Csk-mediated phosphorylation of substrates is regulated by substrate tyrosine phosphorylation

Farmaco

Volumn 53, Issue 4, 1998, Pages 266-272

  Amrein, Kurt E ^a   Molnos, Juliette ^a   Zur Hausen, Jan Dirk ^a   Flint, Nicholas ^a   Takacs, Belá ^a   Burn, Paul ^a  

^a Hoffman La Roche Department of Metabolic Diseases   (United States)

Author keywords

Cellular signalling; Lck; Overlay kinase assay; Src; Tyrosine kinase

Indexed keywords

CELL PROTEIN; PROTEIN TYROSINE KINASE;

ANIMAL CELL; AUTOPHOSPHORYLATION; CELL STRAIN 3T3; CHEMOLUMINESCENCE; CONFERENCE PAPER; CONTROLLED STUDY; ENZYME SPECIFICITY; FIBROBLAST CULTURE; IMMUNOBLOTTING; MOUSE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN PHOSPHORYLATION; SIGNAL DETECTION;

3T3 CELLS; ANIMALS; LYMPHOCYTE SPECIFIC PROTEIN TYROSINE KINASE P56(LCK); MICE; PHOSPHORYLATION; PROTEIN-TYROSINE KINASES; SRC HOMOLOGY DOMAINS; TYROSINE;

EID: 0031821224     PISSN: 0014827X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-827X(98)00020-2     Document Type: Conference Paper

References (24)

1. c-src. Nature. 351:1991;69-72.
2. lck at Tyr-505 and down regulates its catalytic activity. EMBO J. 11:1992;2919-2924.
3. Imamoto A., Soriano P. Disruption of the csk gene, encoding a negative regulator of Src family tyrosine kinases, leads to neural tube defects and embryonic lethality in mice. Cell. 73:1993;1117-1124.
4. Nada S., Yagi T., Takeda H., Tokunaga T., Nakagawa H., Ikawa Y., Okada M., Aizawa S. Constitutive activation of Src family kinases in mouse embryos that lack Csk. Cell. 73:1993;1125-1135.
5. csk. Nature. 365:1993;156-160.
6. Okada M., Nada S., Yamanashi Y., Yamamoto T., Nakagawa H. CSK: a protein-tyrosine kinase involved in regulation of src family kinases. J. Biol. Chem. 266:1991;24249-24252.
7. lck tyrosine kinase and activates the phosphatase. Mol. Cell. Biol. 14:1994;1308-1321.
8. lck, reveals its oncogenic potential in fibroblasts. Proc. Natl. Acad. Sci. USA. 85:1988;4247-4251.
9. lck mediates both intermolecular and intramolecular interactions. Proc. Natl. Acad. Sci. USA. 90:1993;10285-10289.
10. Mustelin T., Burn P. Regulation of src family tyrosine kinases in lymphocytes. Trends Biochem. Sci. 18:1993;215-220.
11. Murphy S.M., Bergman M., Morgan D.O. Suppression of c-Src activity by C-terminal Src kinase involves the c-Src SH2 and SH3 domains: analysis with Saccharomyces cerevisiae. Mol. Cell. Biol. 13:1993;5290-5300.
12. Superti Furga G., Fumagalli S., Koegl M., Courtneidge S.A., Draetta G. Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src. EMBO J. 12:1993;2625-2634.
13. Hata A., Sabe H., Kurosaki T., Takata M., Hanafusa H. Functional analysis of Csk in signal transduction through the B cell antigen receptor. Mol. Cell. Biol. 14:1994;7306-7313.
14. Amrein K.E., Takacs B., Molnos J., Stieger M., Flint N.A., Burn P. Purification and characterization of Csk protein tyrosine kinase from an Escherichia coli Gro EL/Gro ES expression system. Proc. Natl. Acad. Sci. USA. 92:1995;1048-1052.
15. Secrist J.P., Burns L.A., Karnitz L., Koretzky G.A., Abraham R.T. Stimulatory effects of the protein tyrosine phosphatase inhibitor, pervanadate, on T cell activation events. J. Biol. Chem. 268:1993;5886-5893.
16. Stüber D., Matile H., Garotta G. System for high-level production in Escherichia coli and rapid purification of recombinant proteins: application to epitope mapping, preparation of antibodies and structure-function analysis. Immunol. Methods. 4:1990;121-152.
17. Caspers P., Stieger M., Burn P. Overproduction of bacterial chaperones improves the solubility of recombinant protein tyrosine kinases in Escherichia coli. Cell. Mol. Biol. 40:1994;635-644.
18. Flint N.A., Amrein K.E., Jascur T., Burn P. Purification and characterization of an activated form of the tyrosine kinase Lck from an Escherichia coli expression system. J. Cell. Biochem. 55:1994;389-397.
19. ras GTPase activity in vitro. Biochem. Biophys. Acta. 1222:1994;441-446.
20. Hunter T., Sefton B.M. The transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc. Natl. Acad. Sci. USA. 77:1980;1311-1315.
21. Shisheva A., Shechter Y. Mechanism of pervanadate stimulation and potentiation of insulin-activated glucose transport in rat adipocytes: dissociation from vanadate effect. Endocrinology. 133:1993;1562-1568.
22. Shaw A.S., Amrein K.E., Hammond C., Stern D.F., Sefton B.M., Rose J.K. The lck tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell. 59:1989;627-636.
23. Songyang Z., Shoelson S.E., McGlade J., Olivier P., Pawson T., Bustelo X.R., Barbacid M., Sabe H., Hanafusa H., Yi T., Ren R., Baltimore D., Ratnofsky S., Feldman R.A., Cantley L.C. Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP. SHC, Syk, and Vav, Mol. Cell. Biol. 14:1994;2777-2785.
24. csk in T lymphocytes. Mol. Cell. Biol. 15:1995;5937-5944.