RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo
The small GTPase Rac has a central role in regulating the actin cytoskeleton during cell migration and axon guidance 1 . Elmo has been identified as an upstream regulator of Rac1 that binds to and functionally cooperates with Dock180 (refs 2–4 ). Dock180 does not contain a conventional catalytic dom...
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| Veröffentlicht in: | Nature (London) 2003-07, Vol.424 (6947), p.461-464 |
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| creator | Katoh, Hironori Negishi, Manabu |
| description | The small GTPase Rac has a central role in regulating the actin cytoskeleton during cell migration and axon guidance
1
. Elmo has been identified as an upstream regulator of Rac1 that binds to and functionally cooperates with Dock180 (refs
2–4
). Dock180 does not contain a conventional catalytic domain for guanine nucleotide exchange on Rac, but possesses a domain that directly binds to and specifically activates Rac1 (refs
5
,
6
). The small GTPase RhoG mediates several cellular morphological processes, such as neurite outgrowth in neuronal cells, through a signalling cascade that activates Rac1 (refs
7–12
); however, the downstream target of RhoG and the mechanism by which RhoG regulates Rac1 activity remain unclear. Here we show that RhoG interacts directly with Elmo in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG–Elmo–Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. We conclude that RhoG activates Rac1 through Elmo and Dock180 to control cell morphology. |
| doi_str_mv | 10.1038/nature01817 |
| format | Article |
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1
. Elmo has been identified as an upstream regulator of Rac1 that binds to and functionally cooperates with Dock180 (refs
2–4
). Dock180 does not contain a conventional catalytic domain for guanine nucleotide exchange on Rac, but possesses a domain that directly binds to and specifically activates Rac1 (refs
5
,
6
). The small GTPase RhoG mediates several cellular morphological processes, such as neurite outgrowth in neuronal cells, through a signalling cascade that activates Rac1 (refs
7–12
); however, the downstream target of RhoG and the mechanism by which RhoG regulates Rac1 activity remain unclear. Here we show that RhoG interacts directly with Elmo in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG–Elmo–Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. We conclude that RhoG activates Rac1 through Elmo and Dock180 to control cell morphology.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/nature01817</identifier><identifier>PMID: 12879077</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Biochemistry ; Biological and medical sciences ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell morphology ; Cell Size - drug effects ; Fluorescent Antibody Technique ; GTP Phosphohydrolases - genetics ; GTP Phosphohydrolases - metabolism ; Guanosine Triphosphate - metabolism ; HeLa Cells ; Humanities and Social Sciences ; Humans ; Integrins - metabolism ; letter ; Medical sciences ; multidisciplinary ; Mutation - genetics ; Nerve Growth Factor - pharmacology ; Neurites - metabolism ; PC12 Cells ; Protein Binding ; Protein Transport ; Proteins ; rac GTP-Binding Proteins - genetics ; rac GTP-Binding Proteins - metabolism ; rac1 GTP-Binding Protein - metabolism ; Rats ; rho GTP-Binding Proteins ; Science ; Science (multidisciplinary)</subject><ispartof>Nature (London), 2003-07, Vol.424 (6947), p.461-464</ispartof><rights>Macmillan Magazines Ltd. 2003</rights><rights>2003 INIST-CNRS</rights><rights>COPYRIGHT 2003 Nature Publishing Group</rights><rights>Copyright Macmillan Journals Ltd. Jul 24, 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c616t-fce373fd284b49c86caffb98d2ba205f44e83a8d4431c234fd12f76320ecabd53</citedby><cites>FETCH-LOGICAL-c616t-fce373fd284b49c86caffb98d2ba205f44e83a8d4431c234fd12f76320ecabd53</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/nature01817$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nature01817$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27903,27904,41467,42536,51297</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14980080$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12879077$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Katoh, Hironori</creatorcontrib><creatorcontrib>Negishi, Manabu</creatorcontrib><title>RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>The small GTPase Rac has a central role in regulating the actin cytoskeleton during cell migration and axon guidance
1
. Elmo has been identified as an upstream regulator of Rac1 that binds to and functionally cooperates with Dock180 (refs
2–4
). Dock180 does not contain a conventional catalytic domain for guanine nucleotide exchange on Rac, but possesses a domain that directly binds to and specifically activates Rac1 (refs
5
,
6
). The small GTPase RhoG mediates several cellular morphological processes, such as neurite outgrowth in neuronal cells, through a signalling cascade that activates Rac1 (refs
7–12
); however, the downstream target of RhoG and the mechanism by which RhoG regulates Rac1 activity remain unclear. Here we show that RhoG interacts directly with Elmo in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG–Elmo–Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. We conclude that RhoG activates Rac1 through Elmo and Dock180 to control cell morphology.</description><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell morphology</subject><subject>Cell Size - drug effects</subject><subject>Fluorescent Antibody Technique</subject><subject>GTP Phosphohydrolases - genetics</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>HeLa Cells</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Integrins - metabolism</subject><subject>letter</subject><subject>Medical sciences</subject><subject>multidisciplinary</subject><subject>Mutation - genetics</subject><subject>Nerve Growth Factor - pharmacology</subject><subject>Neurites - metabolism</subject><subject>PC12 Cells</subject><subject>Protein Binding</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>rac GTP-Binding Proteins - genetics</subject><subject>rac GTP-Binding Proteins - metabolism</subject><subject>rac1 GTP-Binding Protein - metabolism</subject><subject>Rats</subject><subject>rho GTP-Binding Proteins</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0tFr1DAcB_AiijunT75LEaaIdv7SpE36eJxzDoaDc-JjSdNf7jLb9Jak6v57c9zB7eRU8lBIPvmGfvklyXMCpwSoeG9lGB0CEYQ_SCaE8TJjpeAPkwlALjIQtDxKnnh_AwAF4exxckRywSvgfJJczZfDeSpVMD9kQJ_OpSJpc5e2xqEKqbEB3fp0sOlPE5ZpWGL6YVDfiYCsMbY1dpGu3BDQ2PSs64enySMtO4_Ptt_j5OvHs-vZp-zy6vxiNr3MVEnKkGmFlFPd5oI1rFKiVFLrphJt3sgcCs0YCipFyxglKqdMtyTXvKQ5oJJNW9Dj5PUmNz5-O6IPdW-8wq6TFofR15xRRop4IcpX_5a0gKIq-X8hiZ2Rkq8TX_4Bb4bR2fi7dQ6soECBRZRt0EJ2WBurhxCLXKCNfXaDRW3i9jRmcsa5YLvQPa9W5ra-j04PoLha7I06mPpm70I0AX-FhRy9ry--zPft27_b6fW32eeDWrnBe4e6XjnTS3dXE6jXc1nfm8uoX2wrG5se253dDmIEJ1sgvZKddtIq43eOVQJAQHTvNs7HI7tAt-v-0Lu_AaBn9TU</recordid><startdate>20030724</startdate><enddate>20030724</enddate><creator>Katoh, Hironori</creator><creator>Negishi, Manabu</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</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>ATWCN</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</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>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7X8</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope></search><sort><creationdate>20030724</creationdate><title>RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo</title><author>Katoh, Hironori ; Negishi, Manabu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c616t-fce373fd284b49c86caffb98d2ba205f44e83a8d4431c234fd12f76320ecabd53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - 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1
. Elmo has been identified as an upstream regulator of Rac1 that binds to and functionally cooperates with Dock180 (refs
2–4
). Dock180 does not contain a conventional catalytic domain for guanine nucleotide exchange on Rac, but possesses a domain that directly binds to and specifically activates Rac1 (refs
5
,
6
). The small GTPase RhoG mediates several cellular morphological processes, such as neurite outgrowth in neuronal cells, through a signalling cascade that activates Rac1 (refs
7–12
); however, the downstream target of RhoG and the mechanism by which RhoG regulates Rac1 activity remain unclear. Here we show that RhoG interacts directly with Elmo in a GTP-dependent manner and forms a ternary complex with Dock180 to induce activation of Rac1. The RhoG–Elmo–Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. We conclude that RhoG activates Rac1 through Elmo and Dock180 to control cell morphology.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>12879077</pmid><doi>10.1038/nature01817</doi><tpages>4</tpages></addata></record> |
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| ispartof | Nature (London), 2003-07, Vol.424 (6947), p.461-464 |
| issn | 0028-0836 1476-4687 |
| language | eng |
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| source | MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online |
| subjects | Animals Biochemistry Biological and medical sciences Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Cell morphology Cell Size - drug effects Fluorescent Antibody Technique GTP Phosphohydrolases - genetics GTP Phosphohydrolases - metabolism Guanosine Triphosphate - metabolism HeLa Cells Humanities and Social Sciences Humans Integrins - metabolism letter Medical sciences multidisciplinary Mutation - genetics Nerve Growth Factor - pharmacology Neurites - metabolism PC12 Cells Protein Binding Protein Transport Proteins rac GTP-Binding Proteins - genetics rac GTP-Binding Proteins - metabolism rac1 GTP-Binding Protein - metabolism Rats rho GTP-Binding Proteins Science Science (multidisciplinary) |
| title | RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo |
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