| http://purl.uniprot.org/citations/22673745 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/22673745 | http://www.w3.org/2000/01/rdf-schema#comment | "RhoA, RhoB and RhoC GTPases are over 85% identical at the amino acid level, with RhoA and RhoC differing at only one residue (43) across the initial two-thirds of their sequences. A putative regulatory distinction between the molecules is their capacity to be uniquely activated by guanine nucleotide exchange factors (GEFs). We hypothesize that variation of amino acid residue 43 between RhoA/B (valine) and RhoC (isoleucine) impacts GEF activity. Direct participation of residue 43 in GEF-catalyzed exchange was confirmed by the observation that mutation of this position to a threonine reduced GEF-catalyzed nucleotide exchange activity in vitro (Vav2, XPLN, GEFT, Dbl and Dbs) and greatly depressed RhoA and RhoC GTP-loading profiles in cell lysates. Using a residue swap approach, substitution of RhoA Val 43 with an Ile was found to significantly promote basal nucleotide exchange activity and enhance GTP-loading in cells. Substitution of Val 43 with an Ile in RhoB negatively affected nucleotide exchange in vitro. Substitution of RhoC Ile 43 with a Val increased GEF-catalyzed exchange in vitro. In addition, RhoC-I43V was more efficacious at driving ovarian cancer cell invasion through matrigrel than wild-type RhoC, RhoC-I43T, wild-type RhoA, RhoA-V43I or RhoA-V43T GTPases. These findings suggest that a divergence between RhoA/B and RhoC at residue 43 impacts basal and GEF-stimulated nucleotide exchange activity."xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.org/dc/terms/identifier | "doi:10.4161/sgtp.19557"xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/author | "Ellerbroek S.M."xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/author | "DeMali K.A."xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/author | "Sloan C.M."xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/author | "Farley J."xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/author | "Peters J.P."xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/author | "Wernli M."xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/author | "Goetzinger C."xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/author | "Quinn C.V."xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/name | "Small GTPases"xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/pages | "15-22"xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/title | "Divergence of Rho residue 43 impacts GEF activity."xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://purl.uniprot.org/core/volume | "3"xsd:string |
| http://purl.uniprot.org/citations/22673745 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/22673745 |
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