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Originally published In Press as doi:10.1074/jbc.M002840200 on June 26, 2000

J. Biol. Chem., Vol. 275, Issue 43, 33280-33288, October 27, 2000
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Dimerization with Retinoid X Receptors and Phosphorylation Modulate the Retinoic Acid-induced Degradation of Retinoic Acid Receptors alpha  and gamma  through the Ubiquitin-Proteasome Pathway*

Eliezer KopfDagger , Jean-Luc Plassat, Valérie Vivat§, Hughes de Thé, Pierre Chambon, and Cécile Rochette-Egly||

From the Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP/Collège de France, BP 163, 67404 Illkirch Cedex, CU de Strasbourg, France and  CNRS UPR 9051, Hôpital Saint Louis, 75475 Paris Cedex 10, France

In eukaryotic cells, the ubiquitin-proteasome pathway is the major mechanism for targeted degradation of proteins. We show that, in F9 cells and in transfected COS-1 cells, the nuclear retinoid receptors, retinoic acid receptor gamma 2 (RARgamma 2), RARalpha 1, and retinoid X receptor alpha 1 (RXRalpha 1) are degraded in a retinoic acid-dependent manner through the ubiquitin-proteasome pathway. The degradation of RARgamma 2 is entirely dependent on its phosphorylation and on its heterodimerization with liganded RXRalpha 1. In contrast, RARalpha 1 degradation can occur in the absence of heterodimerization, whereas it is inhibited by phosphorylation, and heterodimerization reverses that inhibition. RXRalpha 1 degradation is also modulated by heterodimerization. Thus, each partner of RARgamma /RXRalpha and RARalpha /RXRalpha heterodimers modulates the degradation of the other. We conclude that the ligand-dependent degradation of RARs and RXRs by the ubiquitin-proteasome pathway, which is regulated by heterodimerization and by phosphorylation, could be important for the regulation of the magnitude and duration of the effects of retinoid signals.

* This work was supported by funds from CNRS, INSERM, the Collège de France, the Hôpital Universitaire de Strasbourg, the Association pour la Recherche sur le Cancer, and Bristol-Myers Squibb.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 Supported by Fondation Chateaubriand and by an INSERM fellowship.

§ Present address: Bristol-Myers Squibb Pharmaceutical Research Institute, P.O. Box 4000 (K12-03) Princeton, NJ 08543-4000.

|| To whom correspondence should be addressed: Tel.: 33 3 88 65 34 59; Fax: 33 3 88 65 32 01; E-mail: cegly@igbmc.u-strasbg.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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