory mechanisms that are coordinated in order to modulate its activity appropriately. Amongst these, the master-regulator heat shock factor 1 (HSF1) is critically important in upregulating Hsp90 during stress, but is also responsible, through interaction with specific transcription factors (such as STAT1 and Strap/p300) for the integration of a variety of biological signals that ultimately modulate Hsp90 expression. Additionally, transcription factors, such as STAT1, STAT3 (including STAT1-STAT3 oligomers), NF-IL6, and NF-kB, are known to influence Hsp90 expression directly. Co-chaperones offer another mechanism for Hsp90 regulation, and these can modulate the chaperone cycle appropriately for specific clientele. Co-chaperones include those that deliver specific clients to Hsp90, and others that regulate the chaperone cycle for specific Hsp90-client complexes by modulating Hsp90s ATPase activity. Finally, post-translational modification (PTM) of Hsp90 and its co-chaperones helps too further regulate the variety of different Hsp90 complexes found in cells.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Research Centres and Groups: Genome Damage and Stability Centre
Subjects: Q Science > QP Physiology > QP0501 Animal biochemistry
R Medicine
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Depositing User: Chrisostomos Prodromou
Date Deposited: 09 Feb 2017 08:39
Last Modified: 02 Jul 2019 18:34

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Project NameSussex Project NumberFunderFunder Ref
Mechanisms of client protein activation and regulation by the Hsp90 molecular chaperone systemG0662WELLCOME TRUST095605/Z11/Z