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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
28
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pubmed:dateCreated |
2003-7-4
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pubmed:abstractText |
deltaEF1 and SIP1 (or Zfhx1a and Zfhx1b, respectively) are the only known members of the vertebrate Zfh1 family of homeodomain/zinc finger-containing proteins. Similar to other transcription factors, both Smad-interacting protein-1 (SIP1) and deltaEF1 are capable of repressing E-cadherin transcription through binding to the E2 boxes located in its promoter. In the case of deltaEF1, this repression has been proposed to occur via interaction with the corepressor C-terminal binding protein (CtBP). In this study, we show by coimmunoprecipitation that SIP1 and CtBP interact in vivo and that an isolated CtBP-binding SIP1 fragment depends on CtBP for transcriptional repression. However, and most importantly, full-length SIP1 and deltaEF1 proteins do not depend on their interaction with CtBP to repress transcription from the E-cadherin promoter. Furthermore, in E-cadherin-positive kidney epithelial cells, the conditional synthesis of mutant SIP1 that cannot bind to CtBP abrogates endogenous E-cadherin expression in a similar way as wild-type SIP1. Our results indicate that full-length SIP1 can repress E-cadherin in a CtBP-independent manner.
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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/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ZEB2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Zfhx1b protein, mouse
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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 |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
26135-45
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pubmed:dateRevised |
2007-5-30
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pubmed:meshHeading |
pubmed-meshheading:12714599-Alcohol Oxidoreductases,
pubmed-meshheading:12714599-Amino Acid Motifs,
pubmed-meshheading:12714599-Animals,
pubmed-meshheading:12714599-Binding Sites,
pubmed-meshheading:12714599-Blotting, Western,
pubmed-meshheading:12714599-Cadherins,
pubmed-meshheading:12714599-Cell Line,
pubmed-meshheading:12714599-Cells, Cultured,
pubmed-meshheading:12714599-DNA-Binding Proteins,
pubmed-meshheading:12714599-Dogs,
pubmed-meshheading:12714599-Down-Regulation,
pubmed-meshheading:12714599-Gene Expression Regulation,
pubmed-meshheading:12714599-Genes, Reporter,
pubmed-meshheading:12714599-Homeodomain Proteins,
pubmed-meshheading:12714599-Humans,
pubmed-meshheading:12714599-Luciferases,
pubmed-meshheading:12714599-Mice,
pubmed-meshheading:12714599-Microscopy, Fluorescence,
pubmed-meshheading:12714599-Models, Genetic,
pubmed-meshheading:12714599-Mutation,
pubmed-meshheading:12714599-Peptides,
pubmed-meshheading:12714599-Phosphoproteins,
pubmed-meshheading:12714599-Plasmids,
pubmed-meshheading:12714599-Precipitin Tests,
pubmed-meshheading:12714599-Protein Binding,
pubmed-meshheading:12714599-Protein Structure, Tertiary,
pubmed-meshheading:12714599-Repressor Proteins,
pubmed-meshheading:12714599-Transcription, Genetic,
pubmed-meshheading:12714599-Transfection,
pubmed-meshheading:12714599-Tumor Cells, Cultured,
pubmed-meshheading:12714599-Two-Hybrid System Techniques,
pubmed-meshheading:12714599-Up-Regulation
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pubmed:year |
2003
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pubmed:articleTitle |
Interaction between Smad-interacting protein-1 and the corepressor C-terminal binding protein is dispensable for transcriptional repression of E-cadherin.
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pubmed:affiliation |
Department of Developmental Biology (VIB7), Flanders Interuniversity Institute for Biotechnology (VIB) and Laboratory of Molecular Biology (Celgen), University of Leuven, Herestraat 49, B-3000 Leuven, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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