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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
2001-5-23
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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.
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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/Adrenocorticotropic Hormone,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Activated Protein Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAL4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/HOXC4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hoxc4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ku autoantigen,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Octamer Transcription Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/POU2F2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/PRKDC protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Pou2f2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/XRCC5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/high affinity DNA-binding factor...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16848-56
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11279128-Adrenocorticotropic Hormone,
pubmed-meshheading:11279128-Amino Acid Sequence,
pubmed-meshheading:11279128-Animals,
pubmed-meshheading:11279128-Antigens, Nuclear,
pubmed-meshheading:11279128-Chickens,
pubmed-meshheading:11279128-Cloning, Molecular,
pubmed-meshheading:11279128-Cricetinae,
pubmed-meshheading:11279128-DNA Helicases,
pubmed-meshheading:11279128-DNA-Activated Protein Kinase,
pubmed-meshheading:11279128-DNA-Binding Proteins,
pubmed-meshheading:11279128-Dimerization,
pubmed-meshheading:11279128-Fungal Proteins,
pubmed-meshheading:11279128-Gene Expression Regulation,
pubmed-meshheading:11279128-Homeodomain Proteins,
pubmed-meshheading:11279128-Humans,
pubmed-meshheading:11279128-Jurkat Cells,
pubmed-meshheading:11279128-Mice,
pubmed-meshheading:11279128-Molecular Sequence Data,
pubmed-meshheading:11279128-Nuclear Proteins,
pubmed-meshheading:11279128-Octamer Transcription Factor-2,
pubmed-meshheading:11279128-Phosphorylation,
pubmed-meshheading:11279128-Protein Binding,
pubmed-meshheading:11279128-Protein Biosynthesis,
pubmed-meshheading:11279128-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11279128-Recombinant Proteins,
pubmed-meshheading:11279128-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11279128-Sequence Alignment,
pubmed-meshheading:11279128-Sequence Deletion,
pubmed-meshheading:11279128-Sequence Homology, Amino Acid,
pubmed-meshheading:11279128-Ticks,
pubmed-meshheading:11279128-Transcription, Genetic,
pubmed-meshheading:11279128-Transcription Factors,
pubmed-meshheading:11279128-Xenopus
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pubmed:year |
2001
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pubmed:articleTitle |
The binding of Ku antigen to homeodomain proteins promotes their phosphorylation by DNA-dependent protein kinase.
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pubmed:affiliation |
Department of Medicine, The Loeb Health Research Institute at the Ottawa Hospital, University of Ottawa, Ottawa, Ontario K1Y 4E9, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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