Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex
Mammalian Dock180 and ELMO proteins, and their homologues in Caenorhabditis elegans and Drosophila melanogaster , function as critical upstream regulators of Rac during development and cell migration. The mechanism by which Dock180 or ELMO mediates Rac activation is not understood. Here, we identify...
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| Veröffentlicht in: | Nature cell biology 2002-08, Vol.4 (8), p.574-582 |
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| creator | Brugnera, Enrico Haney, Lisa Grimsley, Cynthia Lu, Mingjian Walk, Scott F. Tosello-Trampont, Annie-Carole Macara, Ian G. Madhani, Hiten Fink, Gerald R. Ravichandran, Kodimangalam S. |
| description | Mammalian Dock180 and ELMO proteins, and their homologues in
Caenorhabditis elegans
and
Drosophila melanogaster
, function as critical upstream regulators of Rac during development and cell migration. The mechanism by which Dock180 or ELMO mediates Rac activation is not understood. Here, we identify a domain within Dock180 (denoted Docker) that specifically recognizes nucleotide-free Rac and can mediate GTP loading of Rac
in vitro
. The Docker domain is conserved among known Dock180 family members in metazoans and in a yeast protein. In cells, binding of Dock180 to Rac alone is insufficient for GTP loading, and a Dock180–ELMO1 interaction is required. We can also detect a trimeric ELMO1–Dock180–Rac1 complex and ELMO augments the interaction between Dock180 and Rac. We propose that the Dock180–ELMO complex functions as an unconventional two-part exchange factor for Rac. |
| doi_str_mv | 10.1038/ncb824 |
| format | Article |
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Caenorhabditis elegans
and
Drosophila melanogaster
, function as critical upstream regulators of Rac during development and cell migration. The mechanism by which Dock180 or ELMO mediates Rac activation is not understood. Here, we identify a domain within Dock180 (denoted Docker) that specifically recognizes nucleotide-free Rac and can mediate GTP loading of Rac
in vitro
. The Docker domain is conserved among known Dock180 family members in metazoans and in a yeast protein. In cells, binding of Dock180 to Rac alone is insufficient for GTP loading, and a Dock180–ELMO1 interaction is required. We can also detect a trimeric ELMO1–Dock180–Rac1 complex and ELMO augments the interaction between Dock180 and Rac. We propose that the Dock180–ELMO complex functions as an unconventional two-part exchange factor for Rac.</description><identifier>ISSN: 1465-7392</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/ncb824</identifier><identifier>PMID: 12134158</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Binding Sites ; Biomedical and Life Sciences ; Caenorhabditis elegans ; Caenorhabditis elegans Proteins ; Cancer Research ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; Cell adhesion & migration ; Cell Biology ; Cell Line ; Cellular proteins ; Cellular signal transduction ; Cytoskeletal Proteins ; Developmental Biology ; Drosophila melanogaster ; Guanine ; Guanine Nucleotide Exchange Factors - metabolism ; Guanosine Triphosphate - metabolism ; Humans ; Insects ; Life Sciences ; Macromolecular Substances ; Mammals ; Metazoa ; Molecular Sequence Data ; Phagocytosis ; Physiological aspects ; Protein Structure, Tertiary ; Proteins ; Proteins - chemistry ; Proteins - genetics ; Proteins - metabolism ; rac GTP-Binding Proteins - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Sequence Homology, Amino Acid ; Stem Cells ; Upstream ; Yeasts</subject><ispartof>Nature cell biology, 2002-08, Vol.4 (8), p.574-582</ispartof><rights>Springer Nature Limited 2002</rights><rights>COPYRIGHT 2002 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Aug 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c505t-6c094edcc91af4edb5316c12780d3d8efbcf99fc2baec8d665a686dc39a5e42d3</citedby><cites>FETCH-LOGICAL-c505t-6c094edcc91af4edb5316c12780d3d8efbcf99fc2baec8d665a686dc39a5e42d3</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/ncb824$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/ncb824$$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/12134158$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Brugnera, Enrico</creatorcontrib><creatorcontrib>Haney, Lisa</creatorcontrib><creatorcontrib>Grimsley, Cynthia</creatorcontrib><creatorcontrib>Lu, Mingjian</creatorcontrib><creatorcontrib>Walk, Scott F.</creatorcontrib><creatorcontrib>Tosello-Trampont, Annie-Carole</creatorcontrib><creatorcontrib>Macara, Ian G.</creatorcontrib><creatorcontrib>Madhani, Hiten</creatorcontrib><creatorcontrib>Fink, Gerald R.</creatorcontrib><creatorcontrib>Ravichandran, Kodimangalam S.</creatorcontrib><title>Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex</title><title>Nature cell biology</title><addtitle>Nat Cell Biol</addtitle><addtitle>Nat Cell Biol</addtitle><description>Mammalian Dock180 and ELMO proteins, and their homologues in
Caenorhabditis elegans
and
Drosophila melanogaster
, function as critical upstream regulators of Rac during development and cell migration. The mechanism by which Dock180 or ELMO mediates Rac activation is not understood. Here, we identify a domain within Dock180 (denoted Docker) that specifically recognizes nucleotide-free Rac and can mediate GTP loading of Rac
in vitro
. The Docker domain is conserved among known Dock180 family members in metazoans and in a yeast protein. In cells, binding of Dock180 to Rac alone is insufficient for GTP loading, and a Dock180–ELMO1 interaction is required. We can also detect a trimeric ELMO1–Dock180–Rac1 complex and ELMO augments the interaction between Dock180 and Rac. We propose that the Dock180–ELMO complex functions as an unconventional two-part exchange factor for Rac.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Biomedical and Life Sciences</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans Proteins</subject><subject>Cancer Research</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell adhesion & migration</subject><subject>Cell Biology</subject><subject>Cell Line</subject><subject>Cellular proteins</subject><subject>Cellular signal transduction</subject><subject>Cytoskeletal Proteins</subject><subject>Developmental Biology</subject><subject>Drosophila melanogaster</subject><subject>Guanine</subject><subject>Guanine Nucleotide Exchange Factors - metabolism</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Humans</subject><subject>Insects</subject><subject>Life Sciences</subject><subject>Macromolecular Substances</subject><subject>Mammals</subject><subject>Metazoa</subject><subject>Molecular Sequence Data</subject><subject>Phagocytosis</subject><subject>Physiological aspects</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>rac GTP-Binding Proteins - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Stem Cells</subject><subject>Upstream</subject><subject>Yeasts</subject><issn>1465-7392</issn><issn>1476-4679</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNp9kc9u1DAQxi0EoqXAI6CIA4hDiv_FsY9V2ZZKC5UKPVuOPdm6JPHWdqr2xjvwhjwJrnalVXtAtjQj-zejme9D6C3BhwQz-XmynaT8GdonvBU1F616_pCLpm6ZonvoVUrXGBPOcfsS7RFKGCeN3EffLycbpluYsg-TGaoLY-vTxUllbPa3Pt9XPlUjOG8yuCpfxTCvrkqE6kuwv4jEf3__WSy_nVc2jOsB7l6jF70ZErzZxgN0ebL4efy1Xp6fnh0fLWvb4CbXwmLFwVmriOlL0jWMCEtoK7FjTkLf2V6p3tLOgJVOiMYIKZxlyjTAqWMH6OOm7zqGmxlS1qNPFobBTBDmpKXArKWNoIX88F-yJUqViwv4_gl4HeZYNEmaUsoEb5Qo0OEGWpkBtJ_6kKOx5TgYfRESel_ej4hkVLaC8FLw6VFBYTLc5ZWZU9JnPy4es9tRbQwpRej1OvrRxHtNsH5wWW9cLuC77ahzV8zZYVtbd_Kk8jWtIO52edLqH2bGrcY</recordid><startdate>20020801</startdate><enddate>20020801</enddate><creator>Brugnera, Enrico</creator><creator>Haney, Lisa</creator><creator>Grimsley, Cynthia</creator><creator>Lu, Mingjian</creator><creator>Walk, Scott F.</creator><creator>Tosello-Trampont, Annie-Carole</creator><creator>Macara, Ian G.</creator><creator>Madhani, Hiten</creator><creator>Fink, Gerald R.</creator><creator>Ravichandran, Kodimangalam S.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><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>ISR</scope><scope>3V.</scope><scope>7QL</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>88A</scope><scope>88E</scope><scope>8AO</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>C1K</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><scope>F1W</scope><scope>H98</scope><scope>L.G</scope></search><sort><creationdate>20020801</creationdate><title>Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex</title><author>Brugnera, Enrico ; Haney, Lisa ; Grimsley, Cynthia ; Lu, Mingjian ; Walk, Scott F. ; Tosello-Trampont, Annie-Carole ; Macara, Ian G. ; Madhani, Hiten ; Fink, Gerald R. ; Ravichandran, Kodimangalam S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-6c094edcc91af4edb5316c12780d3d8efbcf99fc2baec8d665a686dc39a5e42d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Biomedical and Life Sciences</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans Proteins</topic><topic>Cancer Research</topic><topic>Carrier Proteins - 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Academic</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Aquaculture Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Nature cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Brugnera, Enrico</au><au>Haney, Lisa</au><au>Grimsley, Cynthia</au><au>Lu, Mingjian</au><au>Walk, Scott F.</au><au>Tosello-Trampont, Annie-Carole</au><au>Macara, Ian G.</au><au>Madhani, Hiten</au><au>Fink, Gerald R.</au><au>Ravichandran, Kodimangalam S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex</atitle><jtitle>Nature cell biology</jtitle><stitle>Nat Cell Biol</stitle><addtitle>Nat Cell Biol</addtitle><date>2002-08-01</date><risdate>2002</risdate><volume>4</volume><issue>8</issue><spage>574</spage><epage>582</epage><pages>574-582</pages><issn>1465-7392</issn><eissn>1476-4679</eissn><abstract>Mammalian Dock180 and ELMO proteins, and their homologues in
Caenorhabditis elegans
and
Drosophila melanogaster
, function as critical upstream regulators of Rac during development and cell migration. The mechanism by which Dock180 or ELMO mediates Rac activation is not understood. Here, we identify a domain within Dock180 (denoted Docker) that specifically recognizes nucleotide-free Rac and can mediate GTP loading of Rac
in vitro
. The Docker domain is conserved among known Dock180 family members in metazoans and in a yeast protein. In cells, binding of Dock180 to Rac alone is insufficient for GTP loading, and a Dock180–ELMO1 interaction is required. We can also detect a trimeric ELMO1–Dock180–Rac1 complex and ELMO augments the interaction between Dock180 and Rac. We propose that the Dock180–ELMO complex functions as an unconventional two-part exchange factor for Rac.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>12134158</pmid><doi>10.1038/ncb824</doi><tpages>9</tpages></addata></record> |
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| ispartof | Nature cell biology, 2002-08, Vol.4 (8), p.574-582 |
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| language | eng |
| recordid | cdi_proquest_miscellaneous_860372562 |
| source | MEDLINE; Nature Journals Online; SpringerLink Journals - AutoHoldings |
| subjects | Adaptor Proteins, Signal Transducing Amino Acid Sequence Animals Binding Sites Biomedical and Life Sciences Caenorhabditis elegans Caenorhabditis elegans Proteins Cancer Research Carrier Proteins - chemistry Carrier Proteins - metabolism Cell adhesion & migration Cell Biology Cell Line Cellular proteins Cellular signal transduction Cytoskeletal Proteins Developmental Biology Drosophila melanogaster Guanine Guanine Nucleotide Exchange Factors - metabolism Guanosine Triphosphate - metabolism Humans Insects Life Sciences Macromolecular Substances Mammals Metazoa Molecular Sequence Data Phagocytosis Physiological aspects Protein Structure, Tertiary Proteins Proteins - chemistry Proteins - genetics Proteins - metabolism rac GTP-Binding Proteins - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Homology, Amino Acid Stem Cells Upstream Yeasts |
| title | Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex |
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