| pubmed-article:15385968 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15385968 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:15385968 | lifeskim:mentions | umls-concept:C0032545 | lld:lifeskim |
| pubmed-article:15385968 | lifeskim:mentions | umls-concept:C1337033 | lld:lifeskim |
| pubmed-article:15385968 | lifeskim:mentions | umls-concept:C0285266 | lld:lifeskim |
| pubmed-article:15385968 | lifeskim:mentions | umls-concept:C1155649 | lld:lifeskim |
| pubmed-article:15385968 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:15385968 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:15385968 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:15385968 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:15385968 | lifeskim:mentions | umls-concept:C0444930 | lld:lifeskim |
| pubmed-article:15385968 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:15385968 | pubmed:dateCreated | 2004-9-29 | lld:pubmed |
| pubmed-article:15385968 | pubmed:abstractText | Nonhomologous end joining (NHEJ) is the major DNA double-strand break (DSB) repair pathway in mammalian cells. A critical step in this process is DNA ligation, involving the Xrcc4-DNA ligase IV complex. DNA end processing is often a prerequisite for ligation, but the coordination of these events is poorly understood. We show that polynucleotide kinase (PNK), with its ability to process ionizing radiation-induced 5'-OH and 3'-phosphate DNA termini, functions in NHEJ via an FHA-dependent interaction with CK2-phosphorylated Xrcc4. Analysis of the PNK FHA-Xrcc4 interaction revealed that the PNK FHA domain binds phosphopeptides with a unique selectivity among FHA domains. Disruption of the Xrcc4-PNK interaction in vivo is associated with increased radiosensitivity and slower repair kinetics of DSBs, in conjunction with a diminished efficiency of DNA end joining in vitro. Therefore, these results suggest a new role for Xrcc4 in the coordination of DNA end processing with DNA ligation. | lld:pubmed |
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| pubmed-article:15385968 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15385968 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15385968 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15385968 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:15385968 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:15385968 | pubmed:author | pubmed-author:WeinfeldMicha... | lld:pubmed |
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| pubmed-article:15385968 | pubmed:author | pubmed-author:MetalnikovPav... | lld:pubmed |
| pubmed-article:15385968 | pubmed:author | pubmed-author:O'DonnellPaul... | lld:pubmed |
| pubmed-article:15385968 | pubmed:author | pubmed-author:KochChristine... | lld:pubmed |
| pubmed-article:15385968 | pubmed:author | pubmed-author:GaliciaSarahS | lld:pubmed |
| pubmed-article:15385968 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15385968 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:15385968 | pubmed:volume | 23 | lld:pubmed |
| pubmed-article:15385968 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15385968 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15385968 | pubmed:pagination | 3874-85 | lld:pubmed |
| pubmed-article:15385968 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15385968 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15385968 | pubmed:articleTitle | Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV. | lld:pubmed |
| pubmed-article:15385968 | pubmed:affiliation | Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, ON, Canada. | lld:pubmed |
| pubmed-article:15385968 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15385968 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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