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Originally published In Press as doi:10.1074/jbc.M207148200 on January 14, 2003

J. Biol. Chem., Vol. 278, Issue 14, 12335-12343, April 4, 2003
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Sumoylation of the Progesterone Receptor and of the Steroid Receptor Coactivator SRC-1*

Anne ChauchereauDagger , Larbi Amazit§, Monique Quesne, Anne Guiochon-Mantel, and Edwin Milgrom

From INSERM U135, Hormones, Gènes, and Reproduction, Hôpital de Bicêtre, 78 rue du Général Leclerc, 94275 Le Kremlin-Bicêtre, France

SUMO-1 (small ubiquitin-like modifier) conjugation regulates the subcellular localization, stability, and activity of a variety of proteins. We show here that SUMO-1 overexpression markedly enhances progesterone receptor (PR)-mediated gene transcription. PR undergoes a sumoylation at lysine 388 located in its N-terminal domain. However, sumoylation of the receptor is not responsible for enhanced transcription because substitution of its target lysine did not abolish the effect of SUMO-1 and even converted the receptor into a slightly more active transactivator. Furthermore estrogen receptor alpha  (ERalpha )-driven transcription is also enhanced by SUMO-1 overexpression contrasting with the absence of sumoylation of this receptor. We thus analyzed SUMO-1 conjugation to the steroid receptor coactivator SRC-1. We showed that this protein contains two major sites of conjugation at Lys-732 and Lys-774. Sumoylation was shown to increase PR-SRC-1 interaction and to prolong SRC-1 retention in the nucleus. It did not prevent SRC-1 ubiquitinylation and did not exert a clear effect on the stability of the protein. Overexpression of SUMO-1 enhanced PR-mediated gene transcription even in the presence of non-sumoylated mutants of SRC-1. This observation suggests that among the many protein partners involved in steroid hormone-mediated gene regulation several are probably targets of SUMO-1 modification.

* This work was supported by INSERM, the Association pour la Recherche sur le Cancer, the Ligue contre le Cancer, the Faculté de Médecine Paris-Sud, and the Fondation pour la Recherche Médicale.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 Present address: CNRS UPR9079, Oncogénèse, différenciation et Transduction du signal, Institut André Lwoff, 7 rue Guy Môquet, 94800 Villejuif, France.

§ Supported by the Association pour la Recherche sur le Cancer.

To whom correspondence should be addressed: INSERM U 135 Hormones, Gènes et Reproduction, Hôpital de Bicêtre, 78 rue du Général Leclerc, 94275 Le Kremlin-Bicêtre cedex, France. Tel.: 33-1-45-21-33-29; Fax: 33-1-45-21-27-51; E-mail: u135@kb.inserm.fr.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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