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rdf:type |
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lifeskim:mentions |
umls-concept:C0079427,
umls-concept:C0080055,
umls-concept:C0085862,
umls-concept:C0441655,
umls-concept:C0441712,
umls-concept:C0441889,
umls-concept:C0694888,
umls-concept:C0851285,
umls-concept:C1299583,
umls-concept:C1325410,
umls-concept:C1549571,
umls-concept:C1608386
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pubmed:issue |
2
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pubmed:dateCreated |
2003-3-6
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pubmed:abstractText |
We show in this study that PTEN regulates p53 protein levels and transcriptional activity through both phosphatase-dependent and -independent mechanisms. The onset of tumor development in p53(+/-);Pten(+/-) mice is similar to p53(-/-) animals, and p53 protein levels are dramatically reduced in Pten(-/-) cells and tissues. Reintroducing wild-type or phosphatase-dead PTEN mutants leads to a significant increase in p53 stability. PTEN also physically associates with endogenous p53. Finally, PTEN regulates the transcriptional activity of p53 by modulating its DNA binding activity. This study provides a novel mechanism by which the loss of PTEN can functionally control "two" hits in the course of tumor development by concurrently modulating p53 activity.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin D1,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/MDM2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mdm2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PTEN Phosphohydrolase,
http://linkedlifedata.com/resource/pubmed/chemical/PTEN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-mdm2,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Protein p53,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1535-6108
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pubmed:author |
pubmed-author:CardiffRobert DRD,
pubmed-author:FreemanDaniel JDJ,
pubmed-author:KerteszNathalieN,
pubmed-author:LescheRalfR,
pubmed-author:LiAndrew GAG,
pubmed-author:LiHeng-HongHH,
pubmed-author:LiuXuanX,
pubmed-author:Martinez-DiazHildaH,
pubmed-author:RozengurtNoraN,
pubmed-author:WeiGangG,
pubmed-author:WhaleAndrew DAD,
pubmed-author:WuHongH
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
117-30
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12620407-Animals,
pubmed-meshheading:12620407-Blotting, Northern,
pubmed-meshheading:12620407-Blotting, Western,
pubmed-meshheading:12620407-Cell Line,
pubmed-meshheading:12620407-Chromatin,
pubmed-meshheading:12620407-Cyclin D1,
pubmed-meshheading:12620407-Electrophoretic Mobility Shift Assay,
pubmed-meshheading:12620407-Fibroblasts,
pubmed-meshheading:12620407-Gene Expression Regulation,
pubmed-meshheading:12620407-Genes, Tumor Suppressor,
pubmed-meshheading:12620407-Glutathione Transferase,
pubmed-meshheading:12620407-Humans,
pubmed-meshheading:12620407-Immunoblotting,
pubmed-meshheading:12620407-Mice,
pubmed-meshheading:12620407-Mice, Knockout,
pubmed-meshheading:12620407-Nuclear Proteins,
pubmed-meshheading:12620407-PTEN Phosphohydrolase,
pubmed-meshheading:12620407-Phosphoric Monoester Hydrolases,
pubmed-meshheading:12620407-Precipitin Tests,
pubmed-meshheading:12620407-Proto-Oncogene Proteins,
pubmed-meshheading:12620407-Proto-Oncogene Proteins c-mdm2,
pubmed-meshheading:12620407-Transfection,
pubmed-meshheading:12620407-Tumor Suppressor Protein p53,
pubmed-meshheading:12620407-Tumor Suppressor Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
PTEN tumor suppressor regulates p53 protein levels and activity through phosphatase-dependent and -independent mechanisms.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Molecular and Medical Pharmacology, UCLA School of Medicine, Los Angeles, CA 90095, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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