Involvement of the SH3 domain in Ca2+-mediated regulation of Src family kinases

Biochimie

Volumn 88, Issue 7, 2006, Pages 905-911

  Monteiro, A N A ^a  

^a H LEE MOFFITT CANCER CENTER AND RESEARCH INSTITUTE   (United States)

Author keywords

c Src; c Yes; Calcium; MDCK cells; SH3 domain; Tyrosine kinases

Indexed keywords

CALCIUM ION; PROTEIN SH3; PROTEIN TYROSINE KINASE; CALCIUM; HYBRID PROTEIN; PROTEIN KINASE YES;

ANIMAL CELL; ARTICLE; CELL LINE; CELL LYSATE; CHIMERA; ENZYME ACTIVITY; HUMAN; IN VITRO STUDY; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; REGULATORY MECHANISM; SRC HOMOLOGY DOMAIN; ANIMAL; CELL CULTURE; CHEMISTRY; DRUG EFFECT; ENZYME ACTIVATION; GENETIC TRANSFECTION; GENETICS; IMMUNOPRECIPITATION; METABOLISM; RAT;

ANIMALS; CALCIUM; CELL LINE; CELLS, CULTURED; ENZYME ACTIVATION; IMMUNOPRECIPITATION; PROTO-ONCOGENE PROTEINS C-YES; RATS; RECOMBINANT FUSION PROTEINS; SRC HOMOLOGY DOMAINS; SRC-FAMILY KINASES; TRANSFECTION;

EID: 33746725940     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2006.01.013     Document Type: Article

References (45)

1. Jove R., and Hanafusa H. Cell transformation by the viral src oncogene. Annu. Rev. Cell Biol. 3 (1987) 31-56
2. Zhao Y., Uyttendaele H., Krueger J.G., Sudol M., and Hanafusa H. Inactivation of c-Yes tyrosine kinase by elevation of intracellular calcium levels. Mol. Cell. Biol. 13 (1993) 7507-7514
3. Zhao Y., Sudol M., Hanafusa H., and Krueger J. Increased tyrosine kinase activity of c-Src during calcium-induced keratinocyte differentiation. Proc. Natl. Acad. Sci. USA 89 (1992) 8298-8302
4. Bouchard M.J., Wang L.H., and Schneider R.J. Calcium signaling by HBx protein in hepatitis B virus DNA replication. Science 294 (2001) 2376-2378
5. Rusanescu G., Qi H., Thomas S.M., Brugge J.S., and Halegoua S. Calcium influx induces neurite growth through a Src-Ras signaling cassette. Neuron 15 (1995) 1415-1425
6. Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., Plowman G.D., Rudy B., and Schlessinger J. Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions. Nature 376 (1995) 737-745
7. Summy J.M., Sudol M., Eck M.J., Monteiro A.N., Gatesman A., and Flynn D.C. Specificity in signaling by c-Yes. Front. Biosci. 8 (2003) s185-s205
8. Tsygankov A.Y. Non-receptor protein tyrosine kinases. Front. Biosci. 8 (2003) s595-s635
9. Park J., and Cartwright C.A. Src activity increases and Yes activity decreases during mitosis of human colon carcinoma cells. Mol. Cell. Biol. 15 (1995) 2374-2382
10. Levy J.B., Iba H., and Hanafusa H. Activation of the transforming potential of p60c-Src by a single amino acid change. Proc. Natl. Acad. Sci. USA 83 (1986) 4228-4232
11. Sudol M., Kieswetter C., Zhao Y.H., Dorai T., Wang L.H., and Hanafusa H. Nucleotide sequence of a cDNA for the chick yes proto-oncogene: comparison with the viral yes gene. Nucleic Acids Res. 16 (1988) 9876
12. Higuchi R., and Recombinant P.C.R. In: Innis M.A., Gelfand D.H., Sininski J.J., and White T.J. (Eds). PCR Protocols: A Guide to Methods and Applications (1990), Academic Press, San Diego 177-183
13. Zhao Y.H., Krueger J.G., and Sudol M. Expression of cellular-yes protein in mammalian tissues. Oncogene 5 (1990) 1629-1635
14. Lipsich L.A., Lewis A.J., and Brugge J.S. Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. J. Virol. 48 (1983) 352-360
15. Bourassa C., Chapdelaine A., Roberts K.D., and Chevalier S. Enhancement of the detection of alkali-resistant phosphoproteins in polyacrylamide gels. Anal. Biochem. 169 (1988) 356-362
16. Iba H., Cross F.R., Garber E.A., and Hanafusa H. Low level of cellular protein phosphorylation by nontransforming overproduced p60c-src. Mol. Cell. Biol. 5 (1985) 1058-1066
17. Warren S.L., Handel L.M., and Nelson W.J. Elevated expression of pp60c-src alters a selective morphogenetic property of epithelial cells in vitro without a mitogenic effect. Mol. Cell. Biol. 8 (1988) 632-646
18. Warren S.L., and Nelson W.J. Nonmitogenic morphoregulatory action of pp60v-src on multicellular epithelial structures. Mol. Cell. Biol. 7 (1987) 1326-1337
19. 3 binding site. Science 259 (1993) 1157-1161
20. Boggon T.J., and Eck M.J. Structure and regulation of Src family kinases. Oncogene 23 (2004) 7918-7927
21. 3 domains. Mol. Cell. Biol. 14 (1994) 4509-4521
22. 3 domains specifically regulate kinase activity of expressed Src family proteins. J. Biol. Chem. 270 (1995) 333-339
23. Stein P.L., Vogel H., and Soriano P. Combined deficiencies of Src, Fyn, and Yes tyrosine kinases in mutant mice. Genes Dev. 8 (1994) 1999-2007
24. 2 domains are capable of directing specificity in protein interactions between the non-receptor tyrosine kinases cSrc and cYes. Oncogene 19 (2000) 155-160
25. Sparks A.B., Rider J.E., Hoffman N.G., Fowlkes D.M., Quilliam L.A., and Kay B.K. Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLCgamma, Crk, and Grb2. Proc. Natl. Acad. Sci. USA 93 (1996) 1540-1544
26. Rickles R.J., Botfield M.C., Zhou X., Henry P.A., and Brugge J.S. Phage display selection of ligand residues important for Src homology 3 domain binding specificity. Proc. Natl. Acad. Sci. USA 92 (1995) 10909-10913
27. Soriano P., Montgomery C., Geske R., and Bradley A. Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice. Cell 64 (1991) 693-702
28. Boyce B.F., Yoneda T., Lowe C., Soriano P., and Mundy G.R. Requirement of pp60c-src expression for osteoclasts to form ruffled borders and resorb bone in mice. J. Clin. Invest. 90 (1992) 1622-1627
29. Kaplan K.B., Swedlow J.R., Morgan D.O., and Varmus H.E. c-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism. Genes Dev. 9 (1995) 1505-1517
30. Tsukita S., Oishi K., Akiyama T., Yamanashi Y., Yamamoto T., and Tsukita S. Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated. J. Cell Biol. 113 (1991) 867-879
31. Nusrat A., Chen J.A., Foley C.S., Liang T.W., Tom J., Cromwell M., Quan C., and Mrsny R.J. The coiled-coil domain of occludin can act to organize structural and functional elements of the epithelial tight junction. J. Biol. Chem. 275 (2000) 29816-29822
32. Chen Y.H., Lu Q., Goodenough D.A., and Jeansonne B. Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells. Mol. Biol. Cell 13 (2002) 1227-1237
33. 3 deletions on the functional activities of wild-type and transforming variants of c-Src. Mol. Cell. Biol. 12 (1992) 1835-1845
34. 3 domain of Src interferes with regulation by the phosphorylated carboxyl-terminal tyrosine. J. Biol. Chem. 268 (1993) 18070-18075
35. 3 domains: analysis with Saccharomyces cerevisiae. Mol. Cell. Biol. 13 (1993) 5290-5300
36. 3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions. EMBO J. 14 (1995) 963-975
37. 3 domains of Src. EMBO J. 12 (1993) 2625-2634
38. Xu W., Doshi A., Lei M., Eck M.J., and Harrison S.C. Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol. Cell 3 (1999) 629-638
39. Xu W., Harrison S.C., and Eck M.J. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385 (1997) 595-602
40. Harrison S.C. Variation on an Src-like theme. Cell 112 (2003) 737-740
41. Williams J.C., Weijland A., Gonfloni S., Thompson A., Courtneidge S.A., Superti-Furga G., and Wierenga R.K. 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
42. Sicheri F., Moarefi I., and Kuriyan J. Crystal structure of the Src family tyrosine kinase Hck. Nature 385 (1997) 602-609
43. Matsuda M., Mayer B.J., Fukui Y., and Hanafusa H. Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. Science 248 (1990) 1537-1539
44. Pawson T. New impressions of Src and Hck. Nature 385 585 (1997) 582-583
45. 3 domain displacement. Nature 385 (1997) 650-653