Retinoids and Receptor Interacting Protein 140 (RIP140) in Gene Regulation
Author: Wei, Li-Na
Source: Current Medicinal Chemistry, Volume 11, Number 12, June 2004 , pp. 1527-1532(6)
Publisher: Bentham Science Publishers
Abstract:Retinoids exert pleiotropic effects in various biological processes by binding to their nuclear receptors, the retinoic acid receptors (RARs) and retinoid X receptors (RXRs), to regulate gene transcription. Apo-RARs and RXRs repress target gene expression by recruiting corepressors to the target DNA, triggering chromatin condensation by the action of histone deacetylases present in the corepressor complexes. In contrast, holo-RARs and RXRs recruit coactivators, some known to encode histone acetyl transferases, which trigger histone hyperacetylation, chromatin decondensation, and ultimately gene activation. Receptor interacting protein 140 (RIP140) represents a novel RAR / RXR coregulator that suppresses vitamin A-regulated gene expression in a retinoid- dependent manner. This review addresses the action of different retinoid ligands on gene expression, the molecular mechanisms underlying RAR/RXR-mediated gene regulation, and the unique properties of RIP140 as a novel retinoid hormone-dependent negative coregulator for RAR- and RXR-mediated gene regulation.
Document Type: Review Article
Affiliations: Dept. of Pharmacology, 6-120 Jackson Hall, 321 Church St. SE, Minneapolis, MN 55455, USA
Publication date: June 2004
- Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.