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Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1
journal contribution
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 ProdromouClient 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 CellISSN
1097-2765Publisher
ElsevierExternal DOI
Issue
6Volume
10Page range
1307-1318Department affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2015-02-25First Open Access (FOA) Date
2015-02-25First Compliant Deposit (FCD) Date
2015-02-25Usage metrics
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No categories selectedKeywords
Adenosine Triphosphatases/*metabolismCell LineTransformedCentromere/geneticsCircular DichroismCloningMolecularGenessrcGenetic VectorsHSP90 Heat-Shock Proteins/genetics/*metabolismHumansKineticsMolecular Chaperones/chemistry/*genetics/*metabolismOligonucleotide Array Sequence AnalysisOncogene Protein pp60(v-src)/metabolismPhenotypeRecombinant Proteins/metabolismSaccharomyces cerevisiae/genetics/physiologySaccharomyces cerevisiae Proteins/chemistry/*genetics/*metabolism
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