Oncogenic mutations reduce the stability of Src kinase

Journal of Molecular Biology

Volumn 344, Issue 1, 2004, Pages 281-291

  Fabio Falsone, S ^a   Leptihn, Sebastian ^a   Osterauer, Anja ^a   Haslbeck, Martin ^a   Buchner, Johannes ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

chaperone; kinases; protein stability; regulation; signal transduction

Indexed keywords

PROTEIN TYROSINE KINASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; GENE DELETION; GENE MUTATION; HYDROPHOBICITY; IN VITRO STUDY; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; SIGNAL TRANSDUCTION; TEMPERATURE DEPENDENCE; VIRUS STRAIN;

EID: 7044227709     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.08.091     Document Type: Article

References (41)

1. M. Brown, and J.A. Cooper Regulation, substrates and function of src Biochem. Biophys. Res. Commun. 1287 1996 121 149
2. S. Nada, M. Okada, A. MacAuley, J.A. Cooper, and H. Nakagawa Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src Nature 351 1991 69 72
3. X. Liu, S.R. Brodeur, G. Gish, Z. Songyang, L.C. Cantley, A.P. Laudano, and T. Pawson Regulation of c-Src tyrosine kinase activity by the Src SH2 domain Oncogene 8 1993 1119 1126
4. J.E. Thomas, P. Soriano, and J.S. Brugge Phosphorylation of c-Src on tyrosine 527 by another protein tyrosine kinase Science 254 1991 568 571
5. A.K. Somani, J.S. Bignon, G.B. Mills, K.A. Siminovitch, and D.R. Branch Src kinase activity is regulated by the SHP-1 protein-tyrosine phosphatase J. Biol. Chem. 272 1997 21113 21129
6. A.O. Walter, Z.Y. Peng, and C.A. Cartwright The Shp-2 tyrosine phosphatase activates the Src tyrosine kinase by a non-enzymatic mechanism Oncogene 18 1999 1911 1920
7. J.D. Bjorge, A. Pang, and D.J. Fujita Identification of protein-tyrosine phosphatase 1B as the major tyrosine phosphatase activity capable of dephosphorylating and activating c-Src in several human breast cancer cell lines J. Biol. Chem. 275 2000 41439 41446
8. A.D. Levinson, H. Oppermann, L. Levintow, H.E. Varmus, and J.M. Bishop Evidence that the transforming gene of avian sarcoma virus encodes a protein kinase associated with a phosphoprotein Cell 15 1978 561 572
9. W. Xu, S.C. Harrison, and M.J. Eck Three-dimensional structure of the tyrosine kinase c-Src Nature 385 1997 595 602
10. J.C. Williams, A. Weijland, S. Gonfloni, A. Thompson, S.A. Courtneidge, G. Superti-Furga, and R.K. Wierenga The 2.35 Å crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions J. Mol. Biol. 274 1997 757 775
11. J.A. Cooper, K.L. Gould, C.A. Cartwright, and T. Hunter Tyr527 is phosphorylated in pp60c-src: implications for regulation Science 231 1986 1431 1434
12. M.A. Young, S. Gonfloni, G. Superti-Furga, B. Roux, and J. Kuriyan Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation Cell 105 2001 115 126
13. S. Gonfloni, A. Weijland, J. Kretzschmar, and G. Superti-Furga Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src Nature Struct. Biol. 7 2000 281 286
14. J. Brabek, D. Mojzita, M. Novotny, F. Puta, and P. Folk The SH3 domain of Src can downregulate its kinase activity in the absence of the SH2 domain-pY527 interaction Biochem. Biophys. Res. Commun. 296 2002 664 670
15. I. Moarefi, M. LaFevre-Bernt, F. Sicheri, M. Huse, C.H. Lee, J. Kuriyan, and W.T. Miller Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement Nature 385 1997 650 653
16. G. Sun, A.K. Sharma, and R.J. Budde Autophosphorylation of Src and Yes blocks their inactivation by Csk phosphorylation Oncogene 17 1998 1587 1595
17. W. Xu, A. Doshi, M. Lei, M.J. Eck, and S.C. Harrison Crystal structures of c-Src reveal features of its autoinhibitory mechanism Mol. Cell 3 1999 629 638
18. A.B. Reynolds, J. Vila, T.J. Lansing, W.M. Potts, M.J. Weber, and J.T. Parsons Activation of the oncogenic potential of the avian cellular src protein by specific structural alteration of the carboxy terminus EMBO J. 6 1987 2359 2364
19. T. Takeya, and H. Hanafusa Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus Cell 32 1983 881 890
20. R. Jove, T. Hanafusa, M. Hamaguchi, and H. Hanafusa In vivo phosphorylation states and kinase activities of transforming p60c-src mutants Oncogene Res. 5 1989 49 60
21. K. Miyazaki, T. Senga, S. Matsuda, M. Tanaka, K. Machida, and Y. Takenouchi Critical amino acid substitutions in the Src SH3 domain that convert c-Src to be oncogenic Biochem. Biophys. Res. Commun. 263 1999 759 764
22. J. Buchner Hsp90 & Co. - a holding for folding Trends Biochem. Sci. 24 1999 136 141
23. M. MacLean, and D. Picard Cdc37 goes beyond Hsp90 and kinases Cell Stress Chaperones 8 2003 114 119
24. H. Oppermann, W. Levinson, and J.M. Bishop A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein Proc. Natl Acad. Sci. USA 78 1981 1067 1071
25. Y. Xu, and S. Lindquist Heat-shock protein hsp90 governs the activity of pp60v-src kinase Proc. Natl Acad. Sci. USA 90 1993 7074 7078
26. H. Iba, T. Takeya, F.R. Cross, T. Hanafusa, and H. Hanafusa Rous sarcoma virus variants that carry the cellular src gene instead of the viral src gene cannot transform chicken embryo fibroblasts Proc. Natl Acad. Sci. USA 81 1984 4424 4428
27. L. Whitesell, E.G. Mimnaugh, B. De Costa, C.E. Myers, and L.M. Neckers Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation Proc. Natl Acad. Sci. USA 91 1994 8324 8328
28. Y. Xu, M.A. Singer, and S. Lindquist Maturation of the tyrosine kinase c-src as a kinase and as a substrate depends on the molecular chaperone Hsp90 Proc. Natl Acad. Sci. USA 96 1999 109 114
29. D.R. Stover, J. Liebetanz, and N.B. Lydon Cdc2-mediated modulation of pp60c-src activity J. Biol. Chem. 269 1994 26885 26889
30. R. Karni, S. Mizrachi, E. Reiss-Sklan, A. Gazit, O. Livnah, and A. Levitzki The pp60c-Src inhibitor PP1 is non-competitive against ATP FEBS Letters 537 2003 47 52
31. D. Feder, and J.M. Bishop Purification and enzymatic characterization of pp60c-src from human platelets J. Biol. Chem. 265 1990 8205 8211
32. G.V. Semisotnov, N.A. Rodionova, O.I. Razgulyaev, V.N. Uversky, A.F. Gripas, and R.I. Gilmanshin Study of the "molten globule" intermediate nstate in protein folding by a hydrophobic fluorescent probe Biopolymers 31 1991 119 128
33. J.R. Lakowicz J.R. Lakowicz Principles in Fluorescence Spectroscopy 1999 Plenum Press New York 724
34. S. Reddy, D. Mazzu, D. Mahan, and D. Shalloway Sequence and functional differences between Schmidt-Ruppin D and Schmidt-Ruppin A strains of pp60v-src J. Virol. 64 1990 3545 3550
35. N. Sreerama, S.Y. Venyaminov, and R.W. Woody Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis Anal. Biochem. 287 2000 243 251
36. R.A. Sayle, and E.J. Milner-White RASMOL: biomolecular graphics for all Trends Biochem. Sci. 20 1995 374
37. J. Garnier, J.F. Gibrat, and B. Robson GOR method for predicting protein secondary structure from amino acid sequence Methods Enzymol. 266 1996 540 553
38. C.N. Pace, and J.M. Scholz Measuring the conformational stability of a protein Creighton Protein Structure, a Practical Approach 1997 Oxford University Press Oxford 299
39. C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280
40. M. Eftink Fluorescence methods for studying equilibrium macromolecule-ligand interactions Methods Enzymol. 278 1997 221 257
41. D. Higgins, J. Thompson, T. Gibson, J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucl. Acids Res. 22 1994 4673 4680