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J Biol Chem, Vol. 274, Issue 5, 2885-2892, January 29, 1999

Retinoid Isomers Differ in the Ability to Induce Release of SMRT Corepressor from Retinoic Acid Receptor-alpha

Suk-Hyun Hong and Martin L. Privalsky

From the Section of Microbiology, Division of Biological Sciences, University of California, Davis, California 95616

Nuclear hormone receptors are ligand-regulated transcription factors that modulate the expression of specific target genes in response to the binding of small, hydrophobic hormone ligands. Many nuclear hormone receptors, such as the retinoic acid receptors, can both repress and activate target gene expression; these bimodal transcription properties are mediated by the ability of these receptors to tether auxiliary factors, denoted corepressors and coactivators. Corepressors are typically bound by receptors in the absence of cognate hormone, whereas binding of an appropriate hormone agonist induces an allosteric alteration in the receptor resulting in release of the corepressor and recruitment of coactivator. Structural analysis indicates that there is a close induced fit between the hormone ligand and the receptor polypeptide chain. This observation suggests that different ligands, once bound, may confer distinct conformations on the receptor that may invoke, in turn, distinct functional consequences. We report here that different retinoids do differ in the ability to release corepressor once bound to retinoic acid receptor and suggest that these differences in corepressor release may manifest as differences in transcriptional regulation.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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