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J. Biol. Chem., Vol. 280, Issue 26, 24330-24338, July 1, 2005

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SUMO Modification of the Ets-related Transcription Factor ERM Inhibits Its Transcriptional Activity^*

Cindy Degerny, Didier Monte, Claude Beaudoin¶, Ellis Jaffray||, Laurence Portois, Ron T. Hay||, Yvan de Launoit, and Jean-Luc Baert

From the UMR 8117, CNRS, Université de Lille I, Institut Pasteur de Lille, Institut de Biologie de Lille, BP 447, 1 rue Calmette, 59021 Lille Cedex, France, the ^||School of Biology, University of St. Andrews, The North Haugh, St. Andrews KY16 9ST, United Kingdom, and Laboratoire de Virologie Moléculaire, Faculté de Médecine, Université Libre de Bruxelles, CP 614, 808 route de Lennik, 1070 Brussels, Belgium

A variety of transcription factors are post-translationally modified by SUMO, a 97-residue ubiquitin-like protein bound covalently to the targeted lysine. Here we describe SUMO modification of the Ets family member ERM at positions 89, 263, 293, and 350. To investigate how SUMO modification affects the function of ERM, Ets-responsive intercellular adhesion molecule 1 (ICAM-1) and E74 reporter plasmids were employed to demonstrate that SUMO modification causes inhibition of ERM-dependent transcription without affecting the subcellular localization, stability, or DNA-binding capacity of the protein. When the adenoviral protein Gam1 or the SUMO protease SENP1 was used to inhibit the SUMO modification pathway, ERM-dependent transcription was de-repressed. These results demonstrate that ERM is subject to SUMO modification and that this post-translational modification causes inhibition of transcription-enhancing activity.

Received for publication, October 1, 2004 , and in revised form, March 29, 2005.

** Laboratory supported by the Biology and Biotechnology Research Council (UK).

^* This work was supported in part by grants from the "Centre National de la Recherche Scientifique" (France), the "Institut Pasteur de Lille," the "Association pour la Recherche contre le Cancer" (France), the "Ligue Nationale Contre le Cancer" (Comité Nord, France), the "Fonds National de la Recherche Scientifique" (Belgium), the "Action de Recherche Concertée, Communauté Française de Belgique" (Belgium) the Conseil Régional Nord/pas-de-Calais (France), and the European Regional Development Fund. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a Ph.D. grant from the French Research Ministry.

^¶ Recipient of a postdoctoral fellowship from the Canadian Institutes of Health Research. Present address: CNRS UMR 6547, Equipe Physiologie Comparée et Endocrinologie Moléculaire, Université Blaise Pascal Clermont II, Campus Universitaire des Cézeaux, 24 Avenue des Landais, 63177 Aubière, France.

To whom correspondence should be addressed: UMR 8117 CNRS, Institut de Biologie de Lille, Institut Pasteur de Lille, Université de Lille 1, 1 rue du professeur Calmette, 59021 Lille Cedex, France. Tel.: 33-320-87-11-17; Fax: 33-320-87-11-11; E-mail: yvan.delaunoit{at}ibl.fr.

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