Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk

Experimental Cell Research

Volumn 288, Issue 1, 2003, Pages 110-118

  Lennartsson, Johan ^a,b   Wernstedt, Christer ^a   Engström, Ulla ^a   Hellman, Ulf ^a   Rönnstrand, Lars ^a,c  

^a UPPSALA UNIVERSITY   (Sweden)

^b NATIONAL CANCER INSTITUTE   (United States)

^c LUND UNIVERSITY   (Sweden)

Author keywords

c Kit; Crk; Phosphorylation; PI3 kinase; SH2 domain; Src family kinases

Indexed keywords

ADAPTOR PROTEIN; AMINO ACID; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOPEPTIDE; PROTEIN CRK 2; PROTEIN TYROSINE KINASE; STEM CELL FACTOR; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SRC HOMOLOGY DOMAIN;

EID: 0038825595     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-4827(03)00206-4     Document Type: Article

References (25)

1. Lev S., Blechman J.M., Givol D., Yarden Y. Steel factor and c-kit protooncogene genetic lessons in signal transduction . Crit. Rev. Oncogene. 5:1994;141-168.
2. Galli S.J., Zsebo K.M., Geissler E.N. The kit ligand, stem cell factor. Adv. Immunol. 55:1994;1-96.
3. Linnekin D., DeBerry C.S., Mou S. Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells. J. Biol. Chem. 272:1997;27450-27455.
4. Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H. Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes. J. Biol. Chem. 272:1997;5915-5920.
5. Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R., Siminovitch K.A. SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain. Mol. Cell. Biol. 18:1998;2089-2099.
6. Lennartsson J., Blume-Jensen P., Hermanson M., Pontén E., Carlberg M., Rönnstrand L. Phosphorylation of Shc by Src family kinases is necessary for stem cell factor receptor/c-kit mediated activation of the Ras/MAP kinase pathway and c-fos induction. Oncogene. 18:1999;5546-5553.
7. Serve H., Hsu Y.C., Besmer P. Tyrosine residue 719 of the c-kit receptor is essential for binding of the P85 subunit of phosphatidylinositol (PI) 3-kinase and for c-kit-associated PI 3-kinase activity in COS-1 cells. J. Biol. Chem. 269:1994;6026-6030.
8. Thömmes K., Lennartsson J., Carlberg M., Rönnstrand L. Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor. Biochem. J. 341:1999;211-216.
9. Blume-Jensen P., Rönnstrand L., Gout I., Waterfield M.D., Heldin C.H. Modulation of Kit/stem cell factor receptor-induced signaling by protein kinase C. J. Biol. Chem. 269:1994;21793-21802.
10. Countaway J.L., Nairn A.C., Davis R.J. Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase. J. Biol. Chem. 267:1992;1129-1140.
11. Gandino L., Longati P., Medico E., Prat M., Comoglio P.M. Phosphorylation of serine 985 negatively regulates the hepatocyte growth factor receptor kinase. J. Biol. Chem. 269:1994;1815-1820.
12. Blume-Jensen P., Wernstedt C., Heldin C.H., Rönnstrand L. Identification of the major phosphorylation sites for protein kinase C in kit/stem cell factor receptor in vitro and in intact cells. J. Biol. Chem. 270:1995;14192-14200.
13. Biscardi J.S., Maa M.C., Tice D.A., Cox M.E., Leu T.H., Parsons S.J. c-Src-mediated phosphorylation of the epidermal growth factor receptor on Tyr845 and Tyr1101 is associated with modulation of receptor function. J. Biol. Chem. 274:1999;8335-8343.
14. Hansen K., Johnell M., Siegbahn A., Rorsman C., Engström U., Wernstedt C., Heldin C.H., Rönnstrand L. Mutation of a Src phosphorylation site in the PDGF beta-receptor leads to increased PDGF-stimulated chemotaxis but decreased mitogenesis. EMBO J. 15:1996;5299-5313.
15. Blume-Jensen P., Siegbahn A., Stabel S., Heldin C.H., Rönnstrand L. Increased Kit/SCF receptor induced mitogenicity but abolished cell motility after inhibition of protein kinase C. EMBO J. 12:1993;4199-4209.
16. Blake R.A., Broome M.A., Liu X., Wu J., Gishizky M., Sun L., Courtneidge S.A. SU6656, a selective src family kinase inhibitor, used to probe growth factor signaling. Mol. Cell. Biol. 20:2000;9018-9027.
17. Kiyokawa E., Mochizuki N., Kurata T., Matsuda M. Role of Crk oncogene product in physiologic signaling. Crit. Rev. Oncogene. 8:1997;329-342.
18. Nakashima N., Rose D.W., Xiao S., Egawa K., Martin S.S., Haruta T., Saltiel A.R., Olefsky J.M. The functional role of CrkII in actin cytoskeleton organization and mitogenesis. J. Biol. Chem. 274:1999;3001-3008.
19. Songyang Z., Carraway K.L. III, Eck M.J., Harrison S.C., Feldman R.A., Mohammadi M., Schlessinger J., Hubbard S.R., Smith D.P., Eng C., Lorenzo M.J., Ponder B.A.J., Mayer B.J., Cantley L.C. Catalytic specificity of protein-tyrosine kinases is critical for selective signalling. Nature. 373:1995;536-539.
20. Songyang Z., Shoelson S.E., Chaudhuri M., Gish G., Pawson T., Haser W.G., King F., Roberts T., Ratnofsky S., Lechleider R.J., et al. SH2 domains recognize specific phosphopeptide sequences. Cell. 72:1993;767-778.
21. Ueki K., Fruman D.A., Brachmann S.M., Tseng Y.H., Cantley L.C., Kahn C.R. Molecular balance between the regulatory and catalytic subunits of phosphoinositide 3-kinase regulates cell signaling and survival. Mol. Cell. Biol. 22:2002;965-977.
22. Sattler M., Salgia R., Shrikhande G., Verma S., Pisick E., Prasad K.V., Griffin J.D. Steel factor induces tyrosine phosphorylation of CRKL and binding of CRKL to a complex containing c-kit, phosphatidylinositol 3-kinase, and p120(CBL). J. Biol. Chem. 272:1997;10248-10253.
23. Rosen M.K., Yamazaki T., Gish G.D., Kay C.M., Pawson T., Kay L.E. Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein. Nature. 374:1995;477-479.
24. Matsumoto T., Yokote K., Take A., Takemoto M., Asaumi S., Hashimoto Y., Matsuda M., Saito Y., Mori S. Differential interaction of CrkII adaptor protein with platelet-derived growth factor alpha- and beta-receptors is determined by its internal tyrosine phosphorylation. Biochem. Biophys. Res. Commun. 270:2000;28-33.
25. Rönnstrand L., Siegbahn A., Rorsman C., Johnell M., Hansen K., Heldin C.H. Overactivation of phospholipase C-gamma1 renders platelet-derived growth factor beta-receptor-expressing cells independent of the phosphatidylinositol 3-kinase pathway for chemotaxis. J. Biol. Chem. 274:1999;22089-22094.