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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2007-4-24
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pubmed:abstractText |
The DNA-dependent protein kinase catalytic subunit (DNA-PK(CS)) plays an important role during the repair of DNA double-strand breaks (DSBs). It is recruited to DNA ends in the early stages of the nonhomologous end-joining (NHEJ) process, which mediates DSB repair. To study DNA-PK(CS) recruitment in vivo, we used a laser system to introduce DSBs in a specified region of the cell nucleus. We show that DNA-PK(CS) accumulates at DSB sites in a Ku80-dependent manner, and that neither the kinase activity nor the phosphorylation status of DNA-PK(CS) influences its initial accumulation. However, impairment of both of these functions results in deficient DSB repair and the maintained presence of DNA-PK(CS) at unrepaired DSBs. The use of photobleaching techniques allowed us to determine that the kinase activity and phosphorylation status of DNA-PK(CS) influence the stability of its binding to DNA ends. We suggest a model in which DNA-PK(CS) phosphorylation/autophosphorylation facilitates NHEJ by destabilizing the interaction of DNA-PK(CS) with the DNA ends.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-10075677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-10207052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-10207111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-10215620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-10908332,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-11023603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-11256071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-12186630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-12231622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-12379113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-12649176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-12897153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-14506474,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-14654699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-14726021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-15258142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-15314205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-15365186,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-15380098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-15677476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-15758953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-15913400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-16061690,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-16141234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-16314509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-16618811,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-16874298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-16908529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-17124166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-2564870,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-2573661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-8538653,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-8548796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-9435225,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-9810228,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17438073-9861670
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9525
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
177
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
219-29
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17438073-Animals,
pubmed-meshheading:17438073-Antigens, Nuclear,
pubmed-meshheading:17438073-CHO Cells,
pubmed-meshheading:17438073-Catalytic Domain,
pubmed-meshheading:17438073-Cricetinae,
pubmed-meshheading:17438073-Cricetulus,
pubmed-meshheading:17438073-DNA,
pubmed-meshheading:17438073-DNA Breaks, Double-Stranded,
pubmed-meshheading:17438073-DNA Repair,
pubmed-meshheading:17438073-DNA-Activated Protein Kinase,
pubmed-meshheading:17438073-DNA-Binding Proteins,
pubmed-meshheading:17438073-Humans,
pubmed-meshheading:17438073-Lasers,
pubmed-meshheading:17438073-Phosphorylation,
pubmed-meshheading:17438073-Photobleaching
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pubmed:year |
2007
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pubmed:articleTitle |
Autophosphorylation of DNA-PKCS regulates its dynamics at DNA double-strand breaks.
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pubmed:affiliation |
Department of Radiation Oncology, University of Texas Southwestern Medical Center, Dallas, TX 75390, 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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