Mol Cell 2006,
PMID: 16543149
Shah, Salimuddin; Islam, Md Naimul; Dakshanamurthy, Sivanesan; Rizvi, Imran; Rao, Mahadev; Herrell, Roger; Zinser, Glendon; Valrance, Meggan; Aranda, Ana; Moras, Dino; Norman, Anthony; Welsh, JoEllen; Byers, Stephen W
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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Text Mining Data
beta-catenin ⊣ vitamin D receptor (VDR): "
The signaling/oncogenic activity of
beta-catenin can be
repressed by activation of the
vitamin D receptor (VDR)
"
VDR — beta-catenin: "
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
"
VDR → beta-catenin: "
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
"
Manually curated Databases
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