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Originally published In Press as doi:10.1074/jbc.C200712200 on January 15, 2003

J. Biol. Chem., Vol. 278, Issue 10, 8224-8228, March 7, 2003
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Interactions of SKIP/NCoA-62, TFIIB, and Retinoid X Receptor with Vitamin D Receptor Helix H10 Residues*

Janelle B. BarryDagger , Gary M. Leong§, W. Bret Church||, Laura L. Issa**, John A. Eisman, and Edith M. GardinerDagger Dagger

From the Bone and Mineral Research Program and  Molecular Modeling Facility, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney NSW 2010, Australia

The vitamin D receptor (VDR) is a ligand-dependent transcription factor that heterodimerizes with retinoid X receptor (RXR) and interacts with the basal transcription machinery and transcriptional cofactors to regulate target gene activity. The p160 coactivator GRIP1 and the distinct coregulator Ski-interacting protein (SKIP)/NCoA-62 synergistically enhance ligand-dependent VDR transcriptional activity. Both coregulators bind directly to and form a ternary complex with VDR, with GRIP1 contacting the activation function-2 (AF-2) domain and SKIP/NCoA-62 interacting through an AF-2 independent interface. It was previously reported that SKIP/NCoA-62 interaction with VDR was independent of the heterodimerization interface (specifically, helices H10/H11). In contrast, the present study defines specific residues within a conserved and surface-exposed region of VDR helix H10 that are required for interaction with SKIP/NCoA-62 and for full ligand-dependent transactivation activity. SKIP/NCoA-62, the basal transcription factor TFIIB, and RXR all interacted with VDR helix H10 mutants at reduced levels compared with wild type in the absence of ligand and exhibited different degrees of increased interaction upon ligand addition. Thus, SKIP/NCoA-62 interacts with VDR at a highly conserved region not previously associated with coregulator binding to regulate transactivation by a molecular mechanism distinct from that of p160 coactivators.

* This work was supported in part by Aza Research Pty. Ltd. and by a block grant from the Australian National Health & Medical Research Council.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Recipient of an Australian Postgraduate Award. Current address: Molecular Oncology Group, McGill University, Montreal, Quebec H3A 1A1, Canada.

§ Recipient of an Australian National Health & Medical Research Council Postgraduate Medical Scholarship during this study. Current address: Pituitary Research Unit, Garvan Inst. of Medical Research, Sydney 2010, Australia.

|| Current address: School of Molecular and Microbial Biosciences, Dept. of Biochemistry, University of Sydney, Sydney 2006, Australia.

** Recipient of an Australian Postgraduate Award. Current address: Gene Regulation Unit, Victor Chang Cardiac Research Inst., Sydney 2010, Australia.

Dagger Dagger To whom correspondence should be addressed: Bone and Mineral Research Program, Garvan Inst. of Medical Research, 384 Victoria St., Darlinghurst, Sydney NSW 2010, Australia. Tel.: 61-2-9295-8248; Fax: 61-2-9295-8241; E-mail: e.gardiner@garvan.org.au.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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