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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2003-6-5
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pubmed:abstractText |
Serum stimulation leads to activation of the serum response factor (SRF)-mediated transcription of immediate-early genes such as c-fos via various signal transduction pathways. We have previously reported that promyelocytic leukemia protein (PML) is involved in the transcriptional regulation by SRF. PML is one of the well-known substrates for modification by small ubiquitin-related modifier-1 (SUMO-1) and several SUMO-1-modified proteins associate with PML. Here, we report that SRF is modified by SUMO-1 chiefly at lysine(147) within the DNA-binding domain. Substitution of this target lysine for alanine did not affect the translocation of SRF to PML-nuclear bodies. The SRF mutant augmented the transcriptional activity under Rho A-stimulated condition but not under serum-starved condition, suggesting that activated SRF is suppressed by its sumoylation. These data support the transcriptional role of SUMO-1 conjugating system in cellular serum response.
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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, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PML protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO-1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Response Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
306
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
32-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12788062-Amino Acid Sequence,
pubmed-meshheading:12788062-Animals,
pubmed-meshheading:12788062-Base Sequence,
pubmed-meshheading:12788062-Binding Sites,
pubmed-meshheading:12788062-DNA, Complementary,
pubmed-meshheading:12788062-HeLa Cells,
pubmed-meshheading:12788062-Humans,
pubmed-meshheading:12788062-Lysine,
pubmed-meshheading:12788062-Neoplasm Proteins,
pubmed-meshheading:12788062-Nuclear Proteins,
pubmed-meshheading:12788062-Protein Processing, Post-Translational,
pubmed-meshheading:12788062-Protein Structure, Tertiary,
pubmed-meshheading:12788062-Recombinant Proteins,
pubmed-meshheading:12788062-SUMO-1 Protein,
pubmed-meshheading:12788062-Serum Response Factor,
pubmed-meshheading:12788062-Transcription, Genetic,
pubmed-meshheading:12788062-Transcription Factors,
pubmed-meshheading:12788062-Tumor Suppressor Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Serum response factor is modulated by the SUMO-1 conjugation system.
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pubmed:affiliation |
Department of Regeneration Medicine, Institute of Molecular Embryology and Genetics, Kumamoto University, 2-2-1 Honjo, 860-0811, Kumamoto, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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