Src and FAK kinases cooperate to phosphorylate paxillin kinase linker, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness.

@article{Brown2005SrcAF,
  title={Src and FAK kinases cooperate to phosphorylate paxillin kinase linker, stimulate its focal adhesion localization, and regulate cell spreading and protrusiveness.},
  author={Michael C. Brown and Leslie A. Cary and Jennifer S Jamieson and Jonathan A Cooper and C. Heath Turner},
  journal={Molecular biology of the cell},
  year={2005},
  volume={16 9},
  pages={
          4316-28
        }
}
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… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 72 extracted citations

Nck adapter proteins: functional versatility in T cells

Cell Communication and Signaling • 2008
View 5 Excerpts
Highly Influenced

Roles of P21-activated kinases and associated proteins in epithelial wound healing.

International review of cell and molecular biology • 2008
View 4 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…