Structural Requirements for Enhancement of T-Cell Responsiveness by the Lymphocyte-Specific Tyrosine Protein Kinase p56^lck

References

• Abraham, Ν., Μ. C. Miceli, J. R. Parnes, and A. Veillette. 1991. Enhancement of T-cell responsiveness by the lymphocyte-specific tyrosine protein kinase p56lck. Nature (London) 350:62–66.
   PubMedGoogle Scholar
• Abraham, N., and A. Veillette. 1990. Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation. Mol. Cell. Biol. 10:5197–5206.
   PubMed Web of Science ®Google Scholar
• Abraham, N., and A. Veillette. Unpublished data.
   Google Scholar
• Albritton, L. M., L. Tseng, D. Scadden, and J. M. Cunningham. 1989. A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection. Cell 57:659–666.
   PubMed Web of Science ®Google Scholar
• Amrein, Κ. Ε., and Β. Μ. Sefton. 1988. Mutation of a site of tyrosine phosphorylation in the lymphocyte-specific tyrosine protein kinase, p56lck, reveals its oncogenic potential in fibroblasts. Proc. Natl. Acad. Sci. USA 85:4247–4251.
   PubMed Web of Science ®Google Scholar
• Bouton, A. H., S. B. Kanner, R. R. Vines, H.-C. R. Wang, J. B. Gibbs, and J. T. Parsons. 1991. Transformation by pp60src or stimulation of cells with epidermal growth factor induces the stable association of tyrosine-phosphorylated cellular proteins with GTPase-activating protein. Mol. Cell. Biol. 11:945–953.
   PubMedGoogle Scholar
• Brott, B. K., S. Decker, M. C. O’Brien, and R. Jove. 1991. Molecular features of the viral and cellular Src kinases involved in interactions with the GTPase-activating protein. Mol. Cell. Biol. 11:5059–5067.
   PubMedGoogle 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
• Caron, L., G. D. Gish, T. Pawson, and A. Veillette. Unpublished data.
   Google Scholar
• Casnellie, J. E., M. L. Harrison, L. J. Pike, Κ. Ε. Hellstrom, and E. G. Krebs. 1982. Phosphorylation of synthetic peptides by a tyrosine kinase from the particulate fraction of a lymphoma cell line. Proc. Natl. Acad. Sci. USA 79:282–286.
   PubMedGoogle Scholar
• Chan, A. C., B. A. Irving, J. D. Fraser, and A. Weiss. 1991. The ζ chain is associated with a tyrosine kinase and upon T-cell antigen receptor stimulation associates with ZAP-70, a 70-kDa tyrosine phosphoprotein. Proc. Natl. Acad. Sci. USA 88:9166–9170.
   PubMedGoogle Scholar
• Cooke, M. P., K. M. Abraham, K. A. Forbush, and R. M. Perlmutter. 1991. Regulation of Τ cell receptor signaling by a src family protein-tyrosine kinase (p59fyn). Cell 65:281–291.
   PubMed Web of Science ®Google Scholar
• Cooke, M. P., and R. M. Perlmutter. 1989. Expression of a novel form of the fyn proto-oncogene in hematopoietic cells. New Biol. 1:66–74.
   PubMedGoogle Scholar
• Cooper, J. A. 1990. The src family of tyrosine-protein kinases, p. 85–113. In Β. Ε. Kemps (ed.), Peptides and protein phosphorylation. CRC Press, Boca Raton, Fla.
   Google Scholar
• Davidson, D., L. M. L. Chow, M. Fournel, and A. Veillette. Differential regulation of T-cell antigen responsiveness by isoforms of the src-related tyrosine protein kinase p59fyn. J. Exp. Med., in press.
   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
• Hsi, E. D., J. N. Siegel, Y. Minami, E. T. Luong, R. D. Klausner, and L. E. Samelson. 1989. Τ cell activation induces rapid tyrosine phosphorylation of a limited number of cellular substrates. J. Biol. Chem. 264:10836–10842.
   PubMedGoogle Scholar
• June, C. H., M. C. Fletcher, J. A. Ledbetter, G. L. Schieven, J. N. Siegel, A. F. Phillips, and L. E. Samelson. 1990. Inhibition of tyrosine phosphorylation prevents T-cell receptor-mediated signal transduction. Proc. Natl. Acad. Sci. USA 87:7722–7726.
   PubMed Web of Science ®Google Scholar
• Kamps, M. P., and Β. Μ. Sefton. 1988. Identification of multiple novel polypeptide substrates of the v-src, v-yes, v-fps, v-ros and v-erb-B oncogenic tyrosine protein kinases utilizing antisera against phosphotyrosine. Oncogene 2:305–315.
   PubMedGoogle Scholar
• Klausner, R. D., and L. E. Samelson. 1991. Τ cell antigen receptor activation pathways: the tyrosine kinase connection. Cell 64:875–878.
   PubMed Web of Science ®Google Scholar
• Koch, C. Α., D. Anderson, M. F. Moran, C. Ellis, and T. Pawson. 1991. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 252:668–674.
   PubMed Web of Science ®Google Scholar
• Koch, C. Α., Μ. Moran, I. Sadowski, and T. Pawson. 1989. The common src homology region 2 domain of cytoplasmic signaling proteins is a positive effector of v-fps tyrosine kinase function. Mol. Cell. Biol. 9:4131–4140.
   PubMedGoogle Scholar
• Luo, K., and Β. Μ. Sefton. 1990. Cross-linking of T-cell surface molecules CD4 and CD8 stimulates phosphorylation of the lck tyrosine protein kinase at the autophosphorylation site. Mol. Cell. Biol. 10:5305–5313.
   PubMed Web of Science ®Google Scholar
• Marth, J. D., J. A. Cooper, C. S. King, S. F. Ziegler, D. A. Tinker, R. W. Overell, E. G. Krebs, and R. M. Perlmutter. 1988. Neoplastic transformation induced by an activated lymphocyte-specific protein tyrosine kinase (pp56lck). Mol. Cell. Biol. 8:540–550.
   PubMed Web of Science ®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 Τ cell lymphoma LSTRA. Cell 43:393–404.
   PubMed Web of Science ®Google Scholar
• Miceli, M. C., and J. R. Parnes. 1991. The roles of CD4 and CD8 in T-cell activation. Sem. Immunol. 3:133–141.
   PubMedGoogle Scholar
• Miceli, M. C., P. von Hoegen, and J. R. Parnes. 1991. Adhesion versus coreceptor function of CD4 and CD8: role of the cytoplasmic tail in coreceptor activity. Proc. Natl. Acad. Sci. USA 88:2623–2627.
   PubMedGoogle Scholar
• Moran, M. F., C. A. Koch, D. Anderson, C. Ellis, L. England, G. S. Martin, and T. Pawson. 1990. Src homology region 2 domains direct protein-protein interactions in signal transduction. Proc. Natl. Acad. Sci. USA 87:8622–8626.
   PubMed Web of Science ®Google Scholar
• Mosmann, T. 1983. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Methods 65:55–63.
   PubMed Web of Science ®Google Scholar
• Mustelin, T., K. M. Coggeshall, N. Isakov, and A. Altman. 1990. Τ cell antigen receptor-mediated activation of phospholipase C requires tyrosine phosphorylation. Science 247:1584–1587.
   PubMed Web of Science ®Google Scholar
• Nishibe, S., M. I. Wahl, S. Μ. Τ. Hernandez-Sotomayor, Ν. Κ. Tonks, S. G. Rhee, and G. Carpenter. 1990. Increase of the catalytic activity of phospholipase C-γ1 by tyrosine phosphorylation. Science 250:1253–1256.
   PubMed Web of Science ®Google Scholar
• Park, D. J., Y. W. Rho, and S. G. Rhee. 1991. CD3 stimulation causes phosphorylation of phospholipase C on serine and tyrosine residues in a human T-cell line. Proc. Natl. Acad. Sci. USA 88:5453–5456.
   PubMedGoogle Scholar
• Reske-Kunz, A. B., and E. Rude. 1985. Insulin-specific Τ cell hybridomas derived from (H-2bxH-2k) F1 mice preferably employ F1-unique restriction elements for antigen recognition. Eur. J. Immunol. 15:1048–1054.
   PubMedGoogle Scholar
• Rudd, C. E., J. M. Trevillyan, J. D. Dasgupta, L. L. Wong, and S. F. Schlossman. 1988. The CD4 receptor is complexed in detergent lysates to a protein-tyrosine kinase (pp58) from human Τ lymphocytes. Proc. Natl. Acad. Sci. USA 85:5190–5194.
   PubMed Web of Science ®Google Scholar
• Samelson, L. E., A. F. Phillips, Ε. Τ. Luong, and R. D. Klausner. 1991. Association of the fyn tyrosine-protein kinase with the Τ cell antigen receptor. Proc. Natl. Acad. Sci. USA 88:4358–4362.
   PubMedGoogle Scholar
• Secrist, J. P., L. Karnitz, and R. T. Abraham. 1991. T-cell antigen receptor ligation induces tyrosine phosphorylation of phospholipase C-gamma 1. J. Biol. Chem. 266:12135–12139.
   PubMedGoogle Scholar
• Sefton, Β. Μ. 1991. The lck tyrosine protein kinase. Oncogene 6:683–686.
   PubMedGoogle Scholar
• Staerz, U. D., H. Rammensee, J. D. Benedetto, and M. J. Sevan. 1985. Characterization of a murine monoclonal antibody specific for an allotypic determinant on Τ cell antigen receptor. J. Immunol. 134:3996–4000.
   Google Scholar
• Stahl, M. L., C. R. Ferenz, K. L. Kelleher, R. W. Kriz, and J. L. Knopf. 1988. Sequence similarity of phospholipase C with the non-catalytic region of src. Nature (London) 332:269–272.
   PubMed Web of Science ®Google Scholar
• Stanley, J. B., R. Gorczynski, C.-K. Huang, L. Love, and G. B. Mills. 1990. Tyrosine phosphorylation is an obligatory event in IL-2 secretion. J. Immunol. 145:2189–2198.
   PubMed Web of Science ®Google Scholar
• Stefanova, I., V. Horejsi, I. J. Ansotegui, W. Knapp, and H. Stockinger. 1991. GPI-anchored cell-surface molecules complexed to protein tyrosine kinases. Science 254:1016–1019.
   PubMed Web of Science ®Google Scholar
• Sultzman, L., C. Ellis, L.-L. Lin, T. Pawson, and J. Knopf. 1991. Platelet-derived growth factor increases the in vivo activity of phospholipase C-γ1 and phospholipase C-γ2. Mol. Cell. Biol. 11:2018–2025.
   PubMed Web of Science ®Google Scholar
• Trevillyan, J. M., Y. Lu, D. Atluru, C. A. Phillips, and J. M. Bjorndahl. 1990. Differential inhibition of Τ cell receptor activation events by a selective inhibitor of protein-tyrosine kinase. J. Immunol. 145:3223–3230.
   PubMed Web of Science ®Google Scholar
• Veillette, Α., Ν. Abraham, L. Caron, and D. Davidson. 1991. The lymphocyte-specific tyrosine protein kinase p56lck. Sem. Immunol. 3:143–152.
   PubMedGoogle Scholar
• Veillette, Α., J. B. Bolen, and M. A. Bookman. 1989. Alterations in tyrosine protein phosphorylation induced by antibody-mediated cross-linking of the CD4 receptor of Τ lymphocytes. Mol. Cell. Biol. 9:4441–4446.
   PubMed Web of Science ®Google Scholar
• Veillette, Α., Μ. A. Bookman, Ε. Μ. Horak, and J. Β. Bolen. 1988. The CD4 and CD8 Τ cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck. Cell 55:301–308.
   PubMed Web of Science ®Google Scholar
• Veillette, Α., Μ. A. Bookman, Ε. Μ. 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 p56lck. Nature (London) 338:257–259.
   PubMed Web of Science ®Google Scholar
• Veillette, Α., L. Caron, M. Fournel, and T. Pawson. Regulation of the enzymatic function of the lymphocyte-specific tyrosine protein kinase p56lck by the non-catalytic SH2 and SH3 domains. Oncogene, in press.
   Google Scholar
• Veillette, Α., and D. Davidson. 1992. Src-related protein tyrosine kinases and T-cell receptor signalling. Trends Genet. 8:61–66.
   PubMedGoogle Scholar
• Veillette, Α., and M. Fournel. 1990. The CD4 associated tyrosine protein kinase p56lck is positively regulated through its site of autophosphorylation. Oncogene 5:1455–1462.
   PubMedGoogle Scholar
• Veillette, Α., I. D. Horak, and J. B. Bolen. 1988. Post-translational alterations of the tyrosine kinase p56lck in response to activators of protein kinase C. Oncogene Res. 2:385–401.
   PubMedGoogle Scholar
• Veillette, Α., I. D. Horak, M. A. Bookman, and J. B. Bolen. 1988. Alterations of the lymphocyte-specific protein tyrosine kinase (p56lck) during T-cell activation. Mol. Cell. Biol. 8:4353–4361.
   PubMed Web of Science ®Google Scholar
• Voronova, A. F., and Β. Μ. Sefton. 1986. Expression of a new tyrosine protein kinase is stimulated by retrovirus promoter insertion. Nature (London) 319:682–685.
   PubMed Web of Science ®Google Scholar
• Weiss, Α., G. Koretzky, R. C. Schatzman, and T. Kadlecek. 1991. Functional activation of the T-cell antigen receptor induces tyrosine phosphorylation of phospholipase C-gamma 1. Proc. Natl. Acad. Sci. USA 88:5484–5488.
   PubMedGoogle Scholar