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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
47
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pubmed:dateCreated |
2005-11-21
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pubmed:abstractText |
The raptor-mTOR protein complex is a key component of a nutrient-sensitive signaling pathway that regulates cell size by controlling the accumulation of cellular mass. How nutrients regulate signaling through the raptor-mTOR complex is not well known. Here we show that a redox-sensitive mechanism regulates the phosphorylation of the raptor-mTOR effector S6K1, the interaction between raptor and mTOR, and the kinase activity of the raptor-mTOR complex. In cells treated with the oxidizing agents diamide or phenylarsine oxide, S6K1 phosphorylation increased and became insensitive to nutrient deprivation. Conversely, the reducing reagent BAL (British anti-Lewisite, also known as 2,3-dimercapto-1-propanol) inhibits S6K1 phosphorylation and stabilizes the interaction of mTOR and raptor to mimic the state of the complex under nutrient-deprived conditions. Our findings suggest that a redox-based signaling mechanism may participate in regulating the nutrient-sensitive raptor-mTOR complex and pathway.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Arsenicals,
http://linkedlifedata.com/resource/pubmed/chemical/Diamide,
http://linkedlifedata.com/resource/pubmed/chemical/Dimercaprol,
http://linkedlifedata.com/resource/pubmed/chemical/MTOR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidants,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/RPTOR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Protein S6 Kinases, 70-kDa,
http://linkedlifedata.com/resource/pubmed/chemical/TOR Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/oxophenylarsine,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein S6 kinase, 70kD...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39505-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16183647-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:16183647-Arsenicals,
pubmed-meshheading:16183647-Cell Line,
pubmed-meshheading:16183647-Diamide,
pubmed-meshheading:16183647-Dimercaprol,
pubmed-meshheading:16183647-Humans,
pubmed-meshheading:16183647-Multiprotein Complexes,
pubmed-meshheading:16183647-Oxidants,
pubmed-meshheading:16183647-Oxidation-Reduction,
pubmed-meshheading:16183647-Phosphorylation,
pubmed-meshheading:16183647-Protein Kinases,
pubmed-meshheading:16183647-Proteins,
pubmed-meshheading:16183647-RNA, Small Interfering,
pubmed-meshheading:16183647-Recombinant Proteins,
pubmed-meshheading:16183647-Ribosomal Protein S6 Kinases, 70-kDa,
pubmed-meshheading:16183647-Signal Transduction,
pubmed-meshheading:16183647-TOR Serine-Threonine Kinases,
pubmed-meshheading:16183647-Transfection
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pubmed:year |
2005
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pubmed:articleTitle |
Redox regulation of the nutrient-sensitive raptor-mTOR pathway and complex.
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pubmed:affiliation |
Department of Biology, Whitehead Institute for Biomedical Research and Massachusetts Institute of Technology, Cambridge, Massachusetts 02142, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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