The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src

EMBO Journal

Volumn 16, Issue 24, 1997, Pages 7261-7271

  Gonfloni, Stefania ^a   Williams, John C ^a,b   Hattula, Katarina ^a,c   Weijland, Albert ^a,d   Wierenga, Rik K ^a   Superti Furga, Giulio ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b Columbia University ^*  (United States)

^c UNIVERSITY OF HELSINKI   (Finland)

^d CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

LINK PROTEIN; MUTANT PROTEIN; PROTEIN KINASE P60; PROTEIN TYROSINE KINASE;

ANIMAL CELL; ARTICLE; CELL TRANSFORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STRUCTURE; FIBROBLAST; MAMMAL CELL; MOUSE; NONHUMAN; ONCOGENE SRC; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION;

3T3 CELLS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CHICKENS; CLONING, MOLECULAR; KINETICS; LYMPHOCYTE SPECIFIC PROTEIN TYROSINE KINASE P56(LCK); MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PHOSPHORYLATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-HCK; RECOMBINANT PROTEINS; SCHIZOSACCHAROMYCES; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SRC HOMOLOGY DOMAINS; SRC-FAMILY KINASES; TRANSFECTION;

EID: 0031464009     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.24.7261     Document Type: Article

References (47)

1. Abagyan, R., Totrov, M. and Kuznetsov, D. (1994) ICM - a new method for protein modelling and design: application to docking and structure prediction from the distorted native conformation. J. Comput. Chem., 15, 488-506.
2. Cas-related protein, Sin. Genes Dev., 10, 1341-1355.
3. Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. (1987) Current Protocols in Molecular Biology. John Wiley and Sons, New York.
4. Beach, D., Rodgers, L. and Gould, J. (1985) ran1+ controls the transition from mitotic division to meiosis in fission yeast. Curr. Genet., 10, 297-311.
5. Briggs, S.D., Sharkey, M., Stevenson, M. and Smithgall, T.E. (1997) SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1. J. Biol. Chem., 272, 17899-17902.
6. Broome, M.A. and Hunter, T. (1996) Requirement for c-Src catalytic activity and the SH3 domain in platelet-derived growth factor BB and epidermal growth factor mitogenic signaling. J. Biol. Chem., 271, 16798-16806.
7. Brown, M.T. and Cooper, J.A. (1996) Regulation, substrates and functions of src. Biochim. Biophys. Acta, 1287, 121-149.
8. Cohen, G.B., Ren, R. and Baltimore, D. (1995) Modular binding domains in signal transduction proteins. Cell, 80, 237-248.
9. De Bondt, H.L., Rosenblatt, J., Jancarik, J., Jones, H.D., Morgan, D.O. and Kim, S.-H. (1993) Crystal structure of cyclin-dependent kinase 2. Nature, 363, 595-602.
10. Erpel, T., Superti-Furga, G. and Courtneidge, S.A. (1995) Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra-and inter-molecular interactions. EMBO J., 14, 963-975.
11. Erpel, T., Alonso, G., Roche, S. and Courtneidge, S.A. (1996) The Src SH3 domain is required for DNA synthesis induced by platelet-derived growth factor and epidermal frowth factor. J. Biol. Chem., 271, 16807-16812.
12. Green, S., Issemann, I. and Sheer, E. (1988) A versatile in vitro and in vivo eukaryotic expression vector for protein engineering. Nucleic Acids Res., 16, 369-370.
13. Hubbard, S.R., Wei, L., Ellis, L. and Hendrickson, W.A. (1994) Crystal structure of the tyrosine kinase domain of the insulin receptor. Nature, 372, 746-754.
14. Hunter, T. (1987) A tail of two src's: mutatis mutandis. Cell, 49, 1-4.
15. Jeffrey, P.D., Russo, A.A., Polyak, K., Gibbs, E., Hurwitz, J., Massagué, J. and Pavletich, N.P. (1995) Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature, 376, 313-320.
16. Johnson, L.N., Noble, M.E.M. and Owen, D.J. (1996) Active and inactive protein kinases: structural basis for regulation. Cell, 85, 149-158.
17. Jove, R. and Hanafusa, H. (1987) Cell transformation by the viral src oncogene. Annu. Rev. Cell. Biol., 3, 31-56.
18. Koegl, M., Courtneidge, S.A. and Superti-Furga, G. (1995) Structural requirements for the efficient regulation of the Src protein tyrosine kinase by Csk. Oncogene, 11, 2317-2329.
19. Kypta, R.M., Goldberg, Y., Ulug, E.T., Courtneidge, S.A. (1990) Association between the PDGF receptor and members of the Src family of tyrosine kinases. Cell, 62, 481-492.
20. src expression: localization of v-src to adhesion plaques is sufficient to transform chicken embryo fibroblasts. Oncogene, 7, 2417-2428.
21. Liu, X., Brodeur, S.R., Gish, G., Songyang, Z., Cantley, L.C., Laudano, A.P. and Pawson, T. (1993) Regulation of c-Src tyrosine kinase activity by the Src SH2 domain. Oncogene, 8, 1119-1126.
22. Lowell, C.A. and Soriano, P. (1996) Knockouts of Src-family kinases: stiff bones, wimpy T cells, and bad memories. Genes Dev., 10, 1845-1857.
23. Martin-Zanca, D., Oskam, R., Mitra, G., Copeland, T. and Barbacid, M. (1984) Molecular and biochemical characterization of the human trk proto-oncogene. Mol. Cell. Biol., 9, 24-33.
24. gag-crk, to a broad range of phosphotyrosine-containing proteins. Science, 248, 1537-1539.
25. Mayer, B.J. (1997) Clamping down on Src activity. Curr. Biol., 7, R295-R298.
26. Moarefi, I., LaFevre-Bernt, M., Sicheri, E. Huse, M., Lee, C.-H., Kuriyan, J. and Miller, W.T. (1997) Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature, 385, 650-653.
27. Murphy, S.M., Bergman, M. and Morgan, D.O. (1993) 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, 5290-5300.
28. Nguyen, J.T. and Lim, W.A. (1997) How Src exercises self-restraint. Nature Struct. Biol., 4, 256-260.
29. Okada, M. Howell, B., Broome, M.A. and Cooper, J.A. (1993) Deletion of the SH3 domain of SRC interferes with regulation by the phosphorylated carboxy terminal tyrosine. J. Biol. Chem., 268, 18070-18075.
30. Parsons, J.T. and Weber, M.J. (1989) Genetics of src: structure and functional organization of a protein tyrosine kinase. Curr. Top. Microbiol. Immunol., 147, 79-127.
31. Pawson, T. (1995) Protein modules and signalling networks. Nature, 373, 573-580.
32. Pawson, T. (1997) New impressions of Src and Hck. Nature, 385, 582-585.
33. Seidel-Dugan, C., Meyer, B., Thomas, S. and Brugge, J. (1992) Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src. Mol. Cell. Biol. 12, 1835-1845.
34. Shalloway, D. and Taylor, S.J. (1997) Src: more than the sum of its parts. Trends Cell Biol., 7, 215-217.
35. Sicheri, F., Moarefi, I. and Kuriyan, J. (1997) Crystal structure of the Src family tyrosine kinase Hck. Nature, 385, 602-609.
36. Sudol, M., Kieswetter, C., Zhao, Y.-H., Dorai, T., Wang, L.-H. and Hanafusa, H. (1988) Nucleotide sequence of a cDNA for the chick yes proto-oncogene: comparison with the viral yes gene. Nucleic Acids Res., 16, 9876.
37. Superti-Furga, G. and Courtneidge, S.A. (1995) Structure-function relationships in Src family and related protein tyrosine kinases. BioEssays, 17, 321-330.
38. Superti-Furga, G. and Gonfloni, S. (1997) A crystal milestone: the structure of regulated Src. BioEssays, 19, 1-4.
39. Superti-Furga, G., Fumagalli, S., Koegl, M., Courtneidge, S.A. and Draetta, G. (1993) Csk inhibition of Src activity requires both the SH2 and SH3 domains of Src. EMBO J., 12, 2625-2634.
40. Superti-Furga, G., Jönsson, K. and Courtneidge, S.A. (1996) A functional screen in yeast for regulators and antagonizers of heterologous protein tyrosine kinases. Nature Biotechnol., 14, 600-605.
41. Tanaka, M., Gupta, R. and Mayer, B.J. (1995) Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adaptor proteins. Mol. Cell. Biol., 15, 6829-6837.
42. Taylor, S.S., Knighton, D.R., Zheng, J., Sowadski, M., Gibbs, C.S. and Zoller, M.J. (1993) A template for the protein kinase family. Trends Biochem. Sci., 18, 84-89.
43. Varmus, H. and Weinberg, R.A. (1993) Genes and the Biology of Cancer. Scientific American Library, New York.
44. Weijland, A., Williams, J.C., Neubauer, G., Courtneidge, S.A., Wierenga, R.K. and Superti-Furga, G. (1997) Src regulated by C-terminal phosphorylation is monomeric. Proc. Natl Acad. Sci. USA, 94, 3590-3595.
45. Williams, J.C., Weijland, A., Gonfloni, S., Thompson, A., Courtneidge, S.A., Superti-Furga, G. and Wierenga, R.K. (1997) The 2.35Å crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions. J. Mol. Biol., in press.
46. Xu, W., Harrison, S.C. and Eck, M.J. (1997) Three-dimensional structure of the tyrosine kinase c-Src. Nature, 385, 595-602.
47. Yamaguchi, H. and Hendrickson, W.A. (1996) Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature, 384, 484-189.