| http://purl.uniprot.org/citations/16000375 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16000375 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16000375 | http://www.w3.org/2000/01/rdf-schema#comment | "The ArfGAP paxillin kinase linker (PKL)/G protein-coupled receptor kinase-interacting protein (GIT)2 has been implicated in regulating cell spreading and motility through its transient recruitment of the p21-activated kinase (PAK) to focal adhesions. The Nck-PAK-PIX-PKL protein complex is recruited to focal adhesions by paxillin upon integrin engagement and Rac activation. In this report, we identify tyrosine-phosphorylated PKL as a protein that associates with the SH3-SH2 adaptor Nck, in a Src-dependent manner, after cell adhesion to fibronectin. Both cell adhesion and Rac activation stimulated PKL tyrosine phosphorylation. PKL is phosphorylated on tyrosine residues 286/392/592 by Src and/or FAK and these sites are required for PKL localization to focal adhesions and for paxillin binding. The absence of either FAK or Src-family kinases prevents PKL phosphorylation and suppresses localization of PKL but not GIT1 to focal adhesions after Rac activation. Expression of an activated FAK mutant in the absence of Src-family kinases partially restores PKL localization, suggesting that Src activation of FAK is required for PKL phosphorylation and localization. Overexpression of the nonphosphorylated GFP-PKL Triple YF mutant stimulates cell spreading and protrusiveness, similar to overexpression of a paxillin mutant that does not bind PKL, suggesting that failure to recruit PKL to focal adhesions interferes with normal cell spreading and motility."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e05-02-0131"xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e05-02-0131"xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/author | "Cooper J.A."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/author | "Cooper J.A."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/author | "Turner C.E."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/author | "Turner C.E."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/author | "Brown M.C."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/author | "Brown M.C."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/author | "Cary L.A."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/author | "Cary L.A."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/author | "Jamieson J.S."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/author | "Jamieson J.S."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/name | "Mol. Biol. Cell"xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/name | "Mol. Biol. Cell"xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/pages | "4316-4328"xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/pages | "4316-4328"xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/title | "Src and FAK kinases cooperate to phosphorylate paxillin kinase linker, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/title | "Src and FAK kinases cooperate to phosphorylate paxillin kinase linker, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness."xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/volume | "16"xsd:string |
| http://purl.uniprot.org/citations/16000375 | http://purl.uniprot.org/core/volume | "16"xsd:string |