SUMO E3 ligase activity of TRIM proteins
SUMOylation governs numerous cellular processes and is essential to most eukaryotic life. Despite increasing recognition of the importance of this process, an extremely limited number of small ubiquitin-like modifier (SUMO) protein ligases (E3s) have been identified. Here we show that at least some...
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| Veröffentlicht in: | Oncogene 2011-03, Vol.30 (9), p.1108-1116 |
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| description | SUMOylation governs numerous cellular processes and is essential to most eukaryotic life. Despite increasing recognition of the importance of this process, an extremely limited number of small ubiquitin-like modifier (SUMO) protein ligases (E3s) have been identified. Here we show that at least some members of the functionally diverse tripartite motif (TRIM) superfamily are SUMO E3s. These TRIM proteins bind both the SUMO-conjugating enzyme Ubc9 and substrates and strongly enhance transfer of SUMOs from Ubc9 to these substrates. Among the substrates of TRIM SUMO E3s are the tumor suppressor p53 and its principal antagonist Mdm2. The E3 activity depends on the TRIM motif, suggesting it to be the first widespread SUMO E3 motif. Given the large number of TRIM proteins, our results may greatly expand the identified SUMO E3s. Furthermore, TRIM E3 activity may be an important contributor to SUMOylation specificity and the versatile functions of TRIM proteins. |
| doi_str_mv | 10.1038/onc.2010.462 |
| format | Article |
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Despite increasing recognition of the importance of this process, an extremely limited number of small ubiquitin-like modifier (SUMO) protein ligases (E3s) have been identified. Here we show that at least some members of the functionally diverse tripartite motif (TRIM) superfamily are SUMO E3s. These TRIM proteins bind both the SUMO-conjugating enzyme Ubc9 and substrates and strongly enhance transfer of SUMOs from Ubc9 to these substrates. Among the substrates of TRIM SUMO E3s are the tumor suppressor p53 and its principal antagonist Mdm2. The E3 activity depends on the TRIM motif, suggesting it to be the first widespread SUMO E3 motif. Given the large number of TRIM proteins, our results may greatly expand the identified SUMO E3s. Furthermore, TRIM E3 activity may be an important contributor to SUMOylation specificity and the versatile functions of TRIM proteins.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/onc.2010.462</identifier><identifier>PMID: 20972456</identifier><identifier>CODEN: ONCNES</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/45/607/1166 ; 631/67 ; 631/80/458/538 ; Animals ; Apoptosis ; Biochemistry ; Biological and medical sciences ; Cell Biology ; Cell Line ; Cell physiology ; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes ; Cellular biology ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Human Genetics ; Humans ; Immunoprecipitation ; Internal Medicine ; Ligases ; MDM2 protein ; Medicine ; Medicine & Public Health ; Microscopy, Fluorescence ; Molecular and cellular biology ; Nuclear Proteins - chemistry ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Oncology ; original-article ; p53 Protein ; Physiological aspects ; Promyelocytic Leukemia Protein ; Protein Binding ; Protein Interaction Domains and Motifs ; Proteins ; Proto-Oncogene Proteins c-mdm2 - metabolism ; RNA, Small Interfering ; Small Ubiquitin-Related Modifier Proteins - chemistry ; Small Ubiquitin-Related Modifier Proteins - genetics ; Small Ubiquitin-Related Modifier Proteins - metabolism ; SUMO protein ; Sumoylation ; Transcription Factors - chemistry ; Transcription Factors - genetics ; Transcription Factors - metabolism ; Tumor proteins ; Tumor suppressor genes ; Tumor Suppressor Protein p53 - genetics ; Tumor Suppressor Protein p53 - metabolism ; Tumor Suppressor Proteins - chemistry ; Tumor Suppressor Proteins - genetics ; Tumor Suppressor Proteins - metabolism ; Tumors ; Ubiquitin ; Ubiquitin-Conjugating Enzymes - metabolism ; Ubiquitin-protein ligase ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - metabolism</subject><ispartof>Oncogene, 2011-03, Vol.30 (9), p.1108-1116</ispartof><rights>Macmillan Publishers Limited 2011</rights><rights>2015 INIST-CNRS</rights><rights>COPYRIGHT 2011 Nature Publishing Group</rights><rights>Macmillan Publishers Limited 2011.</rights><rights>Copyright Nature Publishing Group Mar 3, 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c605t-c97b9a3ced00b52c8b514317582491d5cbaf20e1de2a3d6a91d3f201a9dc52fd3</citedby><cites>FETCH-LOGICAL-c605t-c97b9a3ced00b52c8b514317582491d5cbaf20e1de2a3d6a91d3f201a9dc52fd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/onc.2010.462$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/onc.2010.462$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23943673$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20972456$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chu, Y</creatorcontrib><creatorcontrib>Yang, X</creatorcontrib><title>SUMO E3 ligase activity of TRIM proteins</title><title>Oncogene</title><addtitle>Oncogene</addtitle><addtitle>Oncogene</addtitle><description>SUMOylation governs numerous cellular processes and is essential to most eukaryotic life. Despite increasing recognition of the importance of this process, an extremely limited number of small ubiquitin-like modifier (SUMO) protein ligases (E3s) have been identified. Here we show that at least some members of the functionally diverse tripartite motif (TRIM) superfamily are SUMO E3s. These TRIM proteins bind both the SUMO-conjugating enzyme Ubc9 and substrates and strongly enhance transfer of SUMOs from Ubc9 to these substrates. Among the substrates of TRIM SUMO E3s are the tumor suppressor p53 and its principal antagonist Mdm2. The E3 activity depends on the TRIM motif, suggesting it to be the first widespread SUMO E3 motif. Given the large number of TRIM proteins, our results may greatly expand the identified SUMO E3s. Furthermore, TRIM E3 activity may be an important contributor to SUMOylation specificity and the versatile functions of TRIM proteins.</description><subject>631/45/607/1166</subject><subject>631/67</subject><subject>631/80/458/538</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cell Biology</subject><subject>Cell Line</subject><subject>Cell physiology</subject><subject>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</subject><subject>Cellular biology</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Human Genetics</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Internal Medicine</subject><subject>Ligases</subject><subject>MDM2 protein</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Microscopy, Fluorescence</subject><subject>Molecular and cellular biology</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Oncology</subject><subject>original-article</subject><subject>p53 Protein</subject><subject>Physiological aspects</subject><subject>Promyelocytic Leukemia Protein</subject><subject>Protein Binding</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins c-mdm2 - metabolism</subject><subject>RNA, Small Interfering</subject><subject>Small Ubiquitin-Related Modifier Proteins - chemistry</subject><subject>Small Ubiquitin-Related Modifier Proteins - genetics</subject><subject>Small Ubiquitin-Related Modifier Proteins - metabolism</subject><subject>SUMO protein</subject><subject>Sumoylation</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><subject>Tumor proteins</subject><subject>Tumor suppressor genes</subject><subject>Tumor Suppressor Protein p53 - genetics</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><subject>Tumor Suppressor Proteins - chemistry</subject><subject>Tumor Suppressor Proteins - genetics</subject><subject>Tumor Suppressor Proteins - metabolism</subject><subject>Tumors</subject><subject>Ubiquitin</subject><subject>Ubiquitin-Conjugating Enzymes - metabolism</subject><subject>Ubiquitin-protein ligase</subject><subject>Ubiquitin-Protein Ligases - genetics</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkt1rFDEUxYModq2--SyDIvbBWW--Jy9CKbUWWgraPodMJrOmzCZrMlvof2-G3XZtqUgeQu795Vzu4SD0FsMcA22-xGDnBMqLCfIMzTCTouZcsedoBopDrQgle-hVztcAIBWQl2iPgJKEcTFDBz-vzi-qY1oNfmGyq4wd_Y0fb6vYV5c_Ts-rVYqj8yG_Ri96M2T3Znvvo6tvx5dH3-uzi5PTo8Oz2grgY22VbJWh1nUALSe2aTlmFEveEKZwx21regIOd44Y2glTarQUsFGd5aTv6D76utFdrdul66wLYzKDXiW_NOlWR-P1w07wv_Qi3mha3BCCFYFPW4EUf69dHvXSZ-uGwQQX11krYEw2gsJ_yYbzyViQhXz_iLyO6xSKDwViXFEFk9yHf0FEMMww4ZLsqIUZnPahj2ULOw3Wh4RjrChhk9b8Caqczi29jcH1vtQffPi8-WBTzDm5_t4xDHrKiS450dM6uuSk4O_-dvkevgtGAT5uAZOtGfpkgvV5x1HFqJC0cPWGy6UVFi7tln5y8B-CRM99</recordid><startdate>20110303</startdate><enddate>20110303</enddate><creator>Chu, Y</creator><creator>Yang, X</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>IQODW</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>3V.</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110303</creationdate><title>SUMO E3 ligase activity of TRIM proteins</title><author>Chu, Y ; Yang, X</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c605t-c97b9a3ced00b52c8b514317582491d5cbaf20e1de2a3d6a91d3f201a9dc52fd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>631/45/607/1166</topic><topic>631/67</topic><topic>631/80/458/538</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Cell Biology</topic><topic>Cell Line</topic><topic>Cell physiology</topic><topic>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</topic><topic>Cellular biology</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene expression</topic><topic>Human Genetics</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Internal Medicine</topic><topic>Ligases</topic><topic>MDM2 protein</topic><topic>Medicine</topic><topic>Medicine & Public Health</topic><topic>Microscopy, Fluorescence</topic><topic>Molecular and cellular biology</topic><topic>Nuclear Proteins - chemistry</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>Oncology</topic><topic>original-article</topic><topic>p53 Protein</topic><topic>Physiological aspects</topic><topic>Promyelocytic Leukemia Protein</topic><topic>Protein Binding</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins c-mdm2 - metabolism</topic><topic>RNA, Small Interfering</topic><topic>Small Ubiquitin-Related Modifier Proteins - chemistry</topic><topic>Small Ubiquitin-Related Modifier Proteins - genetics</topic><topic>Small Ubiquitin-Related Modifier Proteins - metabolism</topic><topic>SUMO protein</topic><topic>Sumoylation</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Tumor proteins</topic><topic>Tumor suppressor genes</topic><topic>Tumor Suppressor Protein p53 - genetics</topic><topic>Tumor Suppressor Protein p53 - metabolism</topic><topic>Tumor Suppressor Proteins - chemistry</topic><topic>Tumor Suppressor Proteins - genetics</topic><topic>Tumor Suppressor Proteins - metabolism</topic><topic>Tumors</topic><topic>Ubiquitin</topic><topic>Ubiquitin-Conjugating Enzymes - metabolism</topic><topic>Ubiquitin-protein ligase</topic><topic>Ubiquitin-Protein Ligases - genetics</topic><topic>Ubiquitin-Protein Ligases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chu, Y</creatorcontrib><creatorcontrib>Yang, X</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Oncogene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chu, Y</au><au>Yang, X</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SUMO E3 ligase activity of TRIM proteins</atitle><jtitle>Oncogene</jtitle><stitle>Oncogene</stitle><addtitle>Oncogene</addtitle><date>2011-03-03</date><risdate>2011</risdate><volume>30</volume><issue>9</issue><spage>1108</spage><epage>1116</epage><pages>1108-1116</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><coden>ONCNES</coden><abstract>SUMOylation governs numerous cellular processes and is essential to most eukaryotic life. Despite increasing recognition of the importance of this process, an extremely limited number of small ubiquitin-like modifier (SUMO) protein ligases (E3s) have been identified. Here we show that at least some members of the functionally diverse tripartite motif (TRIM) superfamily are SUMO E3s. These TRIM proteins bind both the SUMO-conjugating enzyme Ubc9 and substrates and strongly enhance transfer of SUMOs from Ubc9 to these substrates. Among the substrates of TRIM SUMO E3s are the tumor suppressor p53 and its principal antagonist Mdm2. The E3 activity depends on the TRIM motif, suggesting it to be the first widespread SUMO E3 motif. Given the large number of TRIM proteins, our results may greatly expand the identified SUMO E3s. Furthermore, TRIM E3 activity may be an important contributor to SUMOylation specificity and the versatile functions of TRIM proteins.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>20972456</pmid><doi>10.1038/onc.2010.462</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/45/607/1166 631/67 631/80/458/538 Animals Apoptosis Biochemistry Biological and medical sciences Cell Biology Cell Line Cell physiology Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Cellular biology DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Enzymes Fundamental and applied biological sciences. Psychology Gene expression Human Genetics Humans Immunoprecipitation Internal Medicine Ligases MDM2 protein Medicine Medicine & Public Health Microscopy, Fluorescence Molecular and cellular biology Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism Oncology original-article p53 Protein Physiological aspects Promyelocytic Leukemia Protein Protein Binding Protein Interaction Domains and Motifs Proteins Proto-Oncogene Proteins c-mdm2 - metabolism RNA, Small Interfering Small Ubiquitin-Related Modifier Proteins - chemistry Small Ubiquitin-Related Modifier Proteins - genetics Small Ubiquitin-Related Modifier Proteins - metabolism SUMO protein Sumoylation Transcription Factors - chemistry Transcription Factors - genetics Transcription Factors - metabolism Tumor proteins Tumor suppressor genes Tumor Suppressor Protein p53 - genetics Tumor Suppressor Protein p53 - metabolism Tumor Suppressor Proteins - chemistry Tumor Suppressor Proteins - genetics Tumor Suppressor Proteins - metabolism Tumors Ubiquitin Ubiquitin-Conjugating Enzymes - metabolism Ubiquitin-protein ligase Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism |
| title | SUMO E3 ligase activity of TRIM proteins |
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