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Submitted on April 19, 2002
Accepted on December 9, 2002
1 Dept. of Life Science, Pohang University of Science and Technology, Pohang 790-784, Korea; Faculty of Marine Bioscience & Technology, Kangnung National University, Kangnung 210-702, Korea;Department of Biochemistry, College of Medicine, University of Ulsan, Seoul 138-736, Korea; Gene Expression Laboratory, The Salk Institute for Biological Studies, San Diego, CA 92037, USA Equal contributions Young Chang Sohn, Ph.D., Faculty of Marine Bioscience & Technology, Kangnung National University, Kangnung 210-702, Korea; Tel +82-33-640-2348, Fax +82-33-640-2410, E-mail ycsohn@kangnung.ac.kr
* To whom correspondence should be addressed. E-mail: jaewoon{at}postech.ac.kr.
Nuclear receptors adopt dramatically different conformations in the presence or absence of ligand, and such holo- and apo-receptors are specifically recognized by transcriptional coactivators and corepressors, respectively. These two states likely exist in dynamic equilibrium, contrary to the conventional model of static off and on conformations. First, corepressor SMRT [for silencing mediator of thyroid hormone receptor (TR) and retinoic acid receptor (RAR)] inhibits the interaction of coactivator steroid receptor coactivator-1 (SRC-1) with liganded-TR/RAR. Second, SMRT enables receptors to adopt apo-form even in the presence of ligand, as demonstrated with limited proteolyses and decreased binding of radio-labeled retinoid to RAR. Finally, chromatin immunoprecipitation results indicate that SMRT and SRC-1 dynamically compete for receptor bindings in vivo in the presence of ligand. These results suggest that corepressor binding can drive receptors to adopt the apo-state, even in the presence of ligand, and inhibit activated holo-nuclear receptors in vivo.
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