Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritis
The E3 ubiquitin ligase synoviolin (SYVN1) functions as an anti‐apoptotic factor that is responsible for the outgrowth of synovial cells during the development of rheumatoid arthritis. The molecular mechanisms underlying SYVN1 regulation of cell death are largely unknown. Here, we report that elevat...
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| Veröffentlicht in: | EMBO reports 2008-05, Vol.9 (5), p.480-485 |
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| creator | Gao, Beixue Lee, Sang-Myeong Chen, An Zhang, Jinping Zhang, Donna D Kannan, Krishnaswamy Ortmann, Robert A Fang, Deyu |
| description | The E3 ubiquitin ligase synoviolin (SYVN1) functions as an anti‐apoptotic factor that is responsible for the outgrowth of synovial cells during the development of rheumatoid arthritis. The molecular mechanisms underlying SYVN1 regulation of cell death are largely unknown. Here, we report that elevated SYVN1 expression correlates with decreased levels of the protein inositol‐requiring enzyme 1 (IRE1)—a pro‐apoptotic factor in the endoplasmic reticulum (ER)‐stress‐induced apoptosis pathway—in synovial fibroblasts from mice with collagen‐induced arthritis (CIA). SYVN1 interacts with and catalyses IRE1 ubiquitination and consequently promotes IRE1 degradation. Suppression of SYVN1 expression in synovial fibroblasts from CIA mice restores IRE1 protein expression and reverses the resistance of ER‐stress‐induced apoptosis of CIA synovial fibroblasts. These results show that SYVN1 causes the overgrowth of synovial cells by degrading IRE1, and therefore antagonizes ER‐stress‐induced cell death. |
| doi_str_mv | 10.1038/embor.2008.37 |
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The molecular mechanisms underlying SYVN1 regulation of cell death are largely unknown. Here, we report that elevated SYVN1 expression correlates with decreased levels of the protein inositol‐requiring enzyme 1 (IRE1)—a pro‐apoptotic factor in the endoplasmic reticulum (ER)‐stress‐induced apoptosis pathway—in synovial fibroblasts from mice with collagen‐induced arthritis (CIA). SYVN1 interacts with and catalyses IRE1 ubiquitination and consequently promotes IRE1 degradation. Suppression of SYVN1 expression in synovial fibroblasts from CIA mice restores IRE1 protein expression and reverses the resistance of ER‐stress‐induced apoptosis of CIA synovial fibroblasts. These results show that SYVN1 causes the overgrowth of synovial cells by degrading IRE1, and therefore antagonizes ER‐stress‐induced cell death.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.1038/embor.2008.37</identifier><identifier>PMID: 18369366</identifier><identifier>CODEN: ERMEAX</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Animals ; Apoptosis ; Apoptosis - physiology ; Arthritis ; Arthritis, Experimental - metabolism ; Arthritis, Experimental - pathology ; Catalysis ; Cells, Cultured ; Cellular biology ; EMBO24 ; EMBO37 ; ER-stress-induced cell death ; Fibroblasts - metabolism ; Half-Life ; IRE1 ; Membrane Proteins - metabolism ; Mice ; Mice, Inbred DBA ; Molecular biology ; Mortality ; Protein-Serine-Threonine Kinases - metabolism ; Rheumatoid arthritis ; RNA, Small Interfering - genetics ; Rodents ; Scientific Report ; Synovial Membrane - cytology ; synoviolin ; Transcription Factor CHOP - metabolism ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - metabolism ; Ubiquitination</subject><ispartof>EMBO reports, 2008-05, Vol.9 (5), p.480-485</ispartof><rights>European Molecular Biology Organization 2008</rights><rights>Copyright © 2008 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group May 2008</rights><rights>Copyright © 2008, European Molecular Biology Organization 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5357-b8ed07cc8738a97deb19df06d3f4c756b507266a5f579755870d4237a71f66a53</citedby><cites>FETCH-LOGICAL-c5357-b8ed07cc8738a97deb19df06d3f4c756b507266a5f579755870d4237a71f66a53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2373369/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2373369/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27901,27902,45550,45551,46384,46808,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18369366$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gao, Beixue</creatorcontrib><creatorcontrib>Lee, Sang-Myeong</creatorcontrib><creatorcontrib>Chen, An</creatorcontrib><creatorcontrib>Zhang, Jinping</creatorcontrib><creatorcontrib>Zhang, Donna D</creatorcontrib><creatorcontrib>Kannan, Krishnaswamy</creatorcontrib><creatorcontrib>Ortmann, Robert A</creatorcontrib><creatorcontrib>Fang, Deyu</creatorcontrib><title>Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritis</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>The E3 ubiquitin ligase synoviolin (SYVN1) functions as an anti‐apoptotic factor that is responsible for the outgrowth of synovial cells during the development of rheumatoid arthritis. The molecular mechanisms underlying SYVN1 regulation of cell death are largely unknown. Here, we report that elevated SYVN1 expression correlates with decreased levels of the protein inositol‐requiring enzyme 1 (IRE1)—a pro‐apoptotic factor in the endoplasmic reticulum (ER)‐stress‐induced apoptosis pathway—in synovial fibroblasts from mice with collagen‐induced arthritis (CIA). SYVN1 interacts with and catalyses IRE1 ubiquitination and consequently promotes IRE1 degradation. Suppression of SYVN1 expression in synovial fibroblasts from CIA mice restores IRE1 protein expression and reverses the resistance of ER‐stress‐induced apoptosis of CIA synovial fibroblasts. These results show that SYVN1 causes the overgrowth of synovial cells by degrading IRE1, and therefore antagonizes ER‐stress‐induced cell death.</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Apoptosis - physiology</subject><subject>Arthritis</subject><subject>Arthritis, Experimental - metabolism</subject><subject>Arthritis, Experimental - pathology</subject><subject>Catalysis</subject><subject>Cells, Cultured</subject><subject>Cellular biology</subject><subject>EMBO24</subject><subject>EMBO37</subject><subject>ER-stress-induced cell death</subject><subject>Fibroblasts - metabolism</subject><subject>Half-Life</subject><subject>IRE1</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred DBA</subject><subject>Molecular biology</subject><subject>Mortality</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Rheumatoid arthritis</subject><subject>RNA, Small Interfering - genetics</subject><subject>Rodents</subject><subject>Scientific Report</subject><subject>Synovial Membrane - cytology</subject><subject>synoviolin</subject><subject>Transcription Factor CHOP - metabolism</subject><subject>Ubiquitin-Protein Ligases - genetics</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><subject>Ubiquitination</subject><issn>1469-221X</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9kc1v0zAYxi0EYqNw5IosDtxS7Lj-yAUJRlcmDZC2InaznNhpPRK7s5ON_vc4TbQBEpz82v69j5_XDwAvMZpjRMRb05Y-zHOExJzwR-AYL1iREczF46nOc3x1BJ7FeI0QogUXT8ERFoQVhLFjsL_cO39rfWMd3AXf-s5EeHaxxLAv7U1vO-tUZ72DymmozSYoPe4THw-tqoG1LYMvGxW7COskAltbGXhnuy2sfNOojXGZdbqvjIYqdNuQZONz8KRWTTQvpnUGvp0u1yefsvOvq7OT9-dZRQnlWSmMRryqBCdCFVybEhe6RkyTelFxykqKeM6YojXlBadUcKQXOeGK43o4JjPwbtTd9WVrdGVcF1Qjd8G2KuylV1b-eePsVm78rUwiZPimGXgzCQR_05vYydbGyqS5nPF9lKzAbIELksDXf4HXvg8uDSdzJGguBF0kKBuhKvgYg6nvnWAkh0TlIVE5JCqTgxl49bv9B3qKMAF0BO5sY_b_V5PLzx8uhvogPB_7YmpxGxMe3P7LyeTcxs78vH9IhR-SccKp_P5lJdeXH9nV6aqQa_ILnzDP3w</recordid><startdate>200805</startdate><enddate>200805</enddate><creator>Gao, Beixue</creator><creator>Lee, Sang-Myeong</creator><creator>Chen, An</creator><creator>Zhang, Jinping</creator><creator>Zhang, Donna D</creator><creator>Kannan, Krishnaswamy</creator><creator>Ortmann, Robert A</creator><creator>Fang, Deyu</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Springer Nature B.V</general><general>Nature Publishing Group</general><scope>BSCLL</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>7QL</scope><scope>7T5</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>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</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>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200805</creationdate><title>Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritis</title><author>Gao, Beixue ; Lee, Sang-Myeong ; Chen, An ; Zhang, Jinping ; Zhang, Donna D ; Kannan, Krishnaswamy ; Ortmann, Robert A ; Fang, Deyu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5357-b8ed07cc8738a97deb19df06d3f4c756b507266a5f579755870d4237a71f66a53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Apoptosis</topic><topic>Apoptosis - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gao, Beixue</au><au>Lee, Sang-Myeong</au><au>Chen, An</au><au>Zhang, Jinping</au><au>Zhang, Donna D</au><au>Kannan, Krishnaswamy</au><au>Ortmann, Robert A</au><au>Fang, Deyu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritis</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2008-05</date><risdate>2008</risdate><volume>9</volume><issue>5</issue><spage>480</spage><epage>485</epage><pages>480-485</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><coden>ERMEAX</coden><abstract>The E3 ubiquitin ligase synoviolin (SYVN1) functions as an anti‐apoptotic factor that is responsible for the outgrowth of synovial cells during the development of rheumatoid arthritis. The molecular mechanisms underlying SYVN1 regulation of cell death are largely unknown. Here, we report that elevated SYVN1 expression correlates with decreased levels of the protein inositol‐requiring enzyme 1 (IRE1)—a pro‐apoptotic factor in the endoplasmic reticulum (ER)‐stress‐induced apoptosis pathway—in synovial fibroblasts from mice with collagen‐induced arthritis (CIA). SYVN1 interacts with and catalyses IRE1 ubiquitination and consequently promotes IRE1 degradation. Suppression of SYVN1 expression in synovial fibroblasts from CIA mice restores IRE1 protein expression and reverses the resistance of ER‐stress‐induced apoptosis of CIA synovial fibroblasts. These results show that SYVN1 causes the overgrowth of synovial cells by degrading IRE1, and therefore antagonizes ER‐stress‐induced cell death.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>18369366</pmid><doi>10.1038/embor.2008.37</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Apoptosis Apoptosis - physiology Arthritis Arthritis, Experimental - metabolism Arthritis, Experimental - pathology Catalysis Cells, Cultured Cellular biology EMBO24 EMBO37 ER-stress-induced cell death Fibroblasts - metabolism Half-Life IRE1 Membrane Proteins - metabolism Mice Mice, Inbred DBA Molecular biology Mortality Protein-Serine-Threonine Kinases - metabolism Rheumatoid arthritis RNA, Small Interfering - genetics Rodents Scientific Report Synovial Membrane - cytology synoviolin Transcription Factor CHOP - metabolism Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Ubiquitination |
| title | Synoviolin promotes IRE1 ubiquitination and degradation in synovial fibroblasts from mice with collagen-induced arthritis |
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