rdf:type |
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lifeskim:mentions |
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pubmed:issue |
30
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pubmed:dateCreated |
2001-7-23
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pubmed:abstractText |
AP-2 transcription factors execute important functions during embryonic development and malignant transformation. Recently, we have isolated a transcriptional repressor of AP-2alpha expression, the novel Krüppel-related zinc finger protein AP-2rep (Klf12). Here, we show that repression of AP-2alpha transcription by AP-2rep is dependent on an N-terminal PVDLS motif that interacts specifically with the corepressor CtBP1 both in vivo and in vitro. This interaction motif was previously identified in the C-terminal region of the adenoviral oncoprotein E1A. Infection of both HeLa and PA-1 cells with adenovirus type 5 strongly induced AP-2alpha mRNA. Consistently, E1A was necessary and sufficient to mediate up-regulation of AP-2alpha. Transiently transfected wild-type E1A protein activated an AP-2rep sensitive cis-regulatory element of the AP-2alpha promoter, but E1A protein harboring a mutation in the PVDLS motif failed to activate. In summary, we conclude that the adenoviral oncoprotein E1A activates transcription from the endogenous AP-2alpha gene, an effect that involves transcriptional derepression of the AP-2alpha promoter by interaction of E1A with the AP-2rep corepressor CtBP1.
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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/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/C-terminal binding protein,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/TFAP2A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tcfap2a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-2,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27944-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:11373277-Adenoviridae,
pubmed-meshheading:11373277-Alcohol Oxidoreductases,
pubmed-meshheading:11373277-Amino Acid Motifs,
pubmed-meshheading:11373277-Amino Acid Sequence,
pubmed-meshheading:11373277-Animals,
pubmed-meshheading:11373277-Blotting, Western,
pubmed-meshheading:11373277-Cells, Cultured,
pubmed-meshheading:11373277-DNA, Complementary,
pubmed-meshheading:11373277-DNA-Binding Proteins,
pubmed-meshheading:11373277-Enzyme Activation,
pubmed-meshheading:11373277-HeLa Cells,
pubmed-meshheading:11373277-Humans,
pubmed-meshheading:11373277-Mice,
pubmed-meshheading:11373277-Molecular Sequence Data,
pubmed-meshheading:11373277-Mutagenesis, Site-Directed,
pubmed-meshheading:11373277-Mutation,
pubmed-meshheading:11373277-Phosphoproteins,
pubmed-meshheading:11373277-Plasmids,
pubmed-meshheading:11373277-Precipitin Tests,
pubmed-meshheading:11373277-Promoter Regions, Genetic,
pubmed-meshheading:11373277-Protein Binding,
pubmed-meshheading:11373277-Protein Structure, Tertiary,
pubmed-meshheading:11373277-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:11373277-RNA, Messenger,
pubmed-meshheading:11373277-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11373277-Transcription, Genetic,
pubmed-meshheading:11373277-Transcription Factor AP-2,
pubmed-meshheading:11373277-Transcription Factors,
pubmed-meshheading:11373277-Transfection,
pubmed-meshheading:11373277-Two-Hybrid System Techniques
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pubmed:year |
2001
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pubmed:articleTitle |
Induction of AP-2alpha expression by adenoviral infection involves inactivation of the AP-2rep transcriptional corepressor CtBP1.
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pubmed:affiliation |
Institute for Microbiology, University of Regensburg Medical School, Franz-Josef-Strauss-Allee 11, D-93042 Regensburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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