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rdf:type |
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lifeskim:mentions |
umls-concept:C0007595,
umls-concept:C0038952,
umls-concept:C0086597,
umls-concept:C0178539,
umls-concept:C0694895,
umls-concept:C0871261,
umls-concept:C1442080,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2587213,
umls-concept:C2911692
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pubmed:issue |
5
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pubmed:dateCreated |
2003-12-3
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pubmed:abstractText |
Mutations in either the TSC1 or TSC2 tumor suppressor gene are responsible for Tuberous Sclerosis Complex. The gene products of TSC1 and TSC2 form a functional complex and inhibit the phosphorylation of S6K and 4EBP1, two key regulators of translation. Here, we describe that TSC2 is regulated by cellular energy levels and plays an essential role in the cellular energy response pathway. Under energy starvation conditions, the AMP-activated protein kinase (AMPK) phosphorylates TSC2 and enhances its activity. Phosphorylation of TSC2 by AMPK is required for translation regulation and cell size control in response to energy deprivation. Furthermore, TSC2 and its phosphorylation by AMPK protect cells from energy deprivation-induced apoptosis. These observations demonstrate a model where TSC2 functions as a key player in regulation of the common mTOR pathway of protein synthesis, cell growth, and viability in response to cellular energy levels.
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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/AMP-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/EIF4EBP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Eif4ebp1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
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/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ribosomal protein S6 kinase, 70kD...,
http://linkedlifedata.com/resource/pubmed/chemical/tuberous sclerosis complex 2 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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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 |
115
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
577-90
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:14651849-AMP-Activated Protein Kinases,
pubmed-meshheading:14651849-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:14651849-Animals,
pubmed-meshheading:14651849-Apoptosis,
pubmed-meshheading:14651849-Carrier Proteins,
pubmed-meshheading:14651849-Cell Division,
pubmed-meshheading:14651849-Cell Respiration,
pubmed-meshheading:14651849-Cell Survival,
pubmed-meshheading:14651849-Energy Metabolism,
pubmed-meshheading:14651849-Food Deprivation,
pubmed-meshheading:14651849-Glucose,
pubmed-meshheading:14651849-Humans,
pubmed-meshheading:14651849-Mice,
pubmed-meshheading:14651849-Multienzyme Complexes,
pubmed-meshheading:14651849-Phosphoproteins,
pubmed-meshheading:14651849-Phosphorylation,
pubmed-meshheading:14651849-Protein-Serine-Threonine Kinases,
pubmed-meshheading:14651849-Repressor Proteins,
pubmed-meshheading:14651849-Ribosomal Protein S6 Kinases, 70-kDa,
pubmed-meshheading:14651849-Tumor Suppressor Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
TSC2 mediates cellular energy response to control cell growth and survival.
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pubmed:affiliation |
Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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