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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
2003-8-4
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pubmed:abstractText |
Tuberous sclerosis complex (TSC) is a genetic disease caused by mutation in either TSC1 or TSC2. The TSC1 and TSC2 gene products form a functional complex and inhibit phosphorylation of S6K and 4EBP1. These functions of TSC1/TSC2 are likely mediated by mTOR. Here we report that TSC2 is a GTPase-activating protein (GAP) toward Rheb, a Ras family GTPase. Rheb stimulates phosphorylation of S6K and 4EBP1. This function of Rheb is blocked by rapamycin and dominant-negative mTOR. Rheb stimulates the phosphorylation of mTOR and plays an essential role in regulation of S6K and 4EBP1 in response to nutrients and cellular energy status. Our data demonstrate that Rheb acts downstream of TSC1/TSC2 and upstream of mTOR to regulate cell growth.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-10835385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-10872469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-11348591,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-11348592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-11377964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-11390358,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-11438694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-11691993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-11729323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-11930000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-12045200,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-12136010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-12150915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-12172553,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-12172555,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-12271141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-12384518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-12417521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-12423332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-12556239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-2039135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-2821624,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-7566123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-7608212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-8206940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-8269512,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-8352603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-8799170,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-9001246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-9045618,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-9099708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-9463313,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-9603962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12869586-9697416
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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/Antibiotics, Antineoplastic,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/MTOR protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Monomeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RHEB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Protein S6 Kinases, 70-kDa,
http://linkedlifedata.com/resource/pubmed/chemical/Sirolimus,
http://linkedlifedata.com/resource/pubmed/chemical/TOR Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein S6 kinase, 70kD...,
http://linkedlifedata.com/resource/pubmed/chemical/tuberous sclerosis complex 1 protein,
http://linkedlifedata.com/resource/pubmed/chemical/tuberous sclerosis complex 2 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0890-9369
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1829-34
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12869586-Humans,
pubmed-meshheading:12869586-Proteins,
pubmed-meshheading:12869586-Mutation,
pubmed-meshheading:12869586-Phosphorylation,
pubmed-meshheading:12869586-Cell Division,
pubmed-meshheading:12869586-Time Factors,
pubmed-meshheading:12869586-Protein Biosynthesis,
pubmed-meshheading:12869586-Protein Binding,
pubmed-meshheading:12869586-Genes, Dominant,
pubmed-meshheading:12869586-Models, Biological,
pubmed-meshheading:12869586-Antibiotics, Antineoplastic,
pubmed-meshheading:12869586-Cell Line,
pubmed-meshheading:12869586-Dose-Response Relationship, Drug,
pubmed-meshheading:12869586-Hydrolysis,
pubmed-meshheading:12869586-Guanosine Triphosphate,
pubmed-meshheading:12869586-Protein Structure, Tertiary,
pubmed-meshheading:12869586-Repressor Proteins,
pubmed-meshheading:12869586-Plasmids,
pubmed-meshheading:12869586-Signal Transduction,
pubmed-meshheading:12869586-Protein Kinases,
pubmed-meshheading:12869586-GTP Phosphohydrolases
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