| pubmed-article:12024016 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12024016 | lifeskim:mentions | umls-concept:C1522449 | lld:lifeskim |
| pubmed-article:12024016 | lifeskim:mentions | umls-concept:C1704928 | lld:lifeskim |
| pubmed-article:12024016 | lifeskim:mentions | umls-concept:C0376571 | lld:lifeskim |
| pubmed-article:12024016 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:12024016 | lifeskim:mentions | umls-concept:C0332453 | lld:lifeskim |
| pubmed-article:12024016 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:12024016 | pubmed:dateCreated | 2002-5-23 | lld:pubmed |
| pubmed-article:12024016 | pubmed:abstractText | BRCA1 plays an important role in mechanisms of response to double-strand breaks, participating in genome surveillance, DNA repair, and cell cycle checkpoint arrests. Here, we identify a constitutive BRCA1-c-Abl complex and provide evidence for a direct interaction between the PXXP motif in the C terminus of BRCA1 and the SH3 domain of c-Abl. Following exposure to ionizing radiation (IR), the BRCA1-c-Abl complex is disrupted in an ATM-dependent manner, which correlates temporally with ATM-dependent phosphorylation of BRCA1 and ATM-dependent enhancement of the tyrosine kinase activity of c-Abl. The BRCA1-c-Abl interaction is affected by radiation-induced modification to both BRCA1 and c-Abl. We show that the C terminus of BRCA1 is phosphorylated by c-Abl in vitro. In vivo, BRCA1 is phosphorylated at tyrosine residues in an ATM-dependent, radiation-dependent manner. Tyrosine phosphorylation of BRCA1, however, is not required for the disruption of the BRCA1-c-Abl complex. BRCA1-mutated cells exhibit constitutively high c-Abl kinase activity that is not further increased on exposure to IR. We suggest a model in which BRCA1 acts in concert with ATM to regulate c-Abl tyrosine kinase activity. | lld:pubmed |
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| pubmed-article:12024016 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12024016 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12024016 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12024016 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12024016 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:12024016 | pubmed:author | pubmed-author:PerricaudetMi... | lld:pubmed |
| pubmed-article:12024016 | pubmed:author | pubmed-author:FavaudonVince... | lld:pubmed |
| pubmed-article:12024016 | pubmed:author | pubmed-author:PicardDidierD | lld:pubmed |
| pubmed-article:12024016 | pubmed:author | pubmed-author:ForayNicolasN | lld:pubmed |
| pubmed-article:12024016 | pubmed:author | pubmed-author:MarotDidierD | lld:pubmed |
| pubmed-article:12024016 | pubmed:author | pubmed-author:Randrianariso... | lld:pubmed |
| pubmed-article:12024016 | pubmed:author | pubmed-author:VeneziaNicole... | lld:pubmed |
| pubmed-article:12024016 | pubmed:author | pubmed-author:JeggoPennyP | lld:pubmed |
| pubmed-article:12024016 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12024016 | pubmed:volume | 22 | lld:pubmed |
| pubmed-article:12024016 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12024016 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12024016 | pubmed:pagination | 4020-32 | lld:pubmed |
| pubmed-article:12024016 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:12024016 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12024016 | pubmed:articleTitle | Constitutive association of BRCA1 and c-Abl and its ATM-dependent disruption after irradiation. | lld:pubmed |
| pubmed-article:12024016 | pubmed:affiliation | Radiobiologie Cellulaire et Moléculaire, U350 Inserm, Institut Curie, 91405 Orsay, France. nforay@aol.com | lld:pubmed |
| pubmed-article:12024016 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12024016 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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