Structural basis for the selective activation of Rho GTPases by Dbl exchange factors
Activation of Rho-family GTPases involves the removal of bound GDP and the subsequent loading of GTP, all catalyzed by guanine nucleotide exchange factors (GEFs) of the Dbl-family. Despite high sequence conservation among Rho GTPases, Dbl proteins possess a wide spectrum of discriminatory potentials...
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| Veröffentlicht in: | NAT. STRUCT. MOL. BIOL 2002-06, Vol.9 (6), p.468-475 |
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| creator | Sondek, John Snyder, Jason T Worthylake, David K Rossman, Kent L Betts, Laurie Pruitt, Wendy M Siderovski, David P Der, Channing J |
| description | Activation of Rho-family GTPases involves the removal of bound GDP and the subsequent loading of GTP, all catalyzed by guanine nucleotide exchange factors (GEFs) of the Dbl-family. Despite high sequence conservation among Rho GTPases, Dbl proteins possess a wide spectrum of discriminatory potentials for Rho-family members. To rationalize this specificity, we have determined crystal structures of the conserved, catalytic fragments (Dbl and pleckstrin homology domains) of the exchange factors intersectin and Dbs in complex with their cognate GTPases, Cdc42 and RhoA, respectively. Structure-based mutagenesis of intersectin and Dbs reveals the key determinants responsible for promoting exchange activity in Cdc42, Rac1 and RhoA. These findings provide critical insight into the structural features necessary for the proper pairing of Dbl-exchange factors with Rho GTPases and now allow for the detailed manipulation of signaling pathways mediated by these oncoproteins
in vivo
. |
| doi_str_mv | 10.1038/nsb796 |
| format | Article |
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in vivo
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in vivo
.</description><subject>Amino Acid Sequence</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>cdc42 GTP-Binding Protein - chemistry</subject><subject>cdc42 GTP-Binding Protein - metabolism</subject><subject>CHEMICAL ACTIVATION</subject><subject>Crystallography, X-Ray</subject><subject>Enzyme Activation</subject><subject>ENZYME ACTIVITY</subject><subject>GTP-ASES</subject><subject>Guanine Nucleotide Exchange Factors - chemistry</subject><subject>Guanine Nucleotide Exchange Factors - metabolism</subject><subject>Guanosine Triphosphate - metabolism</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>MORPHOLOGY</subject><subject>national synchrotron light source</subject><subject>Protein Structure</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Proto-Oncogene Proteins - chemistry</subject><subject>rac1 GTP-Binding Protein - chemistry</subject><subject>rac1 GTP-Binding Protein - metabolism</subject><subject>rho GTP-Binding Proteins - chemistry</subject><subject>rho GTP-Binding Proteins - metabolism</subject><subject>rhoA GTP-Binding Protein - chemistry</subject><subject>rhoA GTP-Binding Protein - metabolism</subject><subject>Sequence Alignment</subject><subject>Structure-Activity Relationship</subject><subject>Substrate Specificity</subject><subject>T-Lymphoma Invasion and Metastasis-inducing Protein 1</subject><issn>1072-8368</issn><issn>1545-9993</issn><issn>2331-365X</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNpl0MtKAzEUBuAgiq23JxCJLnQ1mttMM0upWoWCohXcDUl6xk5pJzXJiH17U2awC7M5i_Px5_AjdELJNSVc3tReD_JsB_UZ5zThWfqxi_qUDFgieSZ76MD7OSFUCJLvox5lhGS5FH00eQuuMaFxaoG18pXHpXU4zAB7WIAJ1TdgtRkqVLbGtsSvM4tHkxflwWO9xnd6geHHzFT9CbiM1Dp_hPZKtfBw3M1D9P5wPxk-JuPn0dPwdpwYIQYhmVIKeXys5BqMUcByaWQJgnCRlZTJAZUMaM6kziQneko0TzOTEsOpFlrxQ3Te5lofqsKbKoCZGVvX8fBCSiEYieaiNStnvxrwoZjbxtXxrIIxybKUpzyiyxYZZ713UBYrVy2VWxeUFJt-i7bfCM-6tEYvYbplXaERXLXAx1WsxG2_-xd12spaxfrhL6pb_wJZXovz</recordid><startdate>20020601</startdate><enddate>20020601</enddate><creator>Sondek, John</creator><creator>Snyder, Jason T</creator><creator>Worthylake, David K</creator><creator>Rossman, Kent L</creator><creator>Betts, Laurie</creator><creator>Pruitt, Wendy M</creator><creator>Siderovski, David P</creator><creator>Der, Channing J</creator><general>Nature Publishing Group US</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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</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>8G5</scope><scope>ABUWG</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>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>OTOTI</scope></search><sort><creationdate>20020601</creationdate><title>Structural basis for the selective activation of Rho GTPases by Dbl exchange factors</title><author>Sondek, John ; Snyder, Jason T ; Worthylake, David K ; Rossman, Kent L ; Betts, Laurie ; Pruitt, Wendy M ; Siderovski, David P ; Der, Channing J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-d11e99992f3beccae298c8fe40346f1287182e1928b6830bd0b356c50c31b4ba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>cdc42 GTP-Binding Protein - chemistry</topic><topic>cdc42 GTP-Binding Protein - metabolism</topic><topic>CHEMICAL ACTIVATION</topic><topic>Crystallography, X-Ray</topic><topic>Enzyme Activation</topic><topic>ENZYME ACTIVITY</topic><topic>GTP-ASES</topic><topic>Guanine Nucleotide Exchange Factors - chemistry</topic><topic>Guanine Nucleotide Exchange Factors - metabolism</topic><topic>Guanosine Triphosphate - metabolism</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Membrane Biology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>MORPHOLOGY</topic><topic>national synchrotron light source</topic><topic>Protein Structure</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>Proto-Oncogene Proteins - chemistry</topic><topic>rac1 GTP-Binding Protein - chemistry</topic><topic>rac1 GTP-Binding Protein - metabolism</topic><topic>rho GTP-Binding Proteins - chemistry</topic><topic>rho GTP-Binding Proteins - 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STRUCT. MOL. BIOL</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sondek, John</au><au>Snyder, Jason T</au><au>Worthylake, David K</au><au>Rossman, Kent L</au><au>Betts, Laurie</au><au>Pruitt, Wendy M</au><au>Siderovski, David P</au><au>Der, Channing J</au><aucorp>Brookhaven National Laboratory (BNL) National Synchrotron Light Source (NSLS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural basis for the selective activation of Rho GTPases by Dbl exchange factors</atitle><jtitle>NAT. STRUCT. MOL. BIOL</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Biol</addtitle><date>2002-06-01</date><risdate>2002</risdate><volume>9</volume><issue>6</issue><spage>468</spage><epage>475</epage><pages>468-475</pages><issn>1072-8368</issn><issn>1545-9993</issn><eissn>2331-365X</eissn><eissn>1545-9985</eissn><abstract>Activation of Rho-family GTPases involves the removal of bound GDP and the subsequent loading of GTP, all catalyzed by guanine nucleotide exchange factors (GEFs) of the Dbl-family. Despite high sequence conservation among Rho GTPases, Dbl proteins possess a wide spectrum of discriminatory potentials for Rho-family members. To rationalize this specificity, we have determined crystal structures of the conserved, catalytic fragments (Dbl and pleckstrin homology domains) of the exchange factors intersectin and Dbs in complex with their cognate GTPases, Cdc42 and RhoA, respectively. Structure-based mutagenesis of intersectin and Dbs reveals the key determinants responsible for promoting exchange activity in Cdc42, Rac1 and RhoA. These findings provide critical insight into the structural features necessary for the proper pairing of Dbl-exchange factors with Rho GTPases and now allow for the detailed manipulation of signaling pathways mediated by these oncoproteins
in vivo
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| subjects | Amino Acid Sequence BASIC BIOLOGICAL SCIENCES Biochemistry Biological Microscopy Biomedical and Life Sciences cdc42 GTP-Binding Protein - chemistry cdc42 GTP-Binding Protein - metabolism CHEMICAL ACTIVATION Crystallography, X-Ray Enzyme Activation ENZYME ACTIVITY GTP-ASES Guanine Nucleotide Exchange Factors - chemistry Guanine Nucleotide Exchange Factors - metabolism Guanosine Triphosphate - metabolism Humans Life Sciences Membrane Biology Models, Molecular Molecular Sequence Data MORPHOLOGY national synchrotron light source Protein Structure Protein Structure, Secondary Protein Structure, Tertiary Proteins - chemistry Proteins - metabolism Proto-Oncogene Proteins - chemistry rac1 GTP-Binding Protein - chemistry rac1 GTP-Binding Protein - metabolism rho GTP-Binding Proteins - chemistry rho GTP-Binding Proteins - metabolism rhoA GTP-Binding Protein - chemistry rhoA GTP-Binding Protein - metabolism Sequence Alignment Structure-Activity Relationship Substrate Specificity T-Lymphoma Invasion and Metastasis-inducing Protein 1 |
| title | Structural basis for the selective activation of Rho GTPases by Dbl exchange factors |
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