2. Academic Validation
  3. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

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

  • Mol Cell. 2002 Dec;10(6):1307-18. doi: 10.1016/s1097-2765(02)00785-2.
Barry Panaretou 1,  Giuliano 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 H Pearl,  Chrisostomos Prodromou
Affiliations

Affiliation

  • 1 Division of Life Sciences, Franklin-Wilkins Building, 150 Stamford Street, SE1 9NN, London, United Kingdom
PMID: 12504007 DOI: 10.1016/s1097-2765(02)00785-2
Abstract

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.

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