Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with vitamin D receptor helix H10 residues

Barry, Janelle B., Leong, Gary M., Church, W. Bret, Issa, Laura L., Eisman, John A. and Gardiner, Edith M. (2003) Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with vitamin D receptor helix H10 residues. Journal of Biological Chemistry, 278 10: 8224-8228. doi:10.1074/jbc.C200712200

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Author Barry, Janelle B.
Leong, Gary M.
Church, W. Bret
Issa, Laura L.
Eisman, John A.
Gardiner, Edith M.
Title Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with vitamin D receptor helix H10 residues
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2003-03-07
Sub-type Article (original research)
DOI 10.1074/jbc.C200712200
Open Access Status File (Publisher version)
Volume 278
Issue 10
Start page 8224
End page 8228
Total pages 5
Place of publication Bethesda
Publisher Amer Soc Biochemistry Molecular Biology Inc
Language eng
Subject 0601 Biochemistry and Cell Biology
0904 Chemical Engineering
Abstract 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.
Keyword Biochemistry & Molecular Biology
Transcription Factor-iib
D-mediated Transcription
Crystal-structure
Nuclear Receptors
Protein
Binding
Ligand
Domain
Skip
Activation
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Citation counts: TR Web of Science Citation Count  Cited 38 times in Thomson Reuters Web of Science Article | Citations
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Created: Wed, 19 Sep 2007, 16:44:33 EST