Unique Catalytic Properties Dictate the Enhanced Function of p59^fynT, the Hemopoietic Cell-Specific Isoform of the Fyn Tyrosine Protein Kinase, in T cells

Refrences

• Abraham, N., M. C. Miceli, J. C. 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 myristylation and autophosphorylation. Mol. Cell. Biol. 10: 5197–5206.
   PubMed Web of Science ®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
• Appleby, M. W., J. A. Gross, M. P. Cooke, S. D. Levin, X. Qian, and R. M. Perlmutter. 1992. Defective T cell receptor signaling in mice lacking the thymic isoform of p59fyn. Cell 70: 751–763.
   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
• Carder, M., M. W. M. Chang, and C. P. Stanners. 1987. The use of the Escherichia coli gene for asparagine synthetase as a selectable marker in a shuttle vector capable of dominant transfection and amplification in animal cells. Mol. Cell. Biol. 7: 1623–1628.
   PubMedGoogle Scholar
• Cicchetti, P., B. J. Mayer, G. Thiel, 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
• Chow, L. M. L., M. Fournel, D. Davidson, and A. Veillette. 1993. Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk. Nature (London) 365: 156–160.
   PubMed Web of Science ®Google Scholar
• Cooke, M. P., K. M. Abraham, K. A. Forbush, and R. M. Perlmutter. 1991. Regulation of T 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 hemopoietic cells. New Biol. 1: 66–74.
   PubMedGoogle Scholar
• Cooper, J. A. 1990. The src family of protein-tyrosine kinases, p. 85–113. In B. E. Kemp (ed.), Peptides and protein phosphorylation. CRC Press, Inc., Boca Raton, Fla.
   Google Scholar
• Davidson, D., L. M. L. Chow, M. Fournel, and A. Veillette. 1992. Differential regulation of T cell antigen responsiveness by isoforms of the src-related tyrosine protein kinase p59fyn. J. Exp. Med. 175: 1483–1492.
   PubMedGoogle Scholar
• Davidson, D., M. Fournel, and A. Veillette. 1994. Oncogenic activation of p59fyn tyrosine protein kinase by mutation of its carboxyl-terminal site of tyrosine phosphorylation, tyrosine 528. J. Biol. Chem. 269: 10956–10963.
   PubMedGoogle Scholar
• Eck, M. J., S. E. Shoelson, and S. C. Harrison. 1993. Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck. Nature (London) 362: 87–91.
   PubMed Web of Science ®Google Scholar
• Grant, S. G. N., T. J. O'Dell, K. A. Karl, P. L. Stein, P. Soriano, and E. R. Kandel. 1992. Impaired long-term potentiation, spatial learning and hippocampal development in fyn mutant mice. Science 258: 1903–1910.
   PubMed Web of Science ®Google Scholar
• Hanks, S. K., and A. M. Quinn. 1991. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200: 38–81.
   PubMed Web of Science ®Google Scholar
• Heikkila, R., J. B. Trepel, F. Cuttitta, L. M. Neckers, and E. A. Sausville. 1987. Bombesin-related peptides induce calcium mobilization in a subset of human small cell lung cancer cell lines. J. Biol. Chem. 262: 16456–16460.
   PubMed Web of Science ®Google Scholar
• Imboden, J. B., and J. D. Stobo. 1985. Transmembrane signaling by the T cell antigen receptor: perturbation of the T3-antigen receptor complex generates inositol phosphates and releases calcium ions from intracellular stores. J. Exp. Med. 161: 446–456.
   PubMedGoogle Scholar
• Knighton, D. R., J. Zheng, L. F. Ten Eyck, V. A. Ashford, N.-H. Xuong, S. S. Taylor, and J. M. Sodawski. 1991. Crystal structure of the catalytic sub-unit of cyclic adenosine monophosphate-depen-dent protein kinase. Science 253: 407–414.
   PubMed Web of Science ®Google Scholar
• Miller, A. D., and G. J. Rosman. 1989. Improved retroviral vectors for gene transfer and expression. BioTechniques 7: 980–990.
   PubMed Web of Science ®Google Scholar
• Nada, S., M. Okada, A. MacAuley, J. A. Cooper, and H. Nakagawa. 1991. Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature (London) 351: 69–72.
   PubMed Web of Science ®Google Scholar
• Niklinska, B. B., H. Yamada, J. J. O'shea, C. H. June, and J. D. Ashwell. 1992. Tyrosine kinase-regulated and inositol phosphate-independent Ca2+ elevation and mobilization in T cells. J. Biol. Chem. 267: 7154–7159.
   PubMed Web of Science ®Google Scholar
• Okada, M., S. Nada, Y. Yamanashi, T. Yamamoto, and H. Nakagawa. 1991. CSK: a protein-tyrosine kinase involved in regulation of src family kinases. J. Biol. Chem. 266: 24249–24252.
   PubMed Web of Science ®Google Scholar
• Pawson, T., and G. D. Gish. 1992. SH2 and SH3 domains: from structure to function. Cell 71: 359–362.
   PubMed Web of Science ®Google Scholar
• Perlmutter, R. M., S. D. Levin, M. W. Appleby, S. J. Anderson, and J. Alberola-Ila. 1993. Regulation of lymphocyte function by protein phosphorylation. Annu. Rev. Biochem. 11: 451–499.
   Google Scholar
• Putney, J. W.Jr., and G. St. J. Bird. 1993. The signal for capacitative calcium entry. Cell 75: 199–201.
   PubMedGoogle Scholar
• Randriamampita, C., and R. Y. Tsien. 1993. Emptying of intracellular Ca2+ stores releases a novel small messenger that stimulates Ca2+ influx. Nature (London) 364: 809–814.
   PubMed Web of Science ®Google Scholar
• Reske-Kunz, A. B., and E. Rude. 1985. Insulin-specific T cell hybridomas derived from (H-2b × H-2k) F1 mice preferably employ F1-unique restriction elements for antigen recognition. Eur. J. Immunol. 15: 1048–1054.
   PubMedGoogle Scholar
• Samelson, L. E., and R. D. Klausner. 1992. Tyrosine kinases and tyrosine-based activation motifs. Current research on activation via the T cell antigen receptor. J. Biol. Chem. 267: 24913–24916.
   Google Scholar
• Samelson, L. E., A. F. Phillips, E. T. Luong, and R. D. Klausner. 1990. Association of the fyn protein-tyrosine kinase with the T-cell antigen receptor. Proc. Natl. Acad. Sci. USA 87: 4358–4362.
   PubMed Web of Science ®Google Scholar
• Shenoy-Scaria, A. M., L. K. Timson Gauen, J. Kwong, A. S. Shaw, and D. M. Lublin. 1993. Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins. Mol. Cell. Biol. 13: 6385–6392.
   PubMed Web of Science ®Google Scholar
• Staerz, U. D., H. Rammensee, J. D. Benedetto, and M. J. J. Bevan. 1985. Characterization of a murine monoclonal antibody specific for an allotypic determinant on T cell antigen receptor. J. Immunol. 134: 3994–4000.
   PubMed Web of Science ®Google Scholar
• Stein, P. L., H.-M. Lee, S. Rich, and P. Soriano. 1992. pp59fyn mutant mice display differential signaling in thymocytes and peripheral T cells. Cell 70: 741–750.
   PubMed Web of Science ®Google Scholar
• Stewart, S. J., G. R. Cunningham, J. A. Strupp, F. S. House, L. L. Kelley, G. S. Henderson, J. H. Exton, and S. B. Bocckino. 1991. Activation of phospholipase D: a signalling system set in motion by perturbation of the T lymphocyte antigen receptor/CD3 complex. Cell Regul. 2: 841–850.
   PubMedGoogle Scholar
• Sudol, M., H. Greulich, L. Newman, A. Sarkar, J. Sukegawa, and T. Yamamoto. 1993. A novel Yes-related kinase, Yrk, is expressed at elevated levels in neural and hematopoietic tissues. Oncogene 8: 823–831.
   PubMed Web of Science ®Google Scholar
• Takeuchi, M., S. Kuramochi, N. Fusaki, S. Nada, J. Kawamura-Tsuzuku, S. Matsuda, K. Toyoshima, M. Okada, and T. Yamamoto. 1993. Functional and physical interaction of protein-tyrosine kinases Fyn and Csk in the T-cell signalling system. J. Biol. Chem. 268: 27413–27419.
   PubMed Web of Science ®Google Scholar
• Timson Gauen, L. K., A.-N. Tony Kong, L. E. Samelson, and A. S. Shaw. 1992. p59fyn tyrosine kinase associates with multiple T-cell receptor subunits through its unique amino-terminal domain. Mol. Cell. Biol. 12: 5438–5446.
   PubMedGoogle Scholar
• Tsygankov, A. Y., B. M. Broker, J. Fargnoli, J. A. Ledbetter, and J. B. Bolen. 1992. Activation of tyrosine kinase p60fyn following T cell antigen receptor cross-linking. J. Biol. Chem. 267: 18259–18262.
   PubMedGoogle Scholar
• Veillette, A., M. A. Bookman, E. M. Horak, and J. B. Bolen. 1988. The CD4 and CDS T-cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck. Cell 55: 301–308.
   PubMed Web of Science ®Google Scholar
• Veillette, A., and D. Davidson. 1992. Src-related protein tyrosine kinases and T-cell receptor signalling. Trends Genet. 8: 61–66.
   PubMedGoogle Scholar
• Veillette, A., 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
• Waksman, G., S. E. Shoelson, N. Pant, D. Cowburn, and J. Kuriyan. 1993. Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell 72: 1–20.
   Google Scholar
• Weiss, A., and D. R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell 76: 263–294.
   PubMed Web of Science ®Google Scholar
• Yagi, T., S. Aizawa, T. Tokunaga, Y. Shigetani, N. Takeda, and Y. Ikawa. 1993. A role for Fyn tyrosine kinase in the suckling behaviour of neonatal mice. Nature (London) 366: 742–745.
   PubMedGoogle Scholar