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rdf:type |
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lifeskim:mentions |
umls-concept:C0205054,
umls-concept:C0521447,
umls-concept:C0542341,
umls-concept:C0851285,
umls-concept:C1336789,
umls-concept:C1514562,
umls-concept:C1521761,
umls-concept:C1707271,
umls-concept:C1879547,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
9
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pubmed:dateCreated |
1998-6-16
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pubmed:abstractText |
Hepatic nuclear factor 4 (HNF4) is a transcription factor whose expression is crucial for mouse embryonic development, for liver-specific gene expression and for the prevention of one form of maturity-onset diabetes of the young. Its domain structure has been defined previously and is similar to other members of the nuclear receptor superfamily. A repressor domain has now been localised to a region of 14 amino acids (residues 428-441) near the C-terminus of HNF4 and is sufficient by itself to repress the activity of the activation function 2 (AF2) domain. Multiple mutations within this repressor domain enhance activity. Interestingly, this repressor domain shares homology with a repressor domain in the progesterone receptor. In a detailed mutagenesis study of the AF2 core, we demonstrate that L 366, which is conserved in the AF2 core between HNF4 and a number of orphan nuclear receptors, is essential for the full activity of the AF2 domain. Furthermore, a double mutation of E 363 and L 366 suggests that these residues might act in a cooperative manner.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-1372244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-1610903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-1631558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-2279702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-7501014,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-7891708,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-7958910,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-8389696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-8446579,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-8521510,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-8562402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-8622695,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-8657158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-8901556,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-8945471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-8995295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-9001222,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-9153304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9547266-9233568
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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/Basic Helix-Loop-Helix Leucine...,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAL4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatocyte Nuclear Factor 4,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tcfl4 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0305-1048
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
26
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2098-104
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9547266-Amino Acid Sequence,
pubmed-meshheading:9547266-Animals,
pubmed-meshheading:9547266-Basic Helix-Loop-Helix Leucine Zipper Transcription Factors,
pubmed-meshheading:9547266-DNA Mutational Analysis,
pubmed-meshheading:9547266-DNA-Binding Proteins,
pubmed-meshheading:9547266-Hepatocyte Nuclear Factor 4,
pubmed-meshheading:9547266-Molecular Sequence Data,
pubmed-meshheading:9547266-Mutagenesis,
pubmed-meshheading:9547266-Phosphoproteins,
pubmed-meshheading:9547266-Proline,
pubmed-meshheading:9547266-Rats,
pubmed-meshheading:9547266-Recombinant Fusion Proteins,
pubmed-meshheading:9547266-Repressor Proteins,
pubmed-meshheading:9547266-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9547266-Transcription Factors,
pubmed-meshheading:9547266-Transcriptional Activation
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pubmed:year |
1998
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pubmed:articleTitle |
The activation function 2 domain of hepatic nuclear factor 4 is regulated by a short C-terminal proline-rich repressor domain.
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pubmed:affiliation |
Chemical Pathology Unit, Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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