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| pubmed-article:21335604 | lifeskim:mentions | umls-concept:C0042153 | lld:lifeskim |
| pubmed-article:21335604 | lifeskim:mentions | umls-concept:C0728940 | lld:lifeskim |
| pubmed-article:21335604 | lifeskim:mentions | umls-concept:C0012899 | lld:lifeskim |
| pubmed-article:21335604 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:21335604 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:21335604 | lifeskim:mentions | umls-concept:C2003852 | lld:lifeskim |
| pubmed-article:21335604 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:21335604 | lifeskim:mentions | umls-concept:C0444930 | lld:lifeskim |
| pubmed-article:21335604 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:21335604 | pubmed:dateCreated | 2011-4-11 | lld:pubmed |
| pubmed-article:21335604 | pubmed:abstractText | The tumor suppressor protein BRCA1 is a constituent of several different protein complexes and is required for homology-directed repair (HDR) of DNA double strand breaks (DSBs). The most recently discovered BRCA1-RAP80 complex is recruited to ubiquitin structures on chromatin surrounding the break. Deficiency of any member of this complex confers hypersensitivity to DNA-damaging agents by undefined mechanisms. In striking contrast to other BRCA1-containing complexes that are known to promote HDR, we demonstrate that the BRCA1-RAP80 complex restricts end resection in S/G(2) phase of the cell cycle, thereby limiting HDR. RAP80 or BRCC36 deficiency resulted in elevated Mre11-CtIP-dependent 5' end resection with a concomitant increase in HDR mechanisms that rely on 3' single-stranded overhangs. We propose a model in which the BRCA1-RAP80 complex limits nuclease accessibility to DSBs, thus preventing excessive end resection and potentially deleterious homology-directed DSB repair mechanisms that can impair genome integrity. | lld:pubmed |
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| pubmed-article:21335604 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:21335604 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:21335604 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21335604 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:21335604 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:21335604 | pubmed:author | pubmed-author:GreenbergRoge... | lld:pubmed |
| pubmed-article:21335604 | pubmed:author | pubmed-author:ColemanKara... | lld:pubmed |
| pubmed-article:21335604 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21335604 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:21335604 | pubmed:volume | 286 | lld:pubmed |
| pubmed-article:21335604 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21335604 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21335604 | pubmed:pagination | 13669-80 | lld:pubmed |
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| pubmed-article:21335604 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21335604 | pubmed:articleTitle | The BRCA1-RAP80 complex regulates DNA repair mechanism utilization by restricting end resection. | lld:pubmed |
| pubmed-article:21335604 | pubmed:affiliation | Department of Cancer Biology, Abramson Family Cancer Research Institute, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6160, USA. | lld:pubmed |
| pubmed-article:21335604 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21335604 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21335604 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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