| http://purl.uniprot.org/citations/9399639 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9399639 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9399639 | http://www.w3.org/2000/01/rdf-schema#comment | "We have used the yeast two-hybrid system to identify proteins that interact with Vav, a GDP/GTP exchange factor for the Rac-1 GTPase that plays an important role in cell signaling and oncogenic transformation. This experimental approach resulted in the isolation of Cbl-b, a signal transduction molecule highly related to the mammalian c-cbl proto-oncogene product and to the C. elegans Sli-1 protein, a negative regulator of the EGF-receptor-like Let23 protein. The interaction between Vav and Cbl-b requires the entire SH3-SH2-SH3 carboxy-terminal domain of Vav and a long stretch of proline-rich sequences present in the central region of Cbl-b. Stimulation of quiescent rodent fibroblasts with either epidermal or platelet-derived growth factors induces an increased affinity of Vav for Cbl-b and results in the subsequent formation of a Vav-dependent trimeric complex with the ligand-stimulated tyrosine kinase receptors. During this process, Vav, but not Cbl-b, becomes highly phosphorylated on tyrosine residues. Overexpression of Cbl-b inhibits the signal transduction pathway of Vav that leads to the stimulation of c-Jun N-terminal kinase. By contrast, expression of truncated Cbl-b proteins and of missense mutants analogous to those found in inactive Sli-1 proteins have no detectable effect on Vav activity. These results indicate that Vav and Cbl-b act coordinately in the first steps of tyrosine protein kinase receptor-mediated signaling and suggest that members of the Sli-1/Cbl family are also negative regulators of signal transduction in mammalian cells."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.onc.1201430"xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.org/dc/terms/identifier | "doi:10.1038/sj.onc.1201430"xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/author | "Gutkind J.S."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/author | "Gutkind J.S."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/author | "Barbacid M."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/author | "Barbacid M."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/author | "Bustelo X.R."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/author | "Bustelo X.R."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/author | "Crespo P."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/author | "Crespo P."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/author | "Lopez-Barahona M."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/author | "Lopez-Barahona M."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/name | "Oncogene"xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/name | "Oncogene"xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/pages | "2511-2520"xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/pages | "2511-2520"xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/title | "Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/title | "Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation."xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/volume | "15"xsd:string |
| http://purl.uniprot.org/citations/9399639 | http://purl.uniprot.org/core/volume | "15"xsd:string |