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. 1998 Aug 3;17(15):4346–4357. doi: 10.1093/emboj/17.15.4346

A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate.

P Lock 1, C L Abram 1, T Gibson 1, S A Courtneidge 1
PMCID: PMC1170768  PMID: 9687503

Abstract

We describe a method for identifying tyrosine kinase substrates using anti-phosphotyrosine antibodies to screen tyrosine-phosphorylated cDNA expression libraries. Several potential Src substrates were identified including Fish, which has five SH3 domains and a recently discovered phox homology (PX) domain. Fish is tyrosine-phosphorylated in Src-transformed fibroblasts (suggesting that it is a target of Src in vivo) and in normal cells following treatment with several growth factors. Treatment of cells with cytochalasin D also resulted in rapid tyrosine phosphorylation of Fish, concomitant with activation of Src. These data suggest that Fish is involved in signalling by tyrosine kinases, and imply a specialized role in the actin cytoskeleton.

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Selected References

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  1. Aspenström P. A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton. Curr Biol. 1997 Jul 1;7(7):479–487. doi: 10.1016/s0960-9822(06)00219-3. [DOI] [PubMed] [Google Scholar]
  2. Barone M. V., Courtneidge S. A. Myc but not Fos rescue of PDGF signalling block caused by kinase-inactive Src. Nature. 1995 Nov 30;378(6556):509–512. doi: 10.1038/378509a0. [DOI] [PubMed] [Google Scholar]
  3. Birney E., Thompson J. D., Gibson T. J. PairWise and SearchWise: finding the optimal alignment in a simultaneous comparison of a protein profile against all DNA translation frames. Nucleic Acids Res. 1996 Jul 15;24(14):2730–2739. doi: 10.1093/nar/24.14.2730. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Bolen J. B., Rowley R. B., Spana C., Tsygankov A. Y. The Src family of tyrosine protein kinases in hemopoietic signal transduction. FASEB J. 1992 Dec;6(15):3403–3409. doi: 10.1096/fasebj.6.15.1281458. [DOI] [PubMed] [Google Scholar]
  5. Brown M. T., Cooper J. A. Regulation, substrates and functions of src. Biochim Biophys Acta. 1996 Jun 7;1287(2-3):121–149. doi: 10.1016/0304-419x(96)00003-0. [DOI] [PubMed] [Google Scholar]
  6. Burdon R. H. Superoxide and hydrogen peroxide in relation to mammalian cell proliferation. Free Radic Biol Med. 1995 Apr;18(4):775–794. doi: 10.1016/0891-5849(94)00198-s. [DOI] [PubMed] [Google Scholar]
  7. Cantley L. C., Auger K. R., Carpenter C., Duckworth B., Graziani A., Kapeller R., Soltoff S. Oncogenes and signal transduction. Cell. 1991 Jan 25;64(2):281–302. doi: 10.1016/0092-8674(91)90639-g. [DOI] [PubMed] [Google Scholar]
  8. Carpino N., Wisniewski D., Strife A., Marshak D., Kobayashi R., Stillman B., Clarkson B. p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells. Cell. 1997 Jan 24;88(2):197–204. doi: 10.1016/s0092-8674(00)81840-1. [DOI] [PubMed] [Google Scholar]
  9. Cartwright C. A., Kamps M. P., Meisler A. I., Pipas J. M., Eckhart W. pp60c-src activation in human colon carcinoma. J Clin Invest. 1989 Jun;83(6):2025–2033. doi: 10.1172/JCI114113. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Cartwright C. A., Meisler A. I., Eckhart W. Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis. Proc Natl Acad Sci U S A. 1990 Jan;87(2):558–562. doi: 10.1073/pnas.87.2.558. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Chang E. C., Barr M., Wang Y., Jung V., Xu H. P., Wigler M. H. Cooperative interaction of S. pombe proteins required for mating and morphogenesis. Cell. 1994 Oct 7;79(1):131–141. doi: 10.1016/0092-8674(94)90406-5. [DOI] [PubMed] [Google Scholar]
  12. Chenevert J., Corrado K., Bender A., Pringle J., Herskowitz I. A yeast gene (BEM1) necessary for cell polarization whose product contains two SH3 domains. Nature. 1992 Mar 5;356(6364):77–79. doi: 10.1038/356077a0. [DOI] [PubMed] [Google Scholar]
  13. Cobb B. S., Schaller M. D., Leu T. H., Parsons J. T. Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, pp125FAK. Mol Cell Biol. 1994 Jan;14(1):147–155. doi: 10.1128/mcb.14.1.147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Courtneidge S. A., Bishop J. M. Transit of pp60v-src to the plasma membrane. Proc Natl Acad Sci U S A. 1982 Dec;79(23):7117–7121. doi: 10.1073/pnas.79.23.7117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Courtneidge S. A., Smith A. E. The complex of polyoma virus middle-T antigen and pp60c-src. EMBO J. 1984 Mar;3(3):585–591. doi: 10.1002/j.1460-2075.1984.tb01852.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Davis S., Lu M. L., Lo S. H., Lin S., Butler J. A., Druker B. J., Roberts T. M., An Q., Chen L. B. Presence of an SH2 domain in the actin-binding protein tensin. Science. 1991 May 3;252(5006):712–715. doi: 10.1126/science.1708917. [DOI] [PubMed] [Google Scholar]
  17. Dikic I., Tokiwa G., Lev S., Courtneidge S. A., Schlessinger J. A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation. Nature. 1996 Oct 10;383(6600):547–550. doi: 10.1038/383547a0. [DOI] [PubMed] [Google Scholar]
  18. Dorseuil O., Reibel L., Bokoch G. M., Camonis J., Gacon G. The Rac target NADPH oxidase p67phox interacts preferentially with Rac2 rather than Rac1. J Biol Chem. 1996 Jan 5;271(1):83–88. doi: 10.1074/jbc.271.1.83. [DOI] [PubMed] [Google Scholar]
  19. Ekena K., Stevens T. H. The Saccharomyces cerevisiae MVP1 gene interacts with VPS1 and is required for vacuolar protein sorting. Mol Cell Biol. 1995 Mar;15(3):1671–1678. doi: 10.1128/mcb.15.3.1671. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Erpel T., Courtneidge S. A. Src family protein tyrosine kinases and cellular signal transduction pathways. Curr Opin Cell Biol. 1995 Apr;7(2):176–182. doi: 10.1016/0955-0674(95)80025-5. [DOI] [PubMed] [Google Scholar]
  21. Erpel T., Superti-Furga G., Courtneidge S. A. Mutational analysis of the Src SH3 domain: the same residues of the ligand binding surface are important for intra- and intermolecular interactions. EMBO J. 1995 Mar 1;14(5):963–975. doi: 10.1002/j.1460-2075.1995.tb07077.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Fincham V. J., Unlu M., Brunton V. G., Pitts J. D., Wyke J. A., Frame M. C. Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins. J Cell Biol. 1996 Dec;135(6 Pt 1):1551–1564. doi: 10.1083/jcb.135.6.1551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Flynn D. C., Leu T. H., Reynolds A. B., Parsons J. T. Identification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp60src substrate. Mol Cell Biol. 1993 Dec;13(12):7892–7900. doi: 10.1128/mcb.13.12.7892. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Fukunaga R., Hunter T. MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates. EMBO J. 1997 Apr 15;16(8):1921–1933. doi: 10.1093/emboj/16.8.1921. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Fumagalli S., Totty N. F., Hsuan J. J., Courtneidge S. A. A target for Src in mitosis. Nature. 1994 Apr 28;368(6474):871–874. doi: 10.1038/368871a0. [DOI] [PubMed] [Google Scholar]
  26. Hall A. Ras-related GTPases and the cytoskeleton. Mol Biol Cell. 1992 May;3(5):475–479. doi: 10.1091/mbc.3.5.475. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Hall A. Rho GTPases and the actin cytoskeleton. Science. 1998 Jan 23;279(5350):509–514. doi: 10.1126/science.279.5350.509. [DOI] [PubMed] [Google Scholar]
  28. Harte M. T., Hildebrand J. D., Burnham M. R., Bouton A. H., Parsons J. T. p130Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase. J Biol Chem. 1996 Jun 7;271(23):13649–13655. doi: 10.1074/jbc.271.23.13649. [DOI] [PubMed] [Google Scholar]
  29. Hwang S., Benjamin L. E., Oh B., Rothstein J. L., Ackerman S. L., Beddington R. S., Solter D., Knowles B. B. Genetic mapping and embryonic expression of a novel, maternally transcribed gene Mem3. Mamm Genome. 1996 Aug;7(8):586–590. doi: 10.1007/s003359900174. [DOI] [PubMed] [Google Scholar]
  30. Ishino M., Ohba T., Sasaki H., Sasaki T. Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn. Oncogene. 1995 Dec 7;11(11):2331–2338. [PubMed] [Google Scholar]
  31. Kavanaugh W. M., Turck C. W., Williams L. T. PTB domain binding to signaling proteins through a sequence motif containing phosphotyrosine. Science. 1995 May 26;268(5214):1177–1179. doi: 10.1126/science.7539155. [DOI] [PubMed] [Google Scholar]
  32. Kozak M. Structural features in eukaryotic mRNAs that modulate the initiation of translation. J Biol Chem. 1991 Oct 25;266(30):19867–19870. [PubMed] [Google Scholar]
  33. Kranenburg O., Poland M., Gebbink M., Oomen L., Moolenaar W. H. Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA. J Cell Sci. 1997 Oct;110(Pt 19):2417–2427. doi: 10.1242/jcs.110.19.2417. [DOI] [PubMed] [Google Scholar]
  34. Kypta R. M., Goldberg Y., Ulug E. T., Courtneidge S. A. Association between the PDGF receptor and members of the src family of tyrosine kinases. Cell. 1990 Aug 10;62(3):481–492. doi: 10.1016/0092-8674(90)90013-5. [DOI] [PubMed] [Google Scholar]
  35. Köhrer K., Emr S. D. The yeast VPS17 gene encodes a membrane-associated protein required for the sorting of soluble vacuolar hydrolases. J Biol Chem. 1993 Jan 5;268(1):559–569. [PubMed] [Google Scholar]
  36. Lee J. W., Choi H. S., Gyuris J., Brent R., Moore D. D. Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol Endocrinol. 1995 Feb;9(2):243–254. doi: 10.1210/mend.9.2.7776974. [DOI] [PubMed] [Google Scholar]
  37. Leeuw T., Fourest-Lieuvin A., Wu C., Chenevert J., Clark K., Whiteway M., Thomas D. Y., Leberer E. Pheromone response in yeast: association of Bem1p with proteins of the MAP kinase cascade and actin. Science. 1995 Nov 17;270(5239):1210–1213. doi: 10.1126/science.270.5239.1210. [DOI] [PubMed] [Google Scholar]
  38. Luttrell L. M., Hawes B. E., van Biesen T., Luttrell D. K., Lansing T. J., Lefkowitz R. J. Role of c-Src tyrosine kinase in G protein-coupled receptor- and Gbetagamma subunit-mediated activation of mitogen-activated protein kinases. J Biol Chem. 1996 Aug 9;271(32):19443–19450. doi: 10.1074/jbc.271.32.19443. [DOI] [PubMed] [Google Scholar]
  39. MacDougall L. K., Domin J., Waterfield M. D. A family of phosphoinositide 3-kinases in Drosophila identifies a new mediator of signal transduction. Curr Biol. 1995 Dec 1;5(12):1404–1415. doi: 10.1016/s0960-9822(95)00278-8. [DOI] [PubMed] [Google Scholar]
  40. McConnell S. J., Yaffe M. P. Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein. J Cell Biol. 1992 Jul;118(2):385–395. doi: 10.1083/jcb.118.2.385. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. McGlade J., Cheng A., Pelicci G., Pelicci P. G., Pawson T. Shc proteins are phosphorylated and regulated by the v-Src and v-Fps protein-tyrosine kinases. Proc Natl Acad Sci U S A. 1992 Oct 1;89(19):8869–8873. doi: 10.1073/pnas.89.19.8869. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Mizushima S., Nagata S. pEF-BOS, a powerful mammalian expression vector. Nucleic Acids Res. 1990 Sep 11;18(17):5322–5322. doi: 10.1093/nar/18.17.5322. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Molz L., Chen Y. W., Hirano M., Williams L. T. Cpk is a novel class of Drosophila PtdIns 3-kinase containing a C2 domain. J Biol Chem. 1996 Jun 7;271(23):13892–13899. doi: 10.1074/jbc.271.23.13892. [DOI] [PubMed] [Google Scholar]
  44. Nobes C. D., Hawkins P., Stephens L., Hall A. Activation of the small GTP-binding proteins rho and rac by growth factor receptors. J Cell Sci. 1995 Jan;108(Pt 1):225–233. doi: 10.1242/jcs.108.1.225. [DOI] [PubMed] [Google Scholar]
  45. Ottenhoff-Kalff A. E., Rijksen G., van Beurden E. A., Hennipman A., Michels A. A., Staal G. E. Characterization of protein tyrosine kinases from human breast cancer: involvement of the c-src oncogene product. Cancer Res. 1992 Sep 1;52(17):4773–4778. [PubMed] [Google Scholar]
  46. Pawson T. Protein modules and signalling networks. Nature. 1995 Feb 16;373(6515):573–580. doi: 10.1038/373573a0. [DOI] [PubMed] [Google Scholar]
  47. Peterson J., Zheng Y., Bender L., Myers A., Cerione R., Bender A. Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast. J Cell Biol. 1994 Dec;127(5):1395–1406. doi: 10.1083/jcb.127.5.1395. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Polte T. R., Hanks S. K. Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas. Proc Natl Acad Sci U S A. 1995 Nov 7;92(23):10678–10682. doi: 10.1073/pnas.92.23.10678. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Ponting C. P. Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains? Protein Sci. 1996 Nov;5(11):2353–2357. doi: 10.1002/pro.5560051122. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Ponting C. P., Parker P. J. Extending the C2 domain family: C2s in PKCs delta, epsilon, eta, theta, phospholipases, GAPs, and perforin. Protein Sci. 1996 Jan;5(1):162–166. doi: 10.1002/pro.5560050120. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Reynolds A. B., Herbert L., Cleveland J. L., Berg S. T., Gaut J. R. p120, a novel substrate of protein tyrosine kinase receptors and of p60v-src, is related to cadherin-binding factors beta-catenin, plakoglobin and armadillo. Oncogene. 1992 Dec;7(12):2439–2445. [PubMed] [Google Scholar]
  52. Ridley A. J., Hall A. Signal transduction pathways regulating Rho-mediated stress fibre formation: requirement for a tyrosine kinase. EMBO J. 1994 Jun 1;13(11):2600–2610. doi: 10.1002/j.1460-2075.1994.tb06550.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Rothberg K. G., Heuser J. E., Donzell W. C., Ying Y. S., Glenney J. R., Anderson R. G. Caveolin, a protein component of caveolae membrane coats. Cell. 1992 Feb 21;68(4):673–682. doi: 10.1016/0092-8674(92)90143-z. [DOI] [PubMed] [Google Scholar]
  54. Sadoshima J., Izumo S. The heterotrimeric G q protein-coupled angiotensin II receptor activates p21 ras via the tyrosine kinase-Shc-Grb2-Sos pathway in cardiac myocytes. EMBO J. 1996 Feb 15;15(4):775–787. [PMC free article] [PubMed] [Google Scholar]
  55. Sakai R., Iwamatsu A., Hirano N., Ogawa S., Tanaka T., Mano H., Yazaki Y., Hirai H. A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J. 1994 Aug 15;13(16):3748–3756. doi: 10.1002/j.1460-2075.1994.tb06684.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Segal A. W., Abo A. The biochemical basis of the NADPH oxidase of phagocytes. Trends Biochem Sci. 1993 Feb;18(2):43–47. doi: 10.1016/0968-0004(93)90051-n. [DOI] [PubMed] [Google Scholar]
  57. Sicheri F., Moarefi I., Kuriyan J. Crystal structure of the Src family tyrosine kinase Hck. Nature. 1997 Feb 13;385(6617):602–609. doi: 10.1038/385602a0. [DOI] [PubMed] [Google Scholar]
  58. Songyang Z., Cantley L. C. Recognition and specificity in protein tyrosine kinase-mediated signalling. Trends Biochem Sci. 1995 Nov;20(11):470–475. doi: 10.1016/s0968-0004(00)89103-3. [DOI] [PubMed] [Google Scholar]
  59. Songyang Z., Shoelson S. E., Chaudhuri M., Gish G., Pawson T., Haser W. G., King F., Roberts T., Ratnofsky S., Lechleider R. J. SH2 domains recognize specific phosphopeptide sequences. Cell. 1993 Mar 12;72(5):767–778. doi: 10.1016/0092-8674(93)90404-e. [DOI] [PubMed] [Google Scholar]
  60. Sparks A. B., Hoffman N. G., McConnell S. J., Fowlkes D. M., Kay B. K. Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins. Nat Biotechnol. 1996 Jun;14(6):741–744. doi: 10.1038/nbt0696-741. [DOI] [PubMed] [Google Scholar]
  61. Superti-Furga G., Courtneidge S. A. Structure-function relationships in Src family and related protein tyrosine kinases. Bioessays. 1995 Apr;17(4):321–330. doi: 10.1002/bies.950170408. [DOI] [PubMed] [Google Scholar]
  62. Tapon N., Nagata K., Lamarche N., Hall A. A new rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways. EMBO J. 1998 Mar 2;17(5):1395–1404. doi: 10.1093/emboj/17.5.1395. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Taylor S. J., Shalloway D. An RNA-binding protein associated with Src through its SH2 and SH3 domains in mitosis. Nature. 1994 Apr 28;368(6474):867–871. doi: 10.1038/368867a0. [DOI] [PubMed] [Google Scholar]
  64. Thompson J. D., Higgins D. G., Gibson T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994 Nov 11;22(22):4673–4680. doi: 10.1093/nar/22.22.4673. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Toda M., Shirao T., Minoshima S., Shimizu N., Toya S., Uyemura K. Molecular cloning of cDNA encoding human drebrin E and chromosomal mapping of its gene. Biochem Biophys Res Commun. 1993 Oct 15;196(1):468–472. doi: 10.1006/bbrc.1993.2273. [DOI] [PubMed] [Google Scholar]
  66. Tsuji E., Tsuji Y., Misumi Y., Fujita A., Sasaguri M., Ideishi M., Arakawa K. Molecular cloning of a novel rat salt-tolerant protein by functional complementation in yeast. Biochem Biophys Res Commun. 1996 Dec 4;229(1):134–138. doi: 10.1006/bbrc.1996.1769. [DOI] [PubMed] [Google Scholar]
  67. Turner C. E., Miller J. T. Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region. J Cell Sci. 1994 Jun;107(Pt 6):1583–1591. doi: 10.1242/jcs.107.6.1583. [DOI] [PubMed] [Google Scholar]
  68. Virbasius J. V., Guilherme A., Czech M. P. Mouse p170 is a novel phosphatidylinositol 3-kinase containing a C2 domain. J Biol Chem. 1996 Jun 7;271(23):13304–13307. doi: 10.1074/jbc.271.23.13304. [DOI] [PubMed] [Google Scholar]
  69. Volpp B. D., Nauseef W. M., Donelson J. E., Moser D. R., Clark R. A. Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase. Proc Natl Acad Sci U S A. 1989 Sep;86(18):7195–7199. doi: 10.1073/pnas.86.18.7195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Wada Y., Anraku Y. Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. II. VAM7, a gene for regulating morphogenic assembly of the vacuoles. J Biol Chem. 1992 Sep 15;267(26):18671–18675. [PubMed] [Google Scholar]
  71. Wientjes F. B., Hsuan J. J., Totty N. F., Segal A. W. p40phox, a third cytosolic component of the activation complex of the NADPH oxidase to contain src homology 3 domains. Biochem J. 1993 Dec 15;296(Pt 3):557–561. doi: 10.1042/bj2960557. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Williams J. C., Weijland A., Gonfloni S., Thompson A., Courtneidge S. A., Superti-Furga G., Wierenga R. K. The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions. J Mol Biol. 1997 Dec 19;274(5):757–775. doi: 10.1006/jmbi.1997.1426. [DOI] [PubMed] [Google Scholar]
  73. Wu H., Reynolds A. B., Kanner S. B., Vines R. R., Parsons J. T. Identification and characterization of a novel cytoskeleton-associated pp60src substrate. Mol Cell Biol. 1991 Oct;11(10):5113–5124. doi: 10.1128/mcb.11.10.5113. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Xu W., Harrison S. C., Eck M. J. Three-dimensional structure of the tyrosine kinase c-Src. Nature. 1997 Feb 13;385(6617):595–602. doi: 10.1038/385595a0. [DOI] [PubMed] [Google Scholar]
  75. Yamabhai M., Kay B. K. Examining the specificity of Src homology 3 domain--ligand interactions with alkaline phosphatase fusion proteins. Anal Biochem. 1997 Apr 5;247(1):143–151. doi: 10.1006/abio.1997.2040. [DOI] [PubMed] [Google Scholar]
  76. Yamanashi Y., Baltimore D. Identification of the Abl- and rasGAP-associated 62 kDa protein as a docking protein, Dok. Cell. 1997 Jan 24;88(2):205–211. doi: 10.1016/s0092-8674(00)81841-3. [DOI] [PubMed] [Google Scholar]
  77. Zheng Y., Cerione R., Bender A. Control of the yeast bud-site assembly GTPase Cdc42. Catalysis of guanine nucleotide exchange by Cdc24 and stimulation of GTPase activity by Bem3. J Biol Chem. 1994 Jan 28;269(4):2369–2372. [PubMed] [Google Scholar]

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