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Research Article

Conformational Changes Induced in the Protein Tyrosine Kinase p72syk by Tyrosine Phosphorylation or by Binding of Phosphorylated Immunoreceptor Tyrosine-Based Activation Motif Peptides

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Pages 1471-1478 | Received 05 Sep 1995, Accepted 23 Jan 1996, Published online: 29 Mar 2023

REFERENCES

  • Backer, J. M., M. G. Myers, Jr., S. E. Shoelson, D. J. Chin, X. J. Sun, M. Miralpeix, P. Hu, B. Margolis, E. Y. Skolnik, and J. Schlessinger. 1992. Phosphatidylinositol 3′-kinase is activated by association with IRS-1 during insulin stimulation. EMBO J. 11:3469–3479.
  • Barsumian, E. L., C. Isersky, M. G. Petrino, and R. P. Siraganian. 1981. IgE-induced histamine release from rat basophilic leukemia cell lines: isolation of releasing and nonreleasing clones. Eur. J. Immunol. 11:317–323.
  • Basciano, L. K., E. H. Berenstein, L. Kmak, and R. P. Siraganian. 1986. Monoclonal antibodies that inhibit IgE binding. J. Biol. Chem. 261:11823–11831.
  • Beaven, M. A., and H. Metzger. 1993. Signal transduction by Fc receptors: the FcεRI case. Immunol. Today 14:222–226.
  • Benhamou, M., J. S. Gutkind, K. C. Robbins, and R. P. Siraganian. 1990. Tyrosine phosphorylation coupled to IgE receptor-mediated signal transduction and histamine release. Proc. Natl. Acad. Sci. USA 87:5327–5330.
  • Benhamou, M., N. J. P. Ryba, H. Kihara, H. Nishikata, and R. P. Siraganian. 1993. Protein-tyrosine kinase p72syk in high affinity IgE receptor signaling. Identification as a component of pp72 and association with the receptor γ chain. J. Biol. Chem. 268:23318–23324.
  • Benhamou, M., and R. P. Siraganian. 1992. Protein-tyrosine phosphorylation: an essential component of FcεRI signaling. Immunol. Today 13:195–197.
  • Bishayee, S., S. Majumdar, C. D. Scher, and S. Khan. 1988. Characterization of a novel anti-peptide antibody that recognizes a specific conformation of the platelet-derived growth factor receptor. Mol. Cell. Biol. 8:3696–3702.
  • Blank, U., C. Ra, L. Miller, K. White, H. Metzger, and J. P. Kinet. 1989. Complete structure and expression in transfected cells of high affinity IgE receptor. Nature (London) 337:187–189.
  • Cambier, J. C., C. M. Pleiman, and M. R. Clark. 1994. Signal transduction by the B cell antigen receptor and its coreceptors. Annu. Rev. Immunol. 12:457–486.
  • Carpenter, C. L., K. R. Auger, M. Chanudhuri, M. Yoakim, B. Schaffhausen, S. Shoelson, and L. C. Cantley. 1993. Phosphoinositide 3-kinase is activated by phosphopeptides that bind to the SH2 domains of the 85-kDa subunit. J. Biol. Chem. 268:9478–9483.
  • Chan, A. C., D. M. Desai, and A. Weiss. 1994. The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu. Rev. Immunol. 12:555–592.
  • 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.
  • Chan, A. C., M. Iwashima, C. W. Turck, and A. Weiss. 1992. ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR ζ chain. Cell 71:649–662.
  • Cooper, J. A., and A. Kashishian. 1993. In vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinase. Mol. Cell. Biol. 13:1737–1745.
  • Couture, C., G. Baier, A. Altman, and T. Mustelin. 1994. p56Ick -independent activation and tyrosine phosphorylation of p72syk by T-cell antigen receptor/ CD3 stimulation. Proc. Natl. Acad. Sci. USA 91:5301–5305.
  • Eiseman, E., and J. B. Bolen. 1992. Signal transduction by the cytoplasmic domains of FcεRIγ and TCR-ζ in rat basophilic leukemia cells. J. Biol. Chem. 267:21027–21032.
  • Garcia, P., S. E. Shoelson, J. S. Drew, and W. T. Miller. 1994. Phosphopeptide occupancy and photoaffinity cross-linking of the v-Src SH2 domain attenuates tyrosine kinase activity. J. Biol. Chem. 269:30574–30579.
  • Hutchcroft, J. E., R. L. Geahlen, G. G. Deanin, and J. M. Oliver. 1992. FcεRI-mediated tyrosine phosphorylation and activation of the 72-kDa protein-tyrosine kinase, PTK72, in RBL-2H3 rat tumor mast cells. Proc. Natl. Acad. Sci. USA 89:9107–9111.
  • Hutchcroft, J. E., M. L. Harrison, and R. L. Geahlen. 1992. Association of the 72-kDa protein-tyrosine kinase PTK72 with the B cell antigen receptor. J. Biol. Chem. 267:8613–8619.
  • Irving, B. A., A. C. Chan, and A. Weiss. 1993. Functional characterization of a signal transducing motif present in the T cell antigen receptor ζ chain. J. Exp. Med. 177:1093–1103.
  • Irving, B. A., and A. Weiss. 1991. The cytoplasmic domain of the T cell receptor ζ chain is sufficient to couple to receptor-associated signal transduction pathways. Cell 64:891–901.
  • Iwashima, M., B. A. Irving, N. S. C. Van Oers, A. C. Chan, and A. Weiss. 1994. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science 263:1136–1139.
  • Jouvin, M. H. E., M. Adamczewski, R. Numerof, O. Letourneur, A. Valle, and J. P. Kinet. 1994. Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor. J. Biol. Chem. 269:5918–5925.
  • Kamps, M. P., and B. M. 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.
  • Kashishian, A., A. Kazlauskas, and J. A. Cooper. 1992. Phosphorylation sites in the PDGF receptor with different specificities for binding GAP and PI3 kinase in vivo. EMBO J. 11:1373–1382.
  • Keating, M. T., J. A. Escobedo, and L. T. Williams. 1988. Ligand activation causes a phosphorylation-dependent change in platelet-derived growth factor receptor conformation. J. Biol. Chem. 263:12805–12808.
  • Kihara, H., and R. P. Siraganian. 1994. Src homology 2 domains of Syk and Lyn bind to tyrosine-phosphorylated subunits of the high affinity IgE receptor. J. Biol. Chem. 269:22427–22432.
  • Kimura, T., J. Zhang, and R. P. Siraganian. Unpublished observations.
  • Kinet, J. P., U. Blank, C. Ra, K. White, H. Metzger, and J. Kochan. 1988. Isolation and characterization of cDNAs coding for the beta subunit of the high-affinity receptor for immunoglobulin E. Proc. Natl. Acad. Sci. USA 85:6483–6487.
  • Koch, C. A., 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.
  • Kolanus, W., C. Romeo, and B. Seed. 1993. T cell activation by clustered tyrosine kinases. Cell 74:171–183.
  • Koyasu, S., A. G. D. Tse, P. Moingeon, R. E. Hussey, A. Mildonian, J. Hannisian, L. K. Clayton, and E. L. Reinherz. 1994. Delineation of a T-cell activation motif required for binding of protein tyrosine kinases containing tandem SH2 domains. Proc. Natl. Acad. Sci. USA 91:6693–6697.
  • Lechleider, R. J., S. Sugimoto, A. M. Bennett, A. S. Kashishian, J. A. Cooper, S. E. Shoelson, C. T. Walsh, and B. G. Neel. 1993. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor β. J. Biol. Chem. 268:21478–21481.
  • Letourneur, F., and R. D. Klausner. 1991. T-cell and basophil activation through the cytoplasmic tail of T-cell-receptor ζ family proteins. Proc. Natl. Acad. Sci. USA 88:8905–8909.
  • MacAuley, A., and J. A. Cooper. 1989. Structural differences between repressed and derepressed forms of p60c-src. Mol. Cell. Biol. 9:2648–2656.
  • Madrenas, J., R. L. Wange, J. L. Wang, N. Isakov, L. E. Samelson, and R. N. Germain. 1995. ζ phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists. Science 267:515–518.
  • Mayer, B. J., and D. Baltimore. 1993. Signalling through SH2 and SH3 domains. Trends Cell Biol. 3:8–13.
  • Minoguchi, K., M. Benhamou, W. D. Swaim, Y. Kawakami, T. Kawakami, and R. P. Siraganian. 1994. Activation of protein tyrosine kinase p72syk by FcεRI aggregation in rat basophilic leukemia cells: p72syk is a minor component but the major protein tyrosine kinase of pp72. J. Biol. Chem. 269:16902–16908.
  • Minoguchi, K., H. Kihara, H. Nishikata, M. M. Hamawy, and R. P. Siraganian. 1994. Src family tyrosine kinase Lyn binds several proteins including paxillin in rat basophilic leukemia cells. Mol. Immunol. 31:519–529.
  • Ottinger, E. A., L. L. Shekels, D. A. Bernlohr, and G. Barany. 1993. Synthesis of phosphotyrosine-containing peptides and their use as substrates for protein tyrosine phosphatases. Biochemistry 32:4354–4361.
  • Panayotou, G., B. Bax, I. Gout, M. Federwisch, B. Wroblowski, R. Dhand, M. J. Fry, T. L. Blundell, A. Wollmer, and M. D. Waterfield. 1992. Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes. EMBO J. 11:4261–4272.
  • Pei, D., U. Lorenz, U. Klingmueller, B. G. Neel, and C. T. Walsh. 1994. Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains. Biochemistry 33:15483–15493.
  • Reth, M. 1989. Antigen receptor tail clue. Nature (London) 338:383–384.
  • Romeo, C., M. Amiot, and B. Seed. 1992. Sequence requirements for induction of cytolysis by the T cell antigen/Fc receptor ζ chain. Cell 68:889–897.
  • Romeo, C., and B. Seed. 1991. Cellular immunity to HIV activated by CD4 fused to T cell or Fc receptor polypeptides. Cell 64:1037–1046.
  • Rowley, R. B., A. L. Burkhardt, H. G. Chao, G. R. Matsueda, and J. B. Bolen. 1995. Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Igα/Igβ immunoreceptor tyrosine activation motif binding and autophos-phorylation. J. Biol. Chem. 270:11590–11594.
  • 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.
  • Shiue, L., J. Green, O. M. Green, J. L. Karas, J. P. Morgenstern, M. K. Ram, M. K. Taylor, M. J. Zoller, L. D. Zydowsky, J. B. Bolen, and J. S. Brugge. 1995. Interaction of p72syk with the γ and β subunits of the high-affinity receptor for immunoglobulin E, FcεRI. Mol. Cell. Biol. 15:272–281.
  • Shiue, L., M. J. Zoller, and J. S. Brugge. 1995. Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE. J. Biol. Chem. 270:10498–10502.
  • Shoelson, S. E., M. Sivaraja, K. P. Williams, P. Hu, J. Schlessinger, and M. A. Weiss. 1993. Specific phosphopeptide binding regulates a conformational change in the PI 3-kinase SH2 domain associated with enzyme activation. EMBO J. 12:795–802.
  • Sloan-Lancaster, J., A. S. Shaw, J. B. Rothbard, and P. M. Allen. 1994. Partial T cell signaling: altered phospho-ζ and lack of ZAP-70 recruitment in APL-induced T cell anergy. Cell 79:913–922.
  • Stephan, V., M. Benhamou, J. S. Gutkind, K. C. Robbins, and R. P. Siraganian. 1992. FcεRI-induced protein tyrosine phosphorylation of pp72 in rat basophilic leukemia cells (RBL-2H3). Evidence for a novel signal transduction pathway unrelated to G protein activation and phosphatidylinositol hydrolysis. J. Biol. Chem. 267:5434–5441.
  • Stracke, M. L., L. K. Basciano, C. Fischler, E. H. Berenstein, and R. P. Siraganian. 1987. Characterization of monoclonal antibodies produced by immunization with partially purified IgE receptor complexes. Mol. Immunol. 24:347–356.
  • Sugimoto, S., T. J. Wandless, S. E. Shoelson, B. G. Neel, and C. T. Walsh. 1994. Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1. J. Biol. Chem. 269:13614–13622.
  • Taniguchi, T., T. Kobayashi, J. Kondo, K. Takahashi, H. Nakamura, J. Suzuki, K. Nagai, T. Yamada, S. Nakamura, and H. Yamamura. 1991. Molecular cloning of a porcine gene syk that encodes a 72-kDa protein-tyrosine kinase showing high susceptibility to proteolysis. J. Biol. Chem. 266:15790–15796.
  • Van Oers, N. S. C., N. Killeen, and A. Weiss. 1994. ZAP-70 is constitutively associated with tyrosine-phosphorylated TCR ζ in murine thymocytes and lymph node T cells. Immunity 1:675–685.
  • Wange, R. L., S. N. Malek, S. Desiderio, and L. E. Samelson. 1993. Tandem SH2 domains of ZAP-70 bind to T cell antigen receptor ζ and CD3ε from activated Jurkat T cells. J. Biol. Chem. 268:19797–19801.
  • Weiss, A. 1993. T cell antigen receptor signal transduction: a tale of tails and cytoplasmic protein-tyrosine kinases. Cell 73:209–212.

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