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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2002-12-30
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pubmed:abstractText |
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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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1097-2765
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pubmed:author |
pubmed-author:ClarkePaul APA,
pubmed-author:CramerRainerR,
pubmed-author:MaloneyAlisonA,
pubmed-author:MeyerPhilippeP,
pubmed-author:MillsonStefan HSH,
pubmed-author:MollapourMehdiM,
pubmed-author:Naaby-HansenSorenS,
pubmed-author:PanaretouBarryB,
pubmed-author:PearlLaurence HLH,
pubmed-author:PiperPeter WPW,
pubmed-author:ProdromouChrisostomosC,
pubmed-author:SiligardiGiulianoG,
pubmed-author:SinghShradhaS,
pubmed-author:SteinRobR,
pubmed-author:SullivanJanis KJK,
pubmed-author:WorkmanPaulP
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pubmed:issnType |
Print
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1307-18
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12504007-Adenosine Triphosphatases,
pubmed-meshheading:12504007-Cell Line, Transformed,
pubmed-meshheading:12504007-Centromere,
pubmed-meshheading:12504007-Circular Dichroism,
pubmed-meshheading:12504007-Cloning, Molecular,
pubmed-meshheading:12504007-Genes, src,
pubmed-meshheading:12504007-Genetic Vectors,
pubmed-meshheading:12504007-HSP90 Heat-Shock Proteins,
pubmed-meshheading:12504007-Humans,
pubmed-meshheading:12504007-Kinetics,
pubmed-meshheading:12504007-Molecular Chaperones,
pubmed-meshheading:12504007-Oligonucleotide Array Sequence Analysis,
pubmed-meshheading:12504007-Oncogene Protein pp60(v-src),
pubmed-meshheading:12504007-Phenotype,
pubmed-meshheading:12504007-Recombinant Proteins,
pubmed-meshheading:12504007-Saccharomyces cerevisiae,
pubmed-meshheading:12504007-Saccharomyces cerevisiae Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.
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pubmed:affiliation |
Division of Life Sciences, Franklin-Wilkins Building, 150 Stamford Street, SE1 9NN, London, United Kingdom
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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