|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
15
|
|
pubmed:dateCreated |
1996-6-20
|
|
pubmed:abstractText |
The DNA-dependent protein kinase (DNA-PK) requires for activity free ends or other discontinuities in the structure of double strand DNA. In vitro, DNA-PK phosphorylates several transcription factors and other DNA-binding proteins and is thought to function in DNA damage recognition or repair and/or transcription. Here we show that in vitro DNA-PK undergoes autophosphorylation of all three protein subunits (DNA-PKcs, Ku p70 and Ku p80) and that phosphorylation correlates with inactivation of the serine/threonine kinase activity of DNA-PK. Significantly, activity is restored by the addition of purified native DNA-PKcs but not Ku, suggesting that inactivation is due to autophosphorylation of DNA-PKcs. Our data also suggest that autophosphorylation results in dissociation of DNA-PKcs from the Ku-DNA complex. We suggest that autophosphorylation is an important mechanism for the regulation of DNA-PK activity.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
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/Ku autoantigen,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PRKDC protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/XRCC5 protein, human
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
12
|
|
pubmed:volume |
271
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
8936-41
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:8621537-Adenosine Triphosphate,
pubmed-meshheading:8621537-Antigens, Nuclear,
pubmed-meshheading:8621537-Base Sequence,
pubmed-meshheading:8621537-DNA,
pubmed-meshheading:8621537-DNA Helicases,
pubmed-meshheading:8621537-DNA-Activated Protein Kinase,
pubmed-meshheading:8621537-DNA-Binding Proteins,
pubmed-meshheading:8621537-Enzyme Activation,
pubmed-meshheading:8621537-Humans,
pubmed-meshheading:8621537-Macromolecular Substances,
pubmed-meshheading:8621537-Molecular Sequence Data,
pubmed-meshheading:8621537-Nuclear Proteins,
pubmed-meshheading:8621537-Peptides,
pubmed-meshheading:8621537-Phosphorylation,
pubmed-meshheading:8621537-Placenta,
pubmed-meshheading:8621537-Protein Binding,
pubmed-meshheading:8621537-Protein-Serine-Threonine Kinases
|
|
pubmed:year |
1996
|
|
pubmed:articleTitle |
The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit.
|
|
pubmed:affiliation |
Department of Biological Sciences, University of Calgary, 2500 University Drive, N.W., Calgary, Alberta, T2N 1N4, Canada.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
