Source:http://linkedlifedata.com/resource/pubmed/id/16582966
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
37
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pubmed:dateCreated |
2006-8-24
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pubmed:abstractText |
We have previously shown that interferon regulatory factor-2 (IRF-2) is acetylated in a cell growth-dependent manner, which enables it to contribute to the transcription of cell growth-regulated promoters. To clarify the function of acetylation of IRF-2, we investigated the proteins that associate with acetylated IRF-2. In 293T cells, the transfection of p300/CBP-associated factor (PCAF) enhanced the acetylation of IRF-2. In cells transfected with both IRF-2 and PCAF, IRF-2 associated with endogenous nucleolin, while in contrast, minimal association was observed when IRF-2 was transfected with a PCAF histone acetyl transferase (HAT) deletion mutant. In a pull-down experiment using stable transfectants, acetylation-defective mutant IRF-2 (IRF-2K75R) recruited nucleolin to a much lesser extent than wild-type IRF-2, suggesting that nucleolin preferentially associates with acetylated IRF-2. Nucleolin in the presence of PCAF enhanced IRF-2-dependent H4 promoter activity in NIH3T3 cells. Nucleolin knock-down using siRNA reduced the IRF-2/PCAF-mediated promoter activity. Chromatin immunoprecipitation analysis indicated that PCAF transfection increased nucleolin binding to IRF-2 bound to the H4 promoter. We conclude that nucleolin is recruited to acetylated IRF-2, thereby contributing to gene regulation crucial for the control of cell growth.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Histone Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/IRF2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Regulatory Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/nucleolin,
http://linkedlifedata.com/resource/pubmed/chemical/p300-CBP Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0950-9232
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5113-24
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:16582966-3T3 Cells,
pubmed-meshheading:16582966-Acetylation,
pubmed-meshheading:16582966-Amino Acid Substitution,
pubmed-meshheading:16582966-Animals,
pubmed-meshheading:16582966-Cell Line,
pubmed-meshheading:16582966-Gene Deletion,
pubmed-meshheading:16582966-Histone Acetyltransferases,
pubmed-meshheading:16582966-Humans,
pubmed-meshheading:16582966-Interferon Regulatory Factor-2,
pubmed-meshheading:16582966-Mice,
pubmed-meshheading:16582966-Mutation,
pubmed-meshheading:16582966-Phosphoproteins,
pubmed-meshheading:16582966-Promoter Regions, Genetic,
pubmed-meshheading:16582966-RNA-Binding Proteins,
pubmed-meshheading:16582966-Recombinant Proteins,
pubmed-meshheading:16582966-Transcriptional Activation,
pubmed-meshheading:16582966-Transfection,
pubmed-meshheading:16582966-p300-CBP Transcription Factors
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pubmed:year |
2006
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pubmed:articleTitle |
Nucleolin is involved in interferon regulatory factor-2-dependent transcriptional activation.
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pubmed:affiliation |
Department of Safety Research on Blood and Biological Products, National Institute of Infectious Diseases, Musashimurayama-shi, Tokyo, Japan. amasumi@nih.go.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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