The SH3 Domain of p56^lck Is Involved in Binding to Phosphatidylinositol 3′-Kinase from T Lymphocytes

References

• Abraham, N., M. C. Miceli, J. R. Parnes, and A. Veillette. 1991. Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck. Nature (London) 350:6266.
   Google Scholar
• Augustine, J. A., S. L. Sutor, and R. T. Abraham. 1991. Interleukin 2- and polyomavirus middle T antigen-induced modification of phosphatidylinositol 3-kinase activity in activated T-lymphocytes. Mol. Cell. Biol. 11:4431–4440.
   PubMed Web of Science ®Google Scholar
• Barber, E. K., J. D. Dasgupta, S. F. Schlossman, J. M. Trevil-lyan, and C. E. Rudd. 1989. The CD4 and CD8 antigens are coupled to a protein-tyrosine kinase (p561ck) that phosphory-lates the CD3 complex. Proc. Natl. Acad. Sci. USA 86:3277–3281.
   PubMed Web of Science ®Google Scholar
• Bjorge, J. D., T.-O. Chan, M. Antczak, H.-J. Kung, and D. Fujita. 1990. Activated type I phosphatidylinositol kinase is associated with the epidermal growth factor (EGF) receptor following EGF stimulation. Proc. Natl. Acad. Sci. USA 87: 3816–3820.
   PubMed Web of Science ®Google Scholar
• Cantley, L. C., K. R. Auger, C. Carpenter, B. Duckworth, A. Graziani, R. Kapeller, and S. Soltoff. 1991. Oncogenes and signal transduction. Cell 64:281–302.
   PubMed Web of Science ®Google Scholar
• Carpenter, C. L., B. C. Duckworth, K. R. Auger, B. Cohen, B. S. Schaffhausen, and L. C. Cantley. 1990. Purification and characterization of phosphoinositide 3-kinase from rat liver. J. Biol. Chem. 265:19704–19711.
   PubMed Web of Science ®Google Scholar
• Chan, T.-O., A. Tanaka, J. D. Bjorge, and D. J. Fujita. 1990. Association of type I phosphatidylinositol kinase activity with mutationally activated forms of human pp60c-src.. Mol. Cell. Biol. 10:3280–3283.
   PubMedGoogle Scholar
• Cicchetti, P., B. J. Mayer, G. Theil, and D. Baltimore. 1992. Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho. Science 257:803–806.
   PubMedGoogle Scholar
• Coughlin, S. R., J. A. Escobedo, and L. T. Williams. 1989. Role of phosphatidylinositol kinase in PDGF receptor signal transduction. Science 243:1191–1193.
   PubMed Web of Science ®Google Scholar
• Courtneidge, S. A., and A. Heber. 1987. An 81 kd protein complexed with middle T antigen and pp60c-src: a possible phosphatidylinositol kinase. Cell 50:1031–1037.
   PubMed Web of Science ®Google Scholar
• Escobedo, J. A., D. R. Kaplan, W. M. Kavanaugh, C. W. Turck, and L. T. Williams. 1991. A phosphatidylinositol-3 kinase binds to platelet-derived growth factor receptors through a specific receptor sequence containing phosphotyrosine. Mol. Cell. Biol. 11:1125–1132.
   PubMed Web of Science ®Google Scholar
• Escobedo, J. A., and L. T. Williams. 1988. A PDGF receptor domain essential for mitogenesis but not for many other responses to PDGF. Nature (London) 335:85–87.
   PubMed Web of Science ®Google Scholar
• Fantl, W. J., J. A. Escobedo, G. A. Martin, C. W. Turck, M. del Rosario, F. McCormick, and L. T. Williams. 1992. Distinct phosphotyrosines on a growth factor receptor bind to specific molecules that mediate different signalling pathways. Cell 69:110.
   Google Scholar
• Fukui, Y., and H. Hanafusa. 1989. Phosphatidylinositol kinase activity associates with viral p60src protein. Mol. Cell. Biol. 9:1651–1658.
   PubMedGoogle Scholar
• Fukui, Y., and H. Hanafusa. 1991. Requirement of phosphati-dylinositol-3 kinase modification for its association with p60src. Mol. Cell. Biol. 11:1972–1979.
   PubMedGoogle Scholar
• Fukui, Y., S. Kombluth, S.-M. Jong, L.-H. Wang, and H. Hanafusa. 1989. Phosphatidylinositol kinase type I activity associates with various oncogene products. Oncogene Res. 4:283–292.
   PubMedGoogle Scholar
• Fukui, Y., M. C. O’Brien, and H. Hanafusa. 1991. Deletions in the SH2 domain of p60v-src prevent association with the detergent-insoluble cellular matrix. Mol. Cell. Biol. 11:1207–1213.
   PubMedGoogle Scholar
• Glaichenhaus, N., N. Shastri, D. R. Littman, and J. M. Turner. 1991. Requirement for association of p56lck with CD4 in antigen-specific signal transduction in T cells. Cell 64:511–520.
   PubMed Web of Science ®Google Scholar
• Gutierrez, C., R. R. Berabe, and J. Vega. 1979. Purification of human T and B cells by a discontinuous density gradient of Percoll. J. Immunol. Methods 29:57–66.
   PubMed Web of Science ®Google Scholar
• Hatakeyama, M., T. Kono, N. Kobayashi, A. Kawahara, S. D. Levin, R. M. Perlmutter, and T. Taniguchi. 1991. Interaction of the IL-2 receptor with the src-family kinase p56lck: identification of novel intermolecular association. Science 252:1523–1528.
   PubMed Web of Science ®Google Scholar
• Hiles, I. D., M. Otsu, S. Volinia, M. J. Fry, R. Dhand, G. Panayotou, F. Ruiz-Larrea, A. Thompson, N. F. Totty, J. J. Hsuan, S. A. Courtneidge, P. J. Parker, and M. D. Waterfield. 1992. Phosphatidylinositol 3-kinase: structure and expression of the 110 kD catalytic subunit. Cell 70:419–429.
   PubMed Web of Science ®Google Scholar
• Hu, P., B. Margolis, E. Y. Skolnik, R. Lammers, A. Ullrich, and J. Schlessinger. 1992. Interaction of phosphatidylinositol 3-kinase-associated p85 with epidermal growth factor and platelet-derived growth factor receptors. Mol. Cell. Biol. 12:981–990.
   PubMed Web of Science ®Google Scholar
• Hunter, T.%% 1989. Oncogene products in the cytoplasm: the protein kinases, p. 147-173. In R. A. Weinberg (ed.), Oncogenes and the molecular origins of cancer. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Kaplan, D. R., M. Whitman, B. Schaffhausen, D. C. Pallas, M. White, L. Cantley, and T. M. Roberts. 1987. Common elements in growth factor stimulation and oncogenic transformation: 85 kd phosphoprotein and phosphatidylinositol kinase activity. Cell 50:1021–1029.
   PubMed Web of Science ®Google Scholar
• Kazlauskas, A., and J. A. Cooper. 1989. Autophosphorylation of the PDGF receptor in the kinase insert region regulates interaction with cell proteins. Cell 58:1121–1133.
   PubMedGoogle Scholar
• Klippel, A., J. A. Escobedo, W. J. Fantl, and L. T. Williams. 1992. The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platelet-derived growth factor beta receptor. Mol. Cell. Biol. 12:1451–1459.
   PubMed Web of Science ®Google Scholar
• Koch, C. A., D. Anderson, M. F. Moran, C. Ellis, and T. Pawson. 1991. SH2 and SH3 domains: elements that control interaction of cytoplasmic signaling proteins. Science 252:668–674.
   PubMed Web of Science ®Google Scholar
• Koga, Y., N. Kimura, J. Minowada, and T. W. Mak. 1988. Expression of the human T-cell-specific tyrosine kinase YT16 (lck) message in leukemic T-cell lines. Cancer Res. 48:856–859.
   PubMedGoogle Scholar
• Ledbetter, J. A., C. H. June, P. S. Rabinovitch, A. Grossmann, T. T. Tsu, and J. B. Imboden. 1988. Signal transduction through CD4 receptors: stimulatory vs. inhibitory activity is regulated by CD4 proximity to the CD3/T cell receptor. Eur. J. Immunol. 18:525–532.
   Google Scholar
• Liu, X., and T. Pawson. Personal communication.
   Google Scholar
• Marth, J. D., R. Peet, E. G. Krebs, and R. M. Perlmutter. 1985. A lymphocyte-specific protein-tyrosine kinase gene is rearranged and overexpressed in the murine T cell lymphoma LSTRA. Cell 43:393–404.
   PubMed Web of Science ®Google Scholar
• McGlade, C. J., C. Ellis, M. Reedijk, D. Anderson, G. Mbamalu, A. D. Reith, G. Panayotou, P. End, A. Bernstein, A. Kazlauskas, and et-al. 1992. SH2 domains of the p85 alpha subunit of phosphatidylinositol 3-kinase regulate binding to growth factor receptors. Mol. Cell. Biol. 12:991–997.
   PubMed Web of Science ®Google Scholar
• Mustelin, T., and A. Altman. 1989. Do CD4 and CD8 control T-cell activation via a specific tyrosine protein kinase? Immunol. Today 10:189–192.
   Google Scholar
• Nel, A. E., S. Pollack, G. Landreth, J. A. Ledbetter, L. Hultin, K. Williams, R. Katz, and B. Akerley. 1990. CD-3-mediated activation of MAP-2 kinase can be modified by ligation of the CD4 receptor. J. Immunol. 145:971–979.
   PubMedGoogle Scholar
• O’Brien, M. C., Y. Fukni, and H. Hanafusa. 1990. Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain. Mol. Cell. Biol. 10:2855–2862.
   PubMedGoogle Scholar
• Otsu, M., I. Hiles, I. Gout, M. J. Fry, F. Ruiz-Larrea, G. Panayotou, A. Thompson, R. Dhand, J. Hsuan, N. Totty, et al. 1991. Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase. Cell 65:91–104.
   PubMed Web of Science ®Google Scholar
• Perlmutter, R. M.%% 1989. T-cell signalling. Science 245:344–347.
   PubMed Web of Science ®Google Scholar
• Perlmutter, R. M., J. D. Marth, D. B. Lewis, R. Peet, S. F. Ziegler, and C. B. Wilson. 1988. Structure and expression of lck transcripts in human lymphoid cells. J. Cell Biochem. 38:117–126.
   PubMedGoogle Scholar
• Reedyk, M., X. Liu, P. van-der-Geer, K. Letwin, M. D. Water-Held, T. Hunter, and T. Pawson. 1992. Tyr721 regulates specific binding of the CSF-1 receptor kinase insert to PI 3′-kinase SH2 domains: a model for SH2-mediated receptor-target interactions. EMBO J. 11:1365–1372.
   PubMedGoogle Scholar
• Shaw, A. S., K. E. Amrein, C. Hammond, D. F. Stern, B. M. Sefton, and J. K. Rose. 1989. The lck tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 59:627–636.
   PubMed Web of Science ®Google Scholar
• Shaw, A. S., J. Chalupny, J. A. Whitney, C. Hammond, K. E. Amrein, P. Kavathas, B. M. Sefton, and J. K. Rose. 1990. Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase. Mol. Cell. Biol. 10:1853–1862.
   PubMed Web of Science ®Google Scholar
• Smith, D. B., and K. S. Johnson. 1988. Single step purification of polypeptides expressed in Escherichia coli as fusion with glutathione agarose. Gene 67:31–40.
   PubMed Web of Science ®Google Scholar
• Tanaka, A., C. P. Gibb, A. A. Arthur, S. K. Anderson, H.-J. Kung, and D. J. Fujita. 1987. DNA sequences encoding the amino-terminal region of the human c-src protein: implications of sequence divergence among src-type kinase oncogenes. Mol. Cell. Biol. 7:1978–1983.
   PubMedGoogle Scholar
• Telfer, J. C., and C. E. Rudd. 1991. A 32-kd GTP-binding protein associated with the CD4-p561ck and CD8-p561ck T-cell receptor complexes. Science 254:439–441.
   PubMedGoogle Scholar
• Thompson, P. A., J. S. Gutkind, K. C. Robbins, J. A. Ledbetter, and J. B. Bolen. 1992. Identification of distinct populations of PI-3 kinase activity following T-cell activation. Oncogene 7: 719–725.
   PubMedGoogle Scholar
• Turner, J. M., M. H. Brodsky, B. A. Irving, S. D. Levin, R. M. Perlmutter, and D. R. Littman. 1990. Interaction of the unique N-terminal region of tyrosine kinase p561ck with cytoplasmic domains of CD4 and CD8 is mediated by cysteine motifs. Cell 60:755–765.
   PubMed Web of Science ®Google Scholar
• Valins, M., and A. Kazlauskas. 1993. Phospholipase C-gamma and phosphatidylinositol-3 kinase are downstream mediators of the PDGF receptor’s mitogenic signal. Cell 73:321–334.
   PubMedGoogle Scholar
• Veillette, A., J. B. Bolen, and M. A. Bookman. 1989. Alterations in tyrosine protein phosphorylation induced by antibody-mediated cross-linking of the CD4 receptor of T lymphocytes. Mol. Cell. Biol. 9:4441–4446.
   PubMed Web of Science ®Google Scholar
• Veillette, A., M. A. Bookman, E. M Horak, and J. B. Bolen. 1988. The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p561ck. Cell 55:301–308.
   PubMed Web of Science ®Google Scholar
• Veillette, A., M. A. Bookman, E. M. Horak, L. E. Samelson, and J. B. Bolen. 1989. Signal transduction through the CD4 receptor involves the activation of the internal membrane tyrosine-protein kinase p561ck. Nature 338:257–259.
   PubMed Web of Science ®Google Scholar
• Veillette, A., F. M. Foss, E. A. Sausville, J. B. Bolen, and N. Rosen. 1987. Expression of the lck tyrosine kinase gene in human colon carcinoma and other non-lymphoid human tumor cell lines. Oncogene Res. 1:357–374.
   PubMedGoogle Scholar
• Veillette, A., I. D. Horak, and J. B. Bolen. 1988. Post-translational alterations of the tyrosine kinase p561ck in response to activators of protein kinase C. Oncogene Res. 2:385–401.
   PubMedGoogle Scholar
• Vogel, L. B., and D. J. Fujita. Stimulation dependent association of p561ck with a 70 kD phosphoprotein that contains significant amino acid identity to GAP-associated p62. Submitted for publication.
   Google Scholar
• Wages, D. S., J. Keefer, T. B. Rail, and M. J. Weber. 1992. Mutations in the SH3 domain of the src oncogene which decrease association of phosphatidylinositol 3′-kinase activity with pp60v-src and alter cellular morphology. J. Virol. 66:1866–1874.
   PubMed Web of Science ®Google Scholar
• Weber, J. R., G. M. Bell, M. Y. Han, T. Pawson, and J. B. Imboden. 1992. Association of the tyrosine kinase LCK with phospholipase C-gamma 1 after stimulation of the T cell antigen receptor. J. Exp. Med. 176:373–379.
   PubMedGoogle Scholar
• Whitman, M., D. R. Kaplan, B. Schaffhausen, and L. Cantley. 1987. Evidence for two distinct phosphatidylinositol kinases in fibroblasts. Biochem. J. 247:165–174.
   PubMed Web of Science ®Google Scholar
• Whitman, M., D. R. Kaplan, B. Schaffhausen, L. Cantley, and T. M. Roberts. 1985. Association of phosphatidylinositol kinase activity with polyoma middle-T competent for transformation. Nature (London) 315:239–242.
   PubMed Web of Science ®Google Scholar
• Whitman, M., and L. Cantley. 1988. Phosphoinositide metabolism and the control of cell proliferation. Biochim. Biophys. Acta 948:327–344.
   Web of Science ®Google Scholar