pubmed-article:10567431 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10567431 | lifeskim:mentions | umls-concept:C2827383 | lld:lifeskim |
pubmed-article:10567431 | lifeskim:mentions | umls-concept:C1414805 | lld:lifeskim |
pubmed-article:10567431 | lifeskim:mentions | umls-concept:C1515877 | lld:lifeskim |
pubmed-article:10567431 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
pubmed-article:10567431 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:10567431 | pubmed:issue | 48 | lld:pubmed |
pubmed-article:10567431 | pubmed:dateCreated | 1999-12-29 | lld:pubmed |
pubmed-article:10567431 | pubmed:abstractText | p70 S6 kinase alpha (p70alpha) is activated in vivo through a multisite phosphorylation in response to mitogens if a sufficient supply of amino acids is available or to high concentrations of amino acids per se. The immunosuppressant drug rapamycin inhibits p70alpha activation in a manner that can be overcome by coexpression of p70alpha with a rapamycin-resistant mutant of the mammalian target of rapamycin (mTOR) but only if the mTOR kinase domain is intact. We report here that a mammalian recombinant p70alpha polypeptide, extracted in an inactive form from rapamycin-treated cells, can be directly phosphorylated by the mTOR kinase in vitro predominantly at the rapamycin-sensitive site Thr-412. mTOR-catalyzed p70alpha phosphorylation in vitro is accompanied by a substantial restoration in p70alpha kinase activity toward its physiologic substrate, the 40 S ribosomal protein S6. Moreover, sequential phosphorylation of p70alpha by mTOR and 3-phosphoinositide-dependent protein kinase 1 in vitro resulted in a synergistic stimulation of p70alpha activity to levels similar to that attained by serum stimulation in vivo. These results indicate that mTOR is likely to function as a direct activator of p70 in vivo, although the relative contribution of mTOR-catalyzed p70 phosphorylation in each of the many circumstances that engender p70 activation remains to be defined. | lld:pubmed |
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pubmed-article:10567431 | pubmed:language | eng | lld:pubmed |
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pubmed-article:10567431 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10567431 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10567431 | pubmed:month | Nov | lld:pubmed |
pubmed-article:10567431 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10567431 | pubmed:author | pubmed-author:HaraKK | lld:pubmed |
pubmed-article:10567431 | pubmed:author | pubmed-author:InoueHH | lld:pubmed |
pubmed-article:10567431 | pubmed:author | pubmed-author:AvruchJJ | lld:pubmed |
pubmed-article:10567431 | pubmed:author | pubmed-author:YonezawaKK | lld:pubmed |
pubmed-article:10567431 | pubmed:author | pubmed-author:TokunagaCC | lld:pubmed |
pubmed-article:10567431 | pubmed:author | pubmed-author:IsotaniSS | lld:pubmed |
pubmed-article:10567431 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10567431 | pubmed:day | 26 | lld:pubmed |
pubmed-article:10567431 | pubmed:volume | 274 | lld:pubmed |
pubmed-article:10567431 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10567431 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10567431 | pubmed:pagination | 34493-8 | lld:pubmed |
pubmed-article:10567431 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:10567431 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10567431 | pubmed:articleTitle | Immunopurified mammalian target of rapamycin phosphorylates and activates p70 S6 kinase alpha in vitro. | lld:pubmed |
pubmed-article:10567431 | pubmed:affiliation | Biosignal Research Center, Kobe University, Kobe 657-8501, Japan. | lld:pubmed |
pubmed-article:10567431 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10567431 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10567431 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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