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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5997
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pubmed:dateCreated |
2010-9-10
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pubmed:abstractText |
SIRT6 belongs to the sirtuin family of protein lysine deacetylases, which regulate aging and genome stability. We found that human SIRT6 has a role in promoting DNA end resection, a crucial step in DNA double-strand break (DSB) repair by homologous recombination. SIRT6 depletion impaired the accumulation of replication protein A and single-stranded DNA at DNA damage sites, reduced rates of homologous recombination, and sensitized cells to DSB-inducing agents. We identified the DSB resection protein CtIP [C-terminal binding protein (CtBP) interacting protein] as a SIRT6 interaction partner and showed that SIRT6-dependent CtIP deacetylation promotes resection. A nonacetylatable CtIP mutant alleviated the effect of SIRT6 depletion on resection, thus identifying CtIP as a key substrate by which SIRT6 facilitates DSB processing and homologous recombination. These findings further clarify how SIRT6 promotes genome stability.
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pubmed:grant |
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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/Camptothecin,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Niacinamide,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RBBP8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SIRT6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sirtuins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
10
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pubmed:volume |
329
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1348-53
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pubmed:meshHeading |
pubmed-meshheading:20829486-Acetylation,
pubmed-meshheading:20829486-Animals,
pubmed-meshheading:20829486-Camptothecin,
pubmed-meshheading:20829486-Carrier Proteins,
pubmed-meshheading:20829486-Cell Cycle,
pubmed-meshheading:20829486-Cell Line,
pubmed-meshheading:20829486-Cell Line, Tumor,
pubmed-meshheading:20829486-Cell Proliferation,
pubmed-meshheading:20829486-DNA,
pubmed-meshheading:20829486-DNA, Single-Stranded,
pubmed-meshheading:20829486-DNA Breaks, Double-Stranded,
pubmed-meshheading:20829486-DNA Repair,
pubmed-meshheading:20829486-Genomic Instability,
pubmed-meshheading:20829486-Humans,
pubmed-meshheading:20829486-Mice,
pubmed-meshheading:20829486-Mutant Proteins,
pubmed-meshheading:20829486-Niacinamide,
pubmed-meshheading:20829486-Nuclear Proteins,
pubmed-meshheading:20829486-Protein Binding,
pubmed-meshheading:20829486-Recombination, Genetic,
pubmed-meshheading:20829486-Sirtuins
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pubmed:year |
2010
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pubmed:articleTitle |
Human SIRT6 promotes DNA end resection through CtIP deacetylation.
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pubmed:affiliation |
Gurdon Institute and Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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