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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2000-11-3
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pubmed:abstractText |
Serine/threonine kinase Akt/PKB is a downstream effector molecule of phosphoinositide 3-kinase and is thought to mediate many biological actions toward anti-apoptotic responses. We found that Akt formed a complex with a 90-kDa heat-shock protein (Hsp90) in vivo. By constructing deletion mutants, we identified that amino acid residues 229-309 of Akt were involved in the binding to Hsp90 and amino acid residues 327-340 of Hsp90beta were involved in the binding to Akt. Inhibition of Akt-Hsp90 binding led to the dephosphorylation and inactivation of Akt, which increased sensitivity of the cells to apoptosis-inducing stimulus. The dephosphorylation of Akt was caused by an increase in protein phosphatase 2A (PP2A)-mediated dephosphorylation and not by a decrease in 3-phosphoinositide-dependent protein kinase-1-mediated phosphorylation. These results indicate that Hsp90 plays an important role in maintaining Akt kinase activity by preventing PP2A-mediated dephosphorylation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-10021376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-10102273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-10226025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-10400666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-10485710,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-10485711,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-10623893,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-2674684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-3037531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-7492306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-7596430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-7637703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-7701324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-8122909,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-8650155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-8710373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-8978681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9038334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9094314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9108479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9228007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9230303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9346240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9368760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9381178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9445477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9521088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9610388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9771973,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9806907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9812896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/10995457-9990018
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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 |
Sep
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pubmed:issn |
0027-8424
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
97
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10832-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
|
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pubmed:year |
2000
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pubmed:articleTitle |
Modulation of Akt kinase activity by binding to Hsp90.
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pubmed:affiliation |
Institute of Molecular and Cellular Biosciences, University of Tokyo, Tokyo 113-0032, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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