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rdf:type |
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lifeskim:mentions |
umls-concept:C0031715,
umls-concept:C0140279,
umls-concept:C0172237,
umls-concept:C0542341,
umls-concept:C1135650,
umls-concept:C1167622,
umls-concept:C1334084,
umls-concept:C1334196,
umls-concept:C1413288,
umls-concept:C1419034,
umls-concept:C1879547,
umls-concept:C1948023
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pubmed:issue |
1
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pubmed:dateCreated |
1997-8-26
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pubmed:abstractText |
The activity of the N-terminal activation function AF-1 of RAR alpha1 is abrogated upon mutation of a phosphorylatable serine residue (Ser-77). Recombinant RAR alpha was phosphorylated by a variety of proline-directed protein kinases in vitro. However, only the coexpression of cdk7 stimulated Ser-77 phosphorylation in vivo and enhanced transactivation by RAR alpha, but not by a S77A RAR mutant. Both free CAK (cdk7, cyclin H, MAT1) and the CAK-containing general transcription factor TFIIH phosphorylated Ser-77 in vitro. Furthermore RAR alpha bound free CAK and purified TFIIH in vitro, and RAR alpha-TFIIH complexes could be isolated from HeLa nuclear extracts. These findings represent the first example of activation of a transactivator through binding to and phosphorylation by a general transcription factor.
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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/Cyclin-Dependent Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Retinoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor TFIIH,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, TFII,
http://linkedlifedata.com/resource/pubmed/chemical/cyclin-dependent kinase-activating...,
http://linkedlifedata.com/resource/pubmed/chemical/retinoic acid receptor alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
97-107
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9230306-Amino Acid Sequence,
pubmed-meshheading:9230306-Animals,
pubmed-meshheading:9230306-COS Cells,
pubmed-meshheading:9230306-Cell Nucleus,
pubmed-meshheading:9230306-Cyclin-Dependent Kinases,
pubmed-meshheading:9230306-DNA Helicases,
pubmed-meshheading:9230306-Dimerization,
pubmed-meshheading:9230306-HeLa Cells,
pubmed-meshheading:9230306-Humans,
pubmed-meshheading:9230306-Molecular Sequence Data,
pubmed-meshheading:9230306-Mutagenesis, Site-Directed,
pubmed-meshheading:9230306-Phosphorylation,
pubmed-meshheading:9230306-Point Mutation,
pubmed-meshheading:9230306-Protein-Serine-Threonine Kinases,
pubmed-meshheading:9230306-Receptors, Retinoic Acid,
pubmed-meshheading:9230306-Recombinant Fusion Proteins,
pubmed-meshheading:9230306-Recombinant Proteins,
pubmed-meshheading:9230306-Sequence Alignment,
pubmed-meshheading:9230306-Serine,
pubmed-meshheading:9230306-Trans-Activators,
pubmed-meshheading:9230306-Transcription Factor TFIIH,
pubmed-meshheading:9230306-Transcription Factors,
pubmed-meshheading:9230306-Transcription Factors, TFII,
pubmed-meshheading:9230306-Transcriptional Activation,
pubmed-meshheading:9230306-Transfection
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pubmed:year |
1997
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pubmed:articleTitle |
Stimulation of RAR alpha activation function AF-1 through binding to the general transcription factor TFIIH and phosphorylation by CDK7.
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pubmed:affiliation |
Centre National de la Recherche Scientifique, Institut National de la Santé et de la Recherche Médicale, Université Louis Pasteur, Collège de France, Illkirch, Strasbourg.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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