The molecular basis of vitamin D receptor and β-catenin crossregulation
The molecular basis of vitamin D receptor and β-catenin crossregulation
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DOI：
10.1016/j.molcel.2006.01.037
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发表时间：
2006-03-17
期刊：
影响因子：
16
通讯作者：
Byers, SW
中科院分区：
文献类型：
--
作者：
Shah, S;Islam, N;Byers, SW
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The signaling/oncogenic activity of P-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-dihydroxy-vitamin 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.