pubmed-article:10085149 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10085149 | lifeskim:mentions | umls-concept:C0227525 | lld:lifeskim |
pubmed-article:10085149 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
pubmed-article:10085149 | lifeskim:mentions | umls-concept:C0003591 | lld:lifeskim |
pubmed-article:10085149 | lifeskim:mentions | umls-concept:C0256079 | lld:lifeskim |
pubmed-article:10085149 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:10085149 | lifeskim:mentions | umls-concept:C1336776 | lld:lifeskim |
pubmed-article:10085149 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
pubmed-article:10085149 | pubmed:issue | 13 | lld:pubmed |
pubmed-article:10085149 | pubmed:dateCreated | 1999-4-29 | lld:pubmed |
pubmed-article:10085149 | pubmed:abstractText | Hepatocyte nuclear factor-4 (HNF-4) is a liver-enriched transcription factor that is crucial in the regulation of a large number of genes involved in glucose, cholesterol, and fatty acid metabolism and in determining the hepatic phenotype. We have previously shown that HNF-4 contains transcription activation functions at the N terminus (AF-1) and the C terminus (AF-2) which work synergistically to confer full HNF-4 activity. Here, we show that HNF-4 recruits the CREB-binding protein (CBP) coactivator on promoters of genes that contain functional HNF-4 sites. HNF-4 interacts with the N-terminal region of CBP (amino acids 1-771) and the C-terminal region of CBP (amino acids 1812-2441). The two activating functions of HNF-4, AF-1 and AF-2, interact with the N terminus and the N and C terminus of CBP, respectively. In addition, we show that in contrast to the other nuclear hormone receptors the interaction between HNF-4 and CBP is ligand-independent. Recruitment of CBP by HNF-4 results in an enhancement of the transcriptional activity of the latter. CBP does not activate gene expression in the absence of HNF-4, and dominant negative forms of HNF-4 prevent transcriptional activation by CBP, suggesting that the mere recruitment of CBP by HNF-4 is not sufficient for enhancement of gene expression. These findings demonstrate that CBP acts as a transcriptional coactivator for HNF-4 and provide new insights into the regulatory function of HNF-4. | lld:pubmed |
pubmed-article:10085149 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10085149 | pubmed:language | eng | lld:pubmed |
pubmed-article:10085149 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10085149 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10085149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10085149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10085149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10085149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:10085149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10085149 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10085149 | pubmed:month | Mar | lld:pubmed |
pubmed-article:10085149 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:10085149 | pubmed:author | pubmed-author:Hadzopoulou-C... | lld:pubmed |
pubmed-article:10085149 | pubmed:author | pubmed-author:DeluCC | lld:pubmed |
pubmed-article:10085149 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10085149 | pubmed:day | 26 | lld:pubmed |
pubmed-article:10085149 | pubmed:volume | 274 | lld:pubmed |
pubmed-article:10085149 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10085149 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10085149 | pubmed:pagination | 9013-21 | lld:pubmed |
pubmed-article:10085149 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:10085149 | pubmed:meshHeading | pubmed-meshheading:10085149... | lld:pubmed |
pubmed-article:10085149 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10085149 | pubmed:articleTitle | CREB-binding protein is a transcriptional coactivator for hepatocyte nuclear factor-4 and enhances apolipoprotein gene expression. | lld:pubmed |
pubmed-article:10085149 | pubmed:affiliation | Department of Medicine, Section of Molecular Genetics, Cardiovascular Institute, Boston University School of Medicine, Center for Advanced Biomedical Research, Boston, Massachusetts 02118-2394, USA. | lld:pubmed |
pubmed-article:10085149 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10085149 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10085149 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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