pubmed-article:21075794 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21075794 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
pubmed-article:21075794 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:21075794 | lifeskim:mentions | umls-concept:C0879393 | lld:lifeskim |
pubmed-article:21075794 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
pubmed-article:21075794 | lifeskim:mentions | umls-concept:C1158537 | lld:lifeskim |
pubmed-article:21075794 | lifeskim:mentions | umls-concept:C1823878 | lld:lifeskim |
pubmed-article:21075794 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:21075794 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:21075794 | pubmed:dateCreated | 2011-3-28 | lld:pubmed |
pubmed-article:21075794 | pubmed:abstractText | MSH6, a key component of the MSH2-MSH6 complex, plays a fundamental role in the repair of mismatched DNA bases. Herein, we report that MSH6 is a novel Ku70-interacting protein identified by yeast two-hybrid screening. Ku70 and Ku86 are two key regulatory subunits of the DNA-dependent protein kinase, which plays an essential role in repair of DNA double-strand breaks (DSBs) through the non-homologous end-joining (NEHJ) pathway. We found that association of Ku70 with MSH6 is enhanced in response to treatment with the radiomimetic drug neocarzinostatin (NCS) or ionizing radiation (IR), a potent inducer of DSBs. Furthermore, MSH6 exhibited diffuse nuclear staining in the majority of untreated cells and forms discrete nuclear foci after NCS or IR treatment. MSH6 colocalizes with ?-H2AX at sites of DNA damage after NCS or IR treatment. Cells depleted of MSH6 accumulate high levels of persistent DSBs, as detected by formation of ?-H2AX foci and by the comet assay. Moreover, MSH6-deficient cells were also shown to exhibit impaired NHEJ, which could be rescued by MSH6 overexpression. MSH6-deficient cells were hypersensitive to NCS- or IR-induced cell death, as revealed by a clonogenic cell-survival assay. These results suggest a potential role for MSH6 in DSB repair through upregulation of NHEJ by association with Ku70. | lld:pubmed |
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pubmed-article:21075794 | pubmed:language | eng | lld:pubmed |
pubmed-article:21075794 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21075794 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:21075794 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:21075794 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:21075794 | pubmed:month | Mar | lld:pubmed |
pubmed-article:21075794 | pubmed:issn | 1362-4962 | lld:pubmed |
pubmed-article:21075794 | pubmed:author | pubmed-author:HyunJin-WonJW | lld:pubmed |
pubmed-article:21075794 | pubmed:author | pubmed-author:YouHo JinHJ | lld:pubmed |
pubmed-article:21075794 | pubmed:author | pubmed-author:LeeJung-HeeJH | lld:pubmed |
pubmed-article:21075794 | pubmed:author | pubmed-author:ChangIn-YoubI... | lld:pubmed |
pubmed-article:21075794 | pubmed:author | pubmed-author:LeeSung... | lld:pubmed |
pubmed-article:21075794 | pubmed:author | pubmed-author:KangYoonsungY | lld:pubmed |
pubmed-article:21075794 | pubmed:author | pubmed-author:ShahiAnkitaA | lld:pubmed |
pubmed-article:21075794 | pubmed:author | pubmed-author:JunJae-YeoulJ... | lld:pubmed |
pubmed-article:21075794 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21075794 | pubmed:volume | 39 | lld:pubmed |
pubmed-article:21075794 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21075794 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21075794 | pubmed:pagination | 2130-43 | lld:pubmed |
pubmed-article:21075794 | pubmed:dateRevised | 2011-7-27 | lld:pubmed |
pubmed-article:21075794 | pubmed:meshHeading | pubmed-meshheading:21075794... | lld:pubmed |
pubmed-article:21075794 | pubmed:meshHeading | pubmed-meshheading:21075794... | lld:pubmed |
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