Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases (original) (raw)

References

1. Nada,S., Okada,M., MacAuley,A., Cooper,J. A. & Nakagawa, H. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature 351, 69– 72 (1991).
   Article ADS CAS Google Scholar
2. Nada,S. et al. Constitutive activation of Src family kinases in mouse embryos that lack Csk. Cell 73, 1125– 1135 (1993).
   Article CAS Google Scholar
3. Brown,M. T. & Cooper,J. A. Regulation, substrates and function of src. Biochem. Biophys. Acta 1287, 121 –149 (1996).
   PubMed Google Scholar
4. Simons,K. & Ikonen,E. Functional rafts in cell membranes. Nature 387, 569–572 (1997).
   Article ADS CAS Google Scholar
5. Brown,D. A. & London,E. Functions of lipid rafts in biological membranes. Annu. Rev. Cell. Dev. Biol. 14, 111–136 (1998).
   Article CAS Google Scholar
6. Anderson,R. G. The caveolae membrane system. Annu. Rev. Biochem. 67 , 199–225 (1998).
   Article CAS Google Scholar
7. Xavier,R., Brennan,T., Li,Q., McCormack,C. & Seed,B. Membrane compartmentation is required for efficient T cell activation. Immunity 8, 723– 732 (1998).
   Article CAS Google Scholar
8. Montixi,C. et al. Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains. EMBO J. 17, 5334–5348 (1998).
   Article CAS Google Scholar
9. Howell,B. W. & Cooper,J. A. Csk suppression of Src involves movement of Csk to sites of Src activity. Mol. Cell. Biol. 14, 5402–5411 (1994).
   Article CAS Google Scholar
10. Sabe,H., Hata,A., Okada,M., Nakagawa,H. & Hanafusa, H. Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src. Proc. Natl Acad. Sci. USA 91, 3984–3988 (1994).
    Article ADS CAS Google Scholar
11. Cloutier,J. F., Chow,L. M. & Veillette, A. Requirement of the SH3 and SH2 domains for the inhibitory function of tyrosine protein kinase p50csk in T lymphocytes. Mol. Cell. Biol. 15, 5937– 5944 (1995).
    Article CAS Google Scholar
12. Zhang,W., Sloan-Lancaster,J., Kitchen, J., Trible,R. P. & Samelson,L. E. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 9, 83–92 (1998 ).
    Article CAS Google Scholar
13. Zhang,W., Trible,R. P. & Samelson, L. E. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 9, 239–246 (1998).
    Article CAS Google Scholar
14. Hanke,J. H. et al. Discovery of a novel, potent and Src family selective protein tyrosine kinase inhibitor. J. Biol. Chem. 271, 695–701 (1996).
    Article CAS Google Scholar
15. Nada,S., Okada,M., Aizawa,S. & Nakagawa,H. Identification of major tyrosine-phosphorylated proteins in Csk-deficient cells. Oncogene 9, 3571–3578 ( 1994).
    CAS PubMed Google Scholar
16. Tsuda,M. et al. Integrin-mediated tyrosine phosphorylation of SHPS-1 and its association with SHP-2. Roles of Fak and Src family kinases. J. Biol. Chem. 273, 13223–13229 (1998).
    Article CAS Google Scholar
17. Harder,K. W., Moller,N. P., Peacock,J. W. & Jirik,F. R. Protein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesion. J. Biol. Chem. 273, 31890–31900 (1998).
    Article CAS Google Scholar
18. Hakak,Y. & Martin,G. S. Ubiquitin-dependent degradation of active Src. Curr. Biol. 9, 1039– 1042 (1999).
    Article CAS Google Scholar
19. Kobayashi. S., Okumura,N., Okada,M. & Nagai,K. Depolarization-induced tyrosine phosphorylation of p130cas. J. Biochem. (Tokyo) 123, 624–629 ( 1998).
    Article Google Scholar
20. Jensen,O. N., Wilm,M., Shevchenko,A. & Mann,M. in Methods in Molecular Biology Vol. 112 (ed. Link, A. J.) 513– 530 (Humana, Totowa, 1999).
    Google Scholar
21. Harlow,E. & Lane,D. in Antibodies, a Laboratory Manual 359–420 (Cold Spring Harbor Laboratory, 1988).
    Google Scholar

Download references