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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
28
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pubmed:dateCreated |
1993-11-24
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pubmed:abstractText |
The serum response factor (SRF) is a 67-kDa phosphoprotein that, together with auxiliary factors, modulates transcription of immediate early genes containing serum response elements in their promoters. Here we show that the carboxyl-terminal domain of human SRF is phosphorylated in vivo and is recognized in vitro by the double-stranded DNA-activated serine/threonine-specific protein kinase, DNA-PK. SRF phosphorylation by DNA-PK was stimulated by its cognate binding site. Protein microsequence analysis of a 22-amino acid synthetic SRF peptide and phosphopeptide analysis of genetically altered glutathione S-transferase-SRF fusion proteins identified Ser-435 and Ser-446 of human SRF as sites phosphorylated by DNA-PK. Both serines are followed by glutamine. Changing Gln-436 and Gln-447 to other residues reduced or eliminated phosphorylation by DNA-PK, confirming that these glutamines are important determinants for kinase recognition. The carboxyl-terminal transcription activation domain was mapped within a 71-amino acid region that contains both DNA-PK phosphorylation sites. Amino acid substitutions that interfered with phosphorylation by DNA-PK at Ser-435/446 in GAL4-SRF fusion proteins were reduced in transactivation potency. From these data we suggest that DNA-PK phosphorylation may modulate SRF activity in vivo.
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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/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
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/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PRKDC protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Response Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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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 |
5
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21147-54
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8407951-3T3 Cells,
pubmed-meshheading:8407951-Amino Acid Sequence,
pubmed-meshheading:8407951-Animals,
pubmed-meshheading:8407951-Base Sequence,
pubmed-meshheading:8407951-Binding Sites,
pubmed-meshheading:8407951-Cells, Cultured,
pubmed-meshheading:8407951-DNA,
pubmed-meshheading:8407951-DNA, Complementary,
pubmed-meshheading:8407951-DNA-Activated Protein Kinase,
pubmed-meshheading:8407951-DNA-Binding Proteins,
pubmed-meshheading:8407951-Fungal Proteins,
pubmed-meshheading:8407951-HeLa Cells,
pubmed-meshheading:8407951-Humans,
pubmed-meshheading:8407951-Mice,
pubmed-meshheading:8407951-Molecular Sequence Data,
pubmed-meshheading:8407951-Nuclear Proteins,
pubmed-meshheading:8407951-Phosphorylation,
pubmed-meshheading:8407951-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8407951-Recombinant Fusion Proteins,
pubmed-meshheading:8407951-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8407951-Serum Response Factor,
pubmed-meshheading:8407951-Transcription, Genetic,
pubmed-meshheading:8407951-Transcription Factors,
pubmed-meshheading:8407951-Transcriptional Activation
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pubmed:year |
1993
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pubmed:articleTitle |
The carboxyl-terminal transactivation domain of human serum response factor contains DNA-activated protein kinase phosphorylation sites.
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pubmed:affiliation |
Institute of Molecular Biology, Academia Sinica, NanKang, Taipei, Taiwan, Republic of China.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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