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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2006-3-17
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pubmed:abstractText |
The signaling/oncogenic activity of beta-catenin can be repressed by activation of the vitamin D receptor (VDR). Conversely, high levels of beta-catenin can potentiate the transcriptional activity of 1,25-dihydroxyvitamin D3 (1,25D). We show here that the effects of beta-catenin on VDR activity are due to interaction between the activator function-2 (AF-2) domain of the VDR and C terminus of beta-catenin. Acetylation of the beta-catenin C terminus differentially regulates its ability to activate TCF or VDR-regulated promoters. Mutation of a specific residue in the AF-2 domain, which renders the VDR trancriptionally inactive in the context of classical coactivators, still allows interaction with beta-catenin and ligand-dependent activation of VDRE-containing promoters. VDR antagonists, which block the VDRE-directed activity of the VDR and recruitment of classical coactivators, do allow VDR to interact with beta-catenin, which suggests that these and perhaps other ligands would permit those functions of the VDR that involve beta-catenin interaction.
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pubmed:grant |
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pubmed:commentsCorrections |
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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 |
Mar
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pubmed:issn |
1097-2765
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pubmed:author |
pubmed-author:ArandaAnaA,
pubmed-author:ByersStephen WSW,
pubmed-author:HerrellRogerR,
pubmed-author:IslamMd NaimulMN,
pubmed-author:MorasDinoD,
pubmed-author:NormanAnthonyA,
pubmed-author:RaoMahadevM,
pubmed-author:RizviImranI,
pubmed-author:ShahSalimuddinS,
pubmed-author:SivanesanDakshanamurthyD,
pubmed-author:ValranceMegganM,
pubmed-author:WelshJoEllenJ,
pubmed-author:ZinserGlendonG
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
799-809
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:16543149-Acetylation,
pubmed-meshheading:16543149-Amino Acid Sequence,
pubmed-meshheading:16543149-Animals,
pubmed-meshheading:16543149-Cell Line,
pubmed-meshheading:16543149-Gene Expression Regulation,
pubmed-meshheading:16543149-Humans,
pubmed-meshheading:16543149-Ligands,
pubmed-meshheading:16543149-Mice,
pubmed-meshheading:16543149-Models, Molecular,
pubmed-meshheading:16543149-Molecular Sequence Data,
pubmed-meshheading:16543149-Promoter Regions, Genetic,
pubmed-meshheading:16543149-Protein Binding,
pubmed-meshheading:16543149-Protein Conformation,
pubmed-meshheading:16543149-Receptors, Calcitriol,
pubmed-meshheading:16543149-Sequence Homology, Amino Acid,
pubmed-meshheading:16543149-Signal Transduction,
pubmed-meshheading:16543149-TCF Transcription Factors,
pubmed-meshheading:16543149-Transcription, Genetic,
pubmed-meshheading:16543149-Transfection,
pubmed-meshheading:16543149-beta Catenin
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pubmed:year |
2006
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pubmed:articleTitle |
The molecular basis of vitamin D receptor and beta-catenin crossregulation.
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pubmed:affiliation |
The Lombardi Comprehensive Cancer Center, Georgetown University School of Medicine, Washington, DC 20007, USA. ss234@georgetown.edu
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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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