PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130
Maintenance of the Golgi apparatus （GA） structure and function depends on Golgi matrix proteins. The posttranslational modification of Golgi proteins such as phosphorylation of members of the golgin and GRASP families is important for determining Golgi architecture. Some Golgi proteins including gol...
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| Veröffentlicht in: | Cell research 2010-09, Vol.20 (9), p.1023-1033 |
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| container_title | Cell research |
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| creator | Zhou, Zhongwei Sun, Xiaotian Zou, Zhenhua Sun, Litao Zhang, Tao Guo, Shaoshi Wen, Ya Liu, Lin Wang, Yi Qin, Jun Li, Lei Gong, Weimin Bao, Shilai |
| description | Maintenance of the Golgi apparatus （GA） structure and function depends on Golgi matrix proteins. The posttranslational modification of Golgi proteins such as phosphorylation of members of the golgin and GRASP families is important for determining Golgi architecture. Some Golgi proteins including golgin-84 are also known to be methylated, but the function of golgin methylation remains unclear. Here, we show that the protein arginine methyltransferase 5 （PRMT5） localizes to the GA and forms complexes with several components involved in GA ribbon formation and vesicle tethering. PRMT5 interacts with the golgin GM130, and depletion of PRMT5 causes defects in Golgi ribbon formation. Furthermore, PRMT5 methylates N-terminal arginines in GM130, and such arginine methylation appears critical for GA ribbon formation. Our findings reveal a molecular mechanism by which PRMT5-dependent arginine methylation of GM130 controls the maintenance of GA architecture. |
| doi_str_mv | 10.1038/cr.2010.56 |
| format | Article |
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The posttranslational modification of Golgi proteins such as phosphorylation of members of the golgin and GRASP families is important for determining Golgi architecture. Some Golgi proteins including golgin-84 are also known to be methylated, but the function of golgin methylation remains unclear. Here, we show that the protein arginine methyltransferase 5 （PRMT5） localizes to the GA and forms complexes with several components involved in GA ribbon formation and vesicle tethering. PRMT5 interacts with the golgin GM130, and depletion of PRMT5 causes defects in Golgi ribbon formation. Furthermore, PRMT5 methylates N-terminal arginines in GM130, and such arginine methylation appears critical for GA ribbon formation. Our findings reveal a molecular mechanism by which PRMT5-dependent arginine methylation of GM130 controls the maintenance of GA architecture.</description><identifier>ISSN: 1001-0602</identifier><identifier>EISSN: 1748-7838</identifier><identifier>DOI: 10.1038/cr.2010.56</identifier><identifier>PMID: 20421892</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/45/607/1172 ; 631/80/458/1648 ; 631/80/642/1525 ; Arginine - metabolism ; Autoantigens - metabolism ; Biomedical and Life Sciences ; Cell Biology ; Cell Line, Tumor ; Golgi Apparatus - chemistry ; Golgi Apparatus - enzymology ; Golgi Apparatus - ultrastructure ; Humans ; Life Sciences ; Membrane Proteins - metabolism ; Methylation ; original-article ; Protein Methyltransferases - analysis ; Protein Methyltransferases - genetics ; Protein Methyltransferases - metabolism ; Protein-Arginine N-Methyltransferases ; Proteins ; RNA Interference ; 基体结构 ; 基质蛋白 ; 家庭成员 ; 甲基化 ; 精氨酸 ; 蛋白质 ; 通用航空 ; 高尔基体</subject><ispartof>Cell research, 2010-09, Vol.20 (9), p.1023-1033</ispartof><rights>Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences 2010</rights><rights>Copyright Nature Publishing Group Sep 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c413t-9e0fa6d9a859f710f127ef41b38db9112617ecf91149923ae3564dc6fc511f2a3</citedby><cites>FETCH-LOGICAL-c413t-9e0fa6d9a859f710f127ef41b38db9112617ecf91149923ae3564dc6fc511f2a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://image.cqvip.com/vip1000/qk/85240X/85240X.jpg</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/cr.2010.56$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/cr.2010.56$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20421892$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhou, Zhongwei</creatorcontrib><creatorcontrib>Sun, Xiaotian</creatorcontrib><creatorcontrib>Zou, Zhenhua</creatorcontrib><creatorcontrib>Sun, Litao</creatorcontrib><creatorcontrib>Zhang, Tao</creatorcontrib><creatorcontrib>Guo, Shaoshi</creatorcontrib><creatorcontrib>Wen, Ya</creatorcontrib><creatorcontrib>Liu, Lin</creatorcontrib><creatorcontrib>Wang, Yi</creatorcontrib><creatorcontrib>Qin, Jun</creatorcontrib><creatorcontrib>Li, Lei</creatorcontrib><creatorcontrib>Gong, Weimin</creatorcontrib><creatorcontrib>Bao, Shilai</creatorcontrib><title>PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130</title><title>Cell research</title><addtitle>Cell Res</addtitle><addtitle>Cell Research</addtitle><description>Maintenance of the Golgi apparatus （GA） structure and function depends on Golgi matrix proteins. The posttranslational modification of Golgi proteins such as phosphorylation of members of the golgin and GRASP families is important for determining Golgi architecture. Some Golgi proteins including golgin-84 are also known to be methylated, but the function of golgin methylation remains unclear. Here, we show that the protein arginine methyltransferase 5 （PRMT5） localizes to the GA and forms complexes with several components involved in GA ribbon formation and vesicle tethering. PRMT5 interacts with the golgin GM130, and depletion of PRMT5 causes defects in Golgi ribbon formation. Furthermore, PRMT5 methylates N-terminal arginines in GM130, and such arginine methylation appears critical for GA ribbon formation. Our findings reveal a molecular mechanism by which PRMT5-dependent arginine methylation of GM130 controls the maintenance of GA architecture.</description><subject>631/45/607/1172</subject><subject>631/80/458/1648</subject><subject>631/80/642/1525</subject><subject>Arginine - metabolism</subject><subject>Autoantigens - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Biology</subject><subject>Cell Line, Tumor</subject><subject>Golgi Apparatus - chemistry</subject><subject>Golgi Apparatus - enzymology</subject><subject>Golgi Apparatus - ultrastructure</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Membrane Proteins - metabolism</subject><subject>Methylation</subject><subject>original-article</subject><subject>Protein Methyltransferases - analysis</subject><subject>Protein Methyltransferases - genetics</subject><subject>Protein Methyltransferases - metabolism</subject><subject>Protein-Arginine N-Methyltransferases</subject><subject>Proteins</subject><subject>RNA Interference</subject><subject>基体结构</subject><subject>基质蛋白</subject><subject>家庭成员</subject><subject>甲基化</subject><subject>精氨酸</subject><subject>蛋白质</subject><subject>通用航空</subject><subject>高尔基体</subject><issn>1001-0602</issn><issn>1748-7838</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNptkE9PGzEQxa2qqPwpFz5AZZVDJdBSj73eXR8RKqFSImgFZ8txxpulm3Virw98exwlrVCFfPCM_XtvRo-QM2BXwETz3YYrznIjqw_kCOqyKepGNB9zzRgUrGL8kBzH-MwYl6WET-SQs5JDo_gR-fXwe_YoacA29WbESCe-bztq1msTzJgijWNIdkwB6bgMPrVLusJx-ZLhzg_Uu_yMtN2KBjqZgWCfyYEzfcTT_X1Cnm5_PN7cFdP7yc-b62lhSxBjoZA5Uy2UaaRyNTAHvEZXwlw0i7kC4BXUaF2uSqW4MChkVS5s5awEcNyIE_Jt57sOfpMwjnrVRYt9bwb0KepaCqWyOWTy_D_y2acw5OU0MF7nMETJMnWxo2zwMQZ0eh26lQkvGdLbnLUNepuzllWGv-wt03yFi3_o32AzcLkDYv4aWgxvZ75j93U_e-mHdpMFem7sH9f1qIWUKp9GvAIx0ZAH</recordid><startdate>20100901</startdate><enddate>20100901</enddate><creator>Zhou, Zhongwei</creator><creator>Sun, Xiaotian</creator><creator>Zou, Zhenhua</creator><creator>Sun, Litao</creator><creator>Zhang, Tao</creator><creator>Guo, Shaoshi</creator><creator>Wen, Ya</creator><creator>Liu, Lin</creator><creator>Wang, Yi</creator><creator>Qin, Jun</creator><creator>Li, Lei</creator><creator>Gong, Weimin</creator><creator>Bao, Shilai</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>W94</scope><scope>WU4</scope><scope>~WA</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>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</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>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20100901</creationdate><title>PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130</title><author>Zhou, Zhongwei ; Sun, Xiaotian ; Zou, Zhenhua ; Sun, Litao ; Zhang, Tao ; Guo, Shaoshi ; Wen, Ya ; Liu, Lin ; Wang, Yi ; Qin, Jun ; Li, Lei ; Gong, Weimin ; Bao, Shilai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-9e0fa6d9a859f710f127ef41b38db9112617ecf91149923ae3564dc6fc511f2a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>631/45/607/1172</topic><topic>631/80/458/1648</topic><topic>631/80/642/1525</topic><topic>Arginine - 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Academic</collection><jtitle>Cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhou, Zhongwei</au><au>Sun, Xiaotian</au><au>Zou, Zhenhua</au><au>Sun, Litao</au><au>Zhang, Tao</au><au>Guo, Shaoshi</au><au>Wen, Ya</au><au>Liu, Lin</au><au>Wang, Yi</au><au>Qin, Jun</au><au>Li, Lei</au><au>Gong, Weimin</au><au>Bao, Shilai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130</atitle><jtitle>Cell research</jtitle><stitle>Cell Res</stitle><addtitle>Cell Research</addtitle><date>2010-09-01</date><risdate>2010</risdate><volume>20</volume><issue>9</issue><spage>1023</spage><epage>1033</epage><pages>1023-1033</pages><issn>1001-0602</issn><eissn>1748-7838</eissn><abstract>Maintenance of the Golgi apparatus （GA） structure and function depends on Golgi matrix proteins. The posttranslational modification of Golgi proteins such as phosphorylation of members of the golgin and GRASP families is important for determining Golgi architecture. Some Golgi proteins including golgin-84 are also known to be methylated, but the function of golgin methylation remains unclear. Here, we show that the protein arginine methyltransferase 5 （PRMT5） localizes to the GA and forms complexes with several components involved in GA ribbon formation and vesicle tethering. PRMT5 interacts with the golgin GM130, and depletion of PRMT5 causes defects in Golgi ribbon formation. Furthermore, PRMT5 methylates N-terminal arginines in GM130, and such arginine methylation appears critical for GA ribbon formation. Our findings reveal a molecular mechanism by which PRMT5-dependent arginine methylation of GM130 controls the maintenance of GA architecture.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>20421892</pmid><doi>10.1038/cr.2010.56</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/45/607/1172 631/80/458/1648 631/80/642/1525 Arginine - metabolism Autoantigens - metabolism Biomedical and Life Sciences Cell Biology Cell Line, Tumor Golgi Apparatus - chemistry Golgi Apparatus - enzymology Golgi Apparatus - ultrastructure Humans Life Sciences Membrane Proteins - metabolism Methylation original-article Protein Methyltransferases - analysis Protein Methyltransferases - genetics Protein Methyltransferases - metabolism Protein-Arginine N-Methyltransferases Proteins RNA Interference 基体结构 基质蛋白 家庭成员 甲基化 精氨酸 蛋白质 通用航空 高尔基体 |
| title | PRMT5 regulates Golgi apparatus structure through methylation of the golgin GM130 |
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