Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases

Nature

Volumn 404, Issue 6781, 2000, Pages 999-1003

  Kawabuchi, Masahiro ^a   Satomi, Yoshinori ^a   Takao, Toshifumi ^a   Shimonishi, Yasutsugu ^a   Nada, Shigeyuki ^a   Nagal, Katsuya ^a   Tarakhovsky, Alexander ^b   Okada, Masato ^a  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF COLOGNE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PHOSPHOPROTEIN; PROTEIN TYROSINE KINASE;

ANIMAL CELL; ARTICLE; CELL DIFFERENTIATION; CELL GROWTH; ENZYME ACTIVITY; ENZYME BINDING; ENZYME REGULATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; RAT; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; ANIMALS; BRAIN; CELL MEMBRANE; CLONING, MOLECULAR; COS CELLS; DNA, COMPLEMENTARY; ENZYME ACTIVATION; ENZYME ACTIVATORS; ESCHERICHIA COLI; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEINS; PHOSPHORYLATION; RATS; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION; SRC HOMOLOGY DOMAINS; SRC-FAMILY KINASES; TISSUE DISTRIBUTION;

EID: 0034720166     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35010121     Document Type: Article

References (21)

1. c-src. Nature 351, 69-72 (1991).
2. Nada, S. et al. Constitutive activation of Src family kinases in mouse embryos that lack Csk. Cell 73, 1125-1135 (1993).
3. Brown, M. T. & Cooper, J. A. Regulation, substrates and function of src. Biochem. Biophys. Acta 1287, 121-149 (1996).
4. Simons, K. & Ikonen, E. Functional rafts in cell membranes. Nature 387, 569-572 (1997).
5. Brown, D. A. & London, E. Functions of lipid rafts in biological membranes. Annu. Rev. Cell. Dev. Biol. 14, 111-136 (1998).
6. Anderson, R. G. The caveolae membrane system. Annu. Rev. Biochem. 67, 199-225 (1998).
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).
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).
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).
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).
11. csk in T lymphocytes. Mol. Cell. Biol. 15, 5937-5944 (1995).
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).
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).
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).
15. Nada, S., Okada, M., Aizawa, S. & Nakagawa, H. Identification of major tyrosine-phosphorylated proteins in Csk-deficient cells. Oncogene 9, 3571-3578 (1994).
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).
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).
18. Hakak, Y. & Martin, G. S. Ubiquitin-dependent degradation of active Src. Curr. Biol. 9, 1039-1042 (1999).
19. cas. J. Biochem. (Tokyo) 123, 624-629 (1998).
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).
21. Harlow, E. & Lane, D. in Antibodies, a Laboratory Manual 359-420 (Cold Spring Harbor Laboratory, 1988).