title: SUMO modification of the Ets-related transcription factor ERM inhibits its transcriptional activity.
abstract: 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.
authors.affiliation: 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.
authors.forename: Cindy
authors.initials: C
authors.lastname: Degerny
authors.forename: Didier
authors.initials: D
authors.lastname: Monte
authors.forename: Claude
authors.initials: C
authors.lastname: Beaudoin
authors.forename: Ellis
authors.initials: E
authors.lastname: Jaffray
authors.forename: Laurence
authors.initials: L
authors.lastname: Portois
authors.forename: Ron T
authors.initials: RT
authors.lastname: Hay
authors.forename: Yvan
authors.initials: Y
authors.lastname: de Launoit
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Baert
mesh_terms: D000256:Adenoviridae / Q000235:genetics; D000818:Animals; D001120:Arginine / Q000737:chemistry; D001665:Binding Sites; D015153:Blotting, Western; D019556:COS Cells; D003546:Cysteine Endopeptidases; D004247:DNA / Q000737:chemistry; D018076:DNA, Complementary / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D010450:Endopeptidases / Q000378:metabolism; D004742:Enhancer Elements, Genetic; D005786:Gene Expression Regulation; D015723:Gene Library; D017930:Genes, Reporter; D006367:HeLa Cells; D006801:Humans; D047468:Immunoprecipitation; D018799:Intercellular Adhesion Molecule-1 / Q000378:metabolism; D008239:Lysine / Q000737:chemistry; D008856:Microscopy, Fluorescence; D008957:Models, Genetic; D010957:Plasmids / Q000378:metabolism; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D011817:Rabbits; D025842:SUMO-1 Protein / Q000378:metabolism / Q000502:physiology*; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics; D014158:Transcription, Genetic; D015533:Transcriptional Activation; D020798:Two-Hybrid System Techniques; D025801:Ubiquitin / Q000737:chemistry
chemical_list: D018076:DNA, Complementary; D004268:DNA-Binding Proteins; C086680:ETV5 protein, human; D025842:SUMO-1 Protein; D014157:Transcription Factors; D025801:Ubiquitin; D018799:Intercellular Adhesion Molecule-1; D004247:DNA; D001120:Arginine; D010450:Endopeptidases; C404512:SENP1 protein, human; D003546:Cysteine Endopeptidases; D008239:Lysine