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Papers In Press, published online ahead of print August 20, 2001
J. Biol. Chem, 10.1074/jbc.M106263200
Submitted on July 5, 2001
Revised on August 17, 2001
Accepted on August 17, 2001
Department of Pharmacology, Case Western Reserve University, Cleveland, OH 44106
Corresponding Author: pnm2{at}po.cwru.edu
The vitamin D receptor (VDR) is a ligand-dependent transcriptional factor that binds to vitamin D-responsive promoter elements as a heterodimer with retinoid X receptor (RXR) to regulate target gene. The steroid receptor coactivator (SRC) proteins are coactivators that interact with the AF-2 activation domain of VDR to augment 1,25-(OH)2 D3 -dependent transcription. In contrast, NCoA-62/SKIP is a distinct, AF-2 independent coactivator for VDR. The current study examined whether these two distinct classes of coactivators impact functionally on VDR-mediated transcription. Using a ternary protein complex binding assay, we observed a marked preference for the direct interaction of NCoA-62/SKIP with liganded VDR-RXR heterodimer as compared to the VDR-VDR homodimer or VDR monomer. The 1,25-(OH)2 D3 liganded VDR also formed a ternary complex with NCoA-62/SKIP and SRC proteins in vitro. Competition experiments using LXXLL peptides showed that NCoA-62/SKIP and SRC coactivators contact different domains of the VDR-RXR heterodimer. Synergistic interplays were observed between NCoA-62/SKIP and SRC coactivators in VDR-mediated transcriptional assays, and protein interference assays indicated a requirement for both NCoA-62/SKIP and SRCs in VDR-mediated transcription. These studies suggest that the ligand-dependent and simultaneous interaction of NCoA-62/SKIP and SRC coactivators with distinct interaction domains within the VDR-RXR heterodimer results in cooperative interplays between coactivators in VDR-mediated transcription.
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