SUMO Modification of the Ets-related Transcription Factor ERM Inhibits Its Transcriptional Activity
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...
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| Veröffentlicht in: | The Journal of biological chemistry 2005-07, Vol.280 (26), p.24330-24338 |
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| container_title | The Journal of biological chemistry |
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| creator | Degerny, Cindy Monte, Didier Beaudoin, Claude Jaffray, Ellis Portois, Laurence Hay, Ron T. de Launoit, Yvan Baert, Jean-Luc |
| description | 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. |
| doi_str_mv | 10.1074/jbc.M411250200 |
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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.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M411250200</identifier><identifier>PMID: 15857832</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenoviridae - genetics ; Animals ; Arginine - chemistry ; Binding Sites ; Blotting, Western ; COS Cells ; Cysteine Endopeptidases ; DNA - chemistry ; DNA, Complementary - metabolism ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; Endopeptidases - metabolism ; Enhancer Elements, Genetic ; Gene Expression Regulation ; Gene Library ; Genes, Reporter ; HeLa Cells ; Humans ; Immunoprecipitation ; Intercellular Adhesion Molecule-1 - metabolism ; Lysine - chemistry ; Microscopy, Fluorescence ; Models, Genetic ; Plasmids - metabolism ; Protein Binding ; Protein Processing, Post-Translational ; Rabbits ; SUMO-1 Protein - metabolism ; SUMO-1 Protein - physiology ; Transcription Factors - chemistry ; Transcription Factors - genetics ; Transcription, Genetic ; Transcriptional Activation ; Two-Hybrid System Techniques ; Ubiquitin - chemistry</subject><ispartof>The Journal of biological chemistry, 2005-07, Vol.280 (26), p.24330-24338</ispartof><rights>2005 © 2005 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c508t-bedaaa07aae9783e536591448a9ed41ded24ab63b41acca34a49c6c2526dd4243</citedby><cites>FETCH-LOGICAL-c508t-bedaaa07aae9783e536591448a9ed41ded24ab63b41acca34a49c6c2526dd4243</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15857832$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Degerny, Cindy</creatorcontrib><creatorcontrib>Monte, Didier</creatorcontrib><creatorcontrib>Beaudoin, Claude</creatorcontrib><creatorcontrib>Jaffray, Ellis</creatorcontrib><creatorcontrib>Portois, Laurence</creatorcontrib><creatorcontrib>Hay, Ron T.</creatorcontrib><creatorcontrib>de Launoit, Yvan</creatorcontrib><creatorcontrib>Baert, Jean-Luc</creatorcontrib><title>SUMO Modification of the Ets-related Transcription Factor ERM Inhibits Its Transcriptional Activity</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A variety of transcription factors are post-translationally modified by SUMO, a 97-residue ubiquitin-like protein bound covalently to the targeted lysine. 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These results demonstrate that ERM is subject to SUMO modification and that this post-translational modification causes inhibition of transcription-enhancing activity.</description><subject>Adenoviridae - genetics</subject><subject>Animals</subject><subject>Arginine - chemistry</subject><subject>Binding Sites</subject><subject>Blotting, Western</subject><subject>COS Cells</subject><subject>Cysteine Endopeptidases</subject><subject>DNA - chemistry</subject><subject>DNA, Complementary - metabolism</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>Endopeptidases - metabolism</subject><subject>Enhancer Elements, Genetic</subject><subject>Gene Expression Regulation</subject><subject>Gene Library</subject><subject>Genes, Reporter</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Intercellular Adhesion Molecule-1 - metabolism</subject><subject>Lysine - chemistry</subject><subject>Microscopy, Fluorescence</subject><subject>Models, Genetic</subject><subject>Plasmids - metabolism</subject><subject>Protein Binding</subject><subject>Protein Processing, Post-Translational</subject><subject>Rabbits</subject><subject>SUMO-1 Protein - metabolism</subject><subject>SUMO-1 Protein - physiology</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - genetics</subject><subject>Transcription, Genetic</subject><subject>Transcriptional Activation</subject><subject>Two-Hybrid System Techniques</subject><subject>Ubiquitin - chemistry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0MFr2zAUBnAxVtqs63XHocPYzakkS7Z1LCXdAg2FrYXdxLP0Mqs4ViYpLf3vpyyBssOYQOjyex9PHyEfOJtz1srLx97OV5JzoZhg7A2ZcdbVVa34j7dkxpjglRaqOyPvUnpk5UjNT8kZV51qu1rMiP3-sLqjq-D82lvIPkw0rGkekC5yqiKOkNHR-whTstFv_4AbsDlEuvi2ostp8L3PiS7L_UvBSK9s9k8-v7wnJ2sYE14c33PycLO4v_5a3d59WV5f3VZWsS5XPToAYC0A6rIcqrpRmkvZgUYnuUMnJPRN3UsO1kItQWrbWKFE45wUsj4nnw-52xh-7TBls_HJ4jjChGGXTNPqVsmm-S_ke6a1LnB-gDaGlCKuzTb6DcQXw5nZ929K_-a1_zLw8Zi86zfoXvmx8AI-HcDgfw7PPqLpfbADbozomBGNKf-o9zndgWHp68ljNMl6nCy6MmKzccH_a4XfRfygEg</recordid><startdate>20050701</startdate><enddate>20050701</enddate><creator>Degerny, Cindy</creator><creator>Monte, Didier</creator><creator>Beaudoin, Claude</creator><creator>Jaffray, Ellis</creator><creator>Portois, Laurence</creator><creator>Hay, Ron T.</creator><creator>de Launoit, Yvan</creator><creator>Baert, Jean-Luc</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20050701</creationdate><title>SUMO Modification of the Ets-related Transcription Factor ERM Inhibits Its Transcriptional Activity</title><author>Degerny, Cindy ; 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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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15857832</pmid><doi>10.1074/jbc.M411250200</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenoviridae - genetics Animals Arginine - chemistry Binding Sites Blotting, Western COS Cells Cysteine Endopeptidases DNA - chemistry DNA, Complementary - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics Endopeptidases - metabolism Enhancer Elements, Genetic Gene Expression Regulation Gene Library Genes, Reporter HeLa Cells Humans Immunoprecipitation Intercellular Adhesion Molecule-1 - metabolism Lysine - chemistry Microscopy, Fluorescence Models, Genetic Plasmids - metabolism Protein Binding Protein Processing, Post-Translational Rabbits SUMO-1 Protein - metabolism SUMO-1 Protein - physiology Transcription Factors - chemistry Transcription Factors - genetics Transcription, Genetic Transcriptional Activation Two-Hybrid System Techniques Ubiquitin - chemistry |
| title | SUMO Modification of the Ets-related Transcription Factor ERM Inhibits Its Transcriptional Activity |
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