| pubmed-article:11279128 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11279128 | lifeskim:mentions | umls-concept:C0212694 | lld:lifeskim |
| pubmed-article:11279128 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:11279128 | lifeskim:mentions | umls-concept:C0242617 | lld:lifeskim |
| pubmed-article:11279128 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
| pubmed-article:11279128 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:11279128 | lifeskim:mentions | umls-concept:C0124761 | lld:lifeskim |
| pubmed-article:11279128 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:11279128 | pubmed:dateCreated | 2001-5-23 | lld:pubmed |
| pubmed-article:11279128 | pubmed:abstractText | The Ku antigen (70- and 80-kDa subunits) is a regulatory subunit of DNA-dependent protein kinase (DNA-PK) that promotes the recruitment of the catalytic subunit of DNA-PK (DNA-PKcs) to DNA ends and to specific DNA sequences from which the kinase is activated. Ku and DNA-PKcs plays essential roles in double-stranded DNA break repair and V(D)J recombination and have been implicated in the regulation of specific gene transcription. In a yeast two-hybrid screen of a Jurkat T cell cDNA library, we have identified a specific interaction between the 70-kDa subunit of Ku heterodimer and the homeodomain of HOXC4, a homeodomain protein expressed in the hematopoietic system. Unexpectedly, a similar interaction with Ku was observed for several additional homeodomain proteins including octamer transcription factors 1 and 2 and Dlx2, suggesting that specific binding to Ku may be a property shared by many homeodomain proteins. Ku-homeodomain binding was mediated through the extreme C terminus of Ku70 and was abrogated by amino acid substitutions at Lys595/Lys596. Ku binding allowed the recruitment of the homeodomain to DNA ends and dramatically enhanced the phosphorylation of homeodomain-containing proteins by DNA-PK. These results suggest that Ku functions as a substrate docking protein for signaling by DNA-PK to homeodomain proteins from DNA ends. | lld:pubmed |
| pubmed-article:11279128 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11279128 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11279128 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11279128 | pubmed:month | May | lld:pubmed |
| pubmed-article:11279128 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11279128 | pubmed:author | pubmed-author:PoppGG | lld:pubmed |
| pubmed-article:11279128 | pubmed:author | pubmed-author:HachéR JRJ | lld:pubmed |
| pubmed-article:11279128 | pubmed:author | pubmed-author:NgseeJ KJK | lld:pubmed |
| pubmed-article:11279128 | pubmed:author | pubmed-author:GiffinWW | lld:pubmed |
| pubmed-article:11279128 | pubmed:author | pubmed-author:Schild-Poulte... | lld:pubmed |
| pubmed-article:11279128 | pubmed:author | pubmed-author:Traykova-Ando... | lld:pubmed |
| pubmed-article:11279128 | pubmed:author | pubmed-author:KochanJ CJC | lld:pubmed |
| pubmed-article:11279128 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11279128 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:11279128 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:11279128 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11279128 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11279128 | pubmed:pagination | 16848-56 | lld:pubmed |
| pubmed-article:11279128 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11279128 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11279128 | pubmed:articleTitle | The binding of Ku antigen to homeodomain proteins promotes their phosphorylation by DNA-dependent protein kinase. | lld:pubmed |
| pubmed-article:11279128 | pubmed:affiliation | Department of Medicine, The Loeb Health Research Institute at the Ottawa Hospital, University of Ottawa, Ottawa, Ontario K1Y 4E9, Canada. | lld:pubmed |
| pubmed-article:11279128 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11279128 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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