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Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

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posted on 2023-06-08, 14:42 authored by Barry Panaretou, Giuliana Siligardi, Philippe Meyer, Alison Maloney, Janis K Sullivan, Shradha Singh, Stefan H Millson, Paul A Clarke, Soren Naaby-Hansen, Rob Stein, Rainer Cramer, Mehdi Mollapour, Paul Workman, Peter W Piper, Laurence PearlLaurence Pearl, Chrisostomos ProdromouChrisostomos Prodromou
Client protein activation by Hsp90 involves a plethora of cochaperones whose roles are poorly defined. A ubiquitous family of stress-regulated proteins have been identified (Aha1, activator of Hsp90 ATPase) that bind directly to Hsp90 and are required for the in vivo Hsp90-dependent activation of clients such as v-Src, implicating them as cochaperones of the Hsp90 system. In vitro, Aha1 and its shorter homolog, Hch1, stimulate the inherent ATPase activity of yeast and human Hsp90. The identification of these Hsp90 cochaperone activators adds to the complex roles of cochaperones in regulating the ATPase-coupled conformational changes of the Hsp90 chaperone cycle.

History

Publication status

  • Published

File Version

  • Published version

Journal

Molecular Cell

ISSN

1097-2765

Publisher

Elsevier

Issue

6

Volume

10

Page range

1307-1318

Department affiliated with

  • Biochemistry Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2015-02-25

First Open Access (FOA) Date

2015-02-25

First Compliant Deposit (FCD) Date

2015-02-25