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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6055
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pubmed:dateCreated |
2011-10-28
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pubmed:databankReference |
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pubmed:abstractText |
Germline mutations of the breast cancer 1 (BRCA1) gene are a major cause of familial breast and ovarian cancer. The BRCA1 protein displays E3 ubiquitin ligase activity, and this enzymatic function is thought to be required for tumor suppression. To test this hypothesis, we generated mice that express an enzymatically defective Brca1. We found that this mutant Brca1 prevents tumor formation to the same degree as does wild-type Brca1 in three different genetically engineered mouse (GEM) models of cancer. In contrast, a mutation that ablates phosphoprotein recognition by the BRCA C terminus (BRCT) domains of BRCA1 elicits tumors in each of the three GEM models. Thus, BRCT phosphoprotein recognition, but not the E3 ligase activity, is required for BRCA1 tumor suppression.
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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/BRCA1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Bach1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Bard1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Basic-Leucine Zipper Transcription...,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1095-9203
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pubmed:author |
pubmed-author:BaerRichardR,
pubmed-author:ColeFrancescaF,
pubmed-author:EgliDieterD,
pubmed-author:HicksJames BJB,
pubmed-author:HirschSteffenS,
pubmed-author:JasinMariaM,
pubmed-author:LinChyuan-ShengCS,
pubmed-author:LudwigThomasT,
pubmed-author:RaviKandasamyK,
pubmed-author:ReczekColleen RCR,
pubmed-author:ReidLatarsha JLJ,
pubmed-author:ShakyaReenaR,
pubmed-author:SzabolcsMatthiasM,
pubmed-author:deRooijDirk GDG
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pubmed:issnType |
Electronic
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pubmed:day |
28
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pubmed:volume |
334
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
525-8
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pubmed:meshHeading |
pubmed-meshheading:22034435-Animals,
pubmed-meshheading:22034435-BRCA1 Protein,
pubmed-meshheading:22034435-Basic-Leucine Zipper Transcription Factors,
pubmed-meshheading:22034435-Cells, Cultured,
pubmed-meshheading:22034435-Disease Models, Animal,
pubmed-meshheading:22034435-Embryonic Stem Cells,
pubmed-meshheading:22034435-Genes, BRCA1,
pubmed-meshheading:22034435-Ligands,
pubmed-meshheading:22034435-Mammary Neoplasms, Experimental,
pubmed-meshheading:22034435-Mice,
pubmed-meshheading:22034435-Mutant Proteins,
pubmed-meshheading:22034435-Pancreatic Neoplasms,
pubmed-meshheading:22034435-Phosphoproteins,
pubmed-meshheading:22034435-Protein Binding,
pubmed-meshheading:22034435-Protein Interaction Domains and Motifs,
pubmed-meshheading:22034435-Protein Multimerization,
pubmed-meshheading:22034435-RING Finger Domains,
pubmed-meshheading:22034435-Tumor Suppressor Proteins,
pubmed-meshheading:22034435-Ubiquitin-Protein Ligases
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pubmed:year |
2011
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pubmed:articleTitle |
BRCA1 tumor suppression depends on BRCT phosphoprotein binding, but not its E3 ligase activity.
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pubmed:affiliation |
Institute for Cancer Genetics, Columbia University, New York, NY 10032, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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