| http://purl.uniprot.org/citations/11604500 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11604500 | http://www.w3.org/2000/01/rdf-schema#comment | "Tyrosine phosphorylation of CAS (Crk-associated substrate, p130(Cas)) has been implicated as a key signaling step in integrin control of normal cellular behaviors, including motility, proliferation, and survival. Aberrant CAS tyrosine phosphorylation may contribute to cell transformation by certain oncoproteins, including v-Crk and v-Src, and to tumor growth and metastasis. The CAS substrate domain (SD) contains 15 Tyr-X-X-Pro motifs, which are thought to represent the major tyrosine phosphorylation sites and to function by recruiting downstream signaling effectors, including c-Crk and Nck. CAS makes multiple interactions, direct and indirect, with the tyrosine kinases Src and focal adhesion kinase (FAK), and as a result of this complexity, several plausible models have been proposed for the mechanism of CAS-SD phosphorylation. The objective of this study was to provide experimental tests of these models in order to determine the most likely mechanism(s) of CAS-SD tyrosine phosphorylation by FAK and Src. In vitro kinase assays indicated that FAK has a very poor capacity to phosphorylate CAS-SD, relative to Src. However, FAK expression along with Src was found to be important for achieving high levels of CAS tyrosine phosphorylation in COS-7 cells, as well as recovery of CAS-associated Src activity toward the SD. Structure-functional studies for both FAK and CAS further indicated that FAK plays a major role in regulating CAS-SD phosphorylation by acting as a docking or scaffolding protein to recruit Src to phosphorylate CAS, while a secondary FAK-independent mechanism involves Src directly bound to the CAS Src-binding domain (SBD). Our results do not support models in which FAK either phosphorylates CAS-SD directly or phosphorylates CAS-SBD to promote Src binding to this site."xsd:string |
| http://purl.uniprot.org/citations/11604500 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.21.22.7641-7652.2001"xsd:string |
| http://purl.uniprot.org/citations/11604500 | http://purl.uniprot.org/core/author | "Zhang X."xsd:string |
| http://purl.uniprot.org/citations/11604500 | http://purl.uniprot.org/core/author | "Hanks S.K."xsd:string |
| http://purl.uniprot.org/citations/11604500 | http://purl.uniprot.org/core/author | "Polte T.R."xsd:string |
| http://purl.uniprot.org/citations/11604500 | http://purl.uniprot.org/core/author | "Ruest P.J."xsd:string |
| http://purl.uniprot.org/citations/11604500 | http://purl.uniprot.org/core/author | "Shin N.Y."xsd:string |
| http://purl.uniprot.org/citations/11604500 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11604500 | http://purl.uniprot.org/core/name | "Mol Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/11604500 | http://purl.uniprot.org/core/pages | "7641-7652"xsd:string |
| http://purl.uniprot.org/citations/11604500 | http://purl.uniprot.org/core/title | "Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src."xsd:string |
| http://purl.uniprot.org/citations/11604500 | http://purl.uniprot.org/core/volume | "21"xsd:string |
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| http://purl.uniprot.org/uniprot/P35968 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/11604500 |