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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2006-2-1
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pubmed:abstractText |
We previously demonstrated that formation of complexes between the DNA-binding domains of hepatocyte nuclear factor 6 (HNF6) and forkhead box a2 (Foxa2) proteins stimulated Foxa2 transcriptional activity. Here, we used HepG2 cell cotransfection assays to demonstrate that HNF6 transcriptional activity was stimulated by CCAAT/enhancer-binding protein alpha (C/EBPalpha), but not by the related C/EBPbeta or C/EBPdelta proteins. Formation of the C/EBPalpha-HNF6 protein complex required the HNF6 cut domain and the C/EBPalpha activation domain (AD) 1/AD2 sequences. This C/EBPalpha-HNF6 transcriptional synergy required both the N-terminal HNF6 polyhistidine and serine/threonine/proline box sequences, as well as the C/EBPalpha AD1/AD2 sequences, the latter of which are known to recruit the CREB binding protein (CBP) transcriptional coactivator. Consistent with these findings, adenovirus E1A-mediated inhibition of p300/CBP histone acetyltransferase activity abrogated C/EBPalpha-HNF6 transcriptional synergy in cotransfection assays. Co-immunoprecipitation assays with liver protein extracts demonstrate an association between the HNF6 and C/EBPalpha transcription factors and the CBP coactivator protein in vivo. Furthermore, chromatin immunoprecipitation assays with hepatoma cells demonstrated that increased levels of both C/EBPalpha and HNF6 proteins were required to stimulate association of these transcription factors and the CBP coactivator protein with the endogenous mouse Foxa2 promoter region. In conclusion, formation of the C/EBPalpha-HNF6 protein complex stimulates recruitment of the CBP coactivator protein for expression of Foxa2, a transcription factor critical for regulating expression of hepatic gluconeogenic genes during fasting.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-10811635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-11027295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-11340085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-11369759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-11559745,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-11684017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-11763995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-11915024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-12054904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-12482952,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-14647040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-15082532,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-15292250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-15380251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-16098831,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-2558052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-2683088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-7652557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-8344962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-8524667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-8664543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-8790352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-9401069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-9441664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-9614204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-9822619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16440369-9915796
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0270-9139
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
43
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
276-86
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16440369-Amino Acid Sequence,
pubmed-meshheading:16440369-Animals,
pubmed-meshheading:16440369-CCAAT-Enhancer-Binding Protein-alpha,
pubmed-meshheading:16440369-CREB-Binding Protein,
pubmed-meshheading:16440369-Cell Line, Tumor,
pubmed-meshheading:16440369-Chromatin Immunoprecipitation,
pubmed-meshheading:16440369-Hepatocyte Nuclear Factor 3-beta,
pubmed-meshheading:16440369-Hepatocyte Nuclear Factor 6,
pubmed-meshheading:16440369-Humans,
pubmed-meshheading:16440369-Mice,
pubmed-meshheading:16440369-Multiprotein Complexes,
pubmed-meshheading:16440369-Promoter Regions, Genetic,
pubmed-meshheading:16440369-Transcription, Genetic,
pubmed-meshheading:16440369-Transfection
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pubmed:year |
2006
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pubmed:articleTitle |
C/EBPalpha and HNF6 protein complex formation stimulates HNF6-dependent transcription by CBP coactivator recruitment in HepG2 cells.
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pubmed:affiliation |
Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, College of Medicine, Chicago, IL 60607-7170, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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