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Research Article

The Cytoplasmic Tyrosine Kinase FER Is Associated with the Catenin-Like Substrate pp120 and Is Activated by Growth Factors

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Pages 4553-4561 | Received 21 Mar 1995, Accepted 23 May 1995, Published online: 30 Mar 2023

REFERENCES

  • Areces, L. B., P. Dello Sbarba, M. Jücker, E. R. Stanley, and R. A. Feldman. 1994. Functional specificity of cytoplasmic and transmembrane tyrosine kinases: identification of 130- and 75-kilodalton substrates of c-fps/fes tyrosine kinase in macrophages. Mol. Cell. Biol. 14:4606–4615.
  • Behrens, J., L. Vakaet, R. Friis, E. Winterhager, F. Van Roy, M. M. Mareel, and W. Birchmeier. 1993. Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/β-catenin complex in cells transformed with a temperature-sensitive v-SRC gene. J. Cell Biol. 120:757–766.
  • Bolen, J. B., R. B. Rowley, C. Spana, and A. Y. Tsygankov. 1992. The Src family of tyrosine protein kinases in hemopoietic signal transduction. FASEB J. 6:3403–3409.
  • Burridge, K., C. E. Turner, and L. H. Romer. 1992. Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119:893–903.
  • Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823–832.
  • Chen, W., and B. Obrink. 1991. Cell contacts mediated by E-cadherin (uvo-morulin) restrict invasive behavior of L-cells. J. Cell Biol. 114:319–327.
  • Cohen, C., and D. A. D. Parry. 1994. α-Helical coiled coils: more facts and better predictions. Science 263:488–489.
  • Courtneidge, S. A., A. R. Dhand, D. Pilat, G. M. Twamley, M. D. Waterfield, and M. Roussel. 1993. Activation of Src family kinases by colony stimulating factor 1 and their association with its receptor. EMBO J. 12:943–950.
  • Downing, J. R., and A. B. Reynolds. 1991. PDGF, CSF-1, and EGF induce tyrosine phosphorylation of p120, a pp60src transformation-associated substrate. Oncogene 6:607–613.
  • Eriksson, A., A. Siegbahn, B. Westermark, C.-H. Heldin, and L. Claesson-Welsh. 1992. PDGF α- and β-receptors activate unique and common signal transduction pathways. EMBO J. 11:543–550.
  • Fabricant, R. N., J. E. De Larco, and G. J. Todaro. 1977. Nerve growth factor receptors on human melanoma cells in culture. Proc. Natl. Acad. Sci. USA 74:565–569.
  • Feldman, R. A., J. L. Gabrilove, J. P. Tam, M. A. S. Moore, and H. Hanafusa. 1985. Specific expression of the human cellular fps/fes encoded protein NCP92 in normal and leukemic myeloid cells. Proc. Natl. Acad. Sci. USA 82:2379–2383.
  • Feller, S. F., and T. W. Wong. 1992. Identification and characterization of a cytosolic protein tyrosine kinase of HeLa cells. Biochemistry 31:3044–3051.
  • Frixen, U., J. Behrens, M. Sachs, G. Eberle, B. Voss, A. Warda, D. Lochner, and W. Birchmeier. 1991. E-cadherin mediated cell-cell adhesion prevents invasiveness of human carcinoma cell lines. J. Cell Biol. 117:173–185.
  • Garritsen, A., P. J. M. van Galen, and W. F. Simmonds. 1993. The N-terminal coiled coil domain of β is essential for γ association: a model for G-protein βγ subunit interaction. Proc. Natl. Acad. Sci. USA 90:7706–7710.
  • Geiger, B., and O. Ayalon. 1992. Cadherins. Annu. Rev. Cell Biol. 8:307–332.
  • Gould, K. L., and T. Hunter. 1988. Platelet-derived growth factor induces multisite phosphorylation of pp60c-src and increases its protein tyrosine kinase activity. Mol. Cell. Biol. 8:3345–3356.
  • Greer, P., J. Haigh, G. Mbamalu, W. Khoo, A. Bernstein, and T. Pawson. 1994. The Fps/Fes protein-tyrosine kinase promotes angiogenesis in transgenic mice. Mol. Cell. Biol. 14:6755–6763.
  • Greer, P., V. Maltby, J. Rossant, A. Bernstein, and T. Pawson. 1990. Myeloid expression of the human c-fps/fes proto-oncogene in transgenic mice. Mol. Cell. Biol. 10:2521–2527.
  • Guan, J. L., and D. Shalloway. 1992. Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature (London) 358:690–692.
  • Guan, K., and J. E. Dixon. 1991. Eukaryotic proteins expressed in Esche-richia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal. Biochem. 192:262–267.
  • Hamaguchi, M., N. Matsuyoshi, Y. Ohnishi, B. Gotoh, M. Takeichi, and Y. Nagai. 1993. p60v-src causes tyrosine phosphorylation and inactivation of the N-cadherin-catenin cell adhesion system. EMBO J. 12:307–314.
  • Hanazono, Y., S. Chiba, K. Sasaki, H. Mano, A. Miyajima, K. Arai, Y. Yazaki, and H. Hiral. 1993. c-fps/fes protein-tyrosine kinase is implicated in a signaling pathway triggered by granulocyte-macrophage colony-stimulating factor and interleukin-3. EMBO J. 12:1641–1646.
  • Hanks, S. K., M. B. Calalb, M. C. Harper, and S. K. Patel. 1992. Focal adhesion protein-tyrosine kinase is phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. USA 89:8487–8491.
  • Hao, Q. L., N. Heisterkamp, and J. Groffen. 1989. Isolation and sequence analysis of a novel human tyrosine kinase gene. Mol. Cell. Biol. 9:1587–1593.
  • Hinck, L., I. S. Nathke, J. Papkoff, and W. J. Nelson. 1994. Dynamics of cadherin/catenin complex formation: novel protein interactions and pathways of complex assembly. J. Cell Biol. 125:1327–1340.
  • Hjermstad, S. J., K. L. Peters, S. D. Briggs, R. I. Glazer, and T. E. Smithgall. 1993. Regulation of the human c-fes protein tyrosine kinase (p93 c-fes) by its src homology 2 domain and major autophosphorylation site (Tyr-713). Oncogene 8:2283–2292.
  • Hoschuetzky, H., H. Aberle, and R. Kemler. 1994. β-Catenin mediates the interaction of the cadherin-catenin complex with epidermal growth factor receptor. J. Cell Biol. 127:1375–1380.
  • Ihle, J. N., B. A. Witthuhn, F. W. Quelle, K. Yamamoto, W. E. Thierfelder, B. Kreider, and O. Silvennoinen. 1994. Signaling by the cytokine receptor superfamily: JAKs and STATs. Trends Biochem. Sci. 19:222–227.
  • Izuhara, K., R. A. Feldman, P. Greer, and N. Harada. 1994. Interaction of the c-fes proto-oncogene product with the interleukin-4 receptor. J. Biol. Chem. 269:18623–18629.
  • Kanner, S. B., A. B. Reynolds, and J. T. Parsons. 1991. Tyrosine phosphor-ylation of a 120-kilodalton pp60src substrate upon epidermal growth factor and platelet-derived growth factor receptor stimulation and in polyomavirus middle-T-antigen transformed cells. Mol. Cell. Biol. 11:713–720.
  • Kanner, S. B., A. B. Reynolds, R. R. Vines, and J. T. Parsons. 1990. Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc. Natl. Acad. Sci. USA 87:3328–3332.
  • Koch, C. A., M. 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.
  • Kornberg, L., H. S. Earp, J. T. Parsons, M. Schaller, and R. L. Juliano. 1992. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated protein kinase. J. Biol. Chem. 267:23439–23442.
  • Kypta, R. M., Y. Goldberg, E. T. Ulug, and S. A. Courtneidge. 1990. Asso ciation between the PDGF receptor and members of the src family of tyrosine kinases. Cell 62:481–492.
  • Letwin, K., S.-P. Yee, and T. Pawson. 1988. Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned using anti-phosphotyrosine antibody. Oncogene 3:621–627.
  • Lipfert, L., B. Haimovich, M. D. Schaller, B. S. Cobb, J. T. Parsons, and J. B. Brugge. 1992. Integrin-dependent phosphorylation and activation of the protein tyrosine kinase pp125FAK in platelets. J. Cell Biol. 119:905–912.
  • Lupas, A., J. M. Lupas, and J. B. Stock. 1992. Do G protein subunits associate via a three-stranded coiled coil? FEBS Lett. 314:105–108.
  • Lupas, A., M. Van Dyke, and J. Stock. 1991. Predicting coiled coils from protein sequences. Science 252:1162–1164.
  • MacDonald, I., J. Levy, and T. Pawson. 1985. Expression of the mammalian c-fes protein in hematopoietic cells and identification of a distinct fes-related protein. Mol. Cell. Biol. 5:2543–2551.
  • Manfredini, R., A. Grande, E. Tagliafico, D. Barbieri, P. Zucchini, G. Citro, G. Zupi, C. Franceschi, U. Torelli, and S. Ferrari. 1993. Inhibition of c-fes expression by an antisense oligomer causes apoptosis of HL60 cells induced to granulocytic differentiation. J. Exp. Med. 178:381–389.
  • Maru, Y., K. L. Peters, D. E. H. Afar, M. Shibuya, O. N. Witte, and T. E. Smithgall. 1995. Tyrosine phosphorylation of BCR by FPS/FES protein-tyrosine kinases induces association of BCR with GRB-2/SOS. Mol. Cell. Biol. 15:835–842.
  • Matsuyoshi, N., M. Hamaguchi, S. Taniguchi, A. Nagafuchi, S. Tsukita, S. Tsukita, and M. Takeichi. 1992. Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts. J. Cell Biol. 118:703–714.
  • Nathke, I., L. Hinck, J. R. Swedlow, J. Papkoff, and W. J. Nelson. 1994. Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells. J. Cell Biol. 125:1341–1352.
  • O'Shea, E. K., J. D. Klemm, P. S. Kim, and T. Alber. 1991. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254:539–544.
  • Pawson, T. 1995. Protein modules and signalling networks. Nature (London) 373:573–580.
  • Peifer, M., S. Berg, and A. B. Reynolds. 1994. A repeating amino acid motif shared by proteins with diverse cellular roles. Cell 76:789–791.
  • Perez, J., X. Shen, S. Finkernagel, L. Sciorra, N. A. Jenkins, D. J. Gilbert, N. G. Copeland, and T. W. Wong. 1994. Identification and chromosomal mapping of a receptor tyrosine kinase with a putative phospholipid binding sequence in its ectodomain. Oncogene 9:211–219.
  • Ponzetto, C., A. Bardelli, Z. Chen, F. Maina, P. dalla Zonca, S. Giordano, A. Graziani, G. Panayotou, and P. M. Comoglio. 1994. A multifunctional docking site mediates signaling and transformation by the hepatocyte growth factor/scatter factor receptor family. Cell 77:261–271.
  • Reynolds, A. B., J. Daniel, P. McCrea, M. J. Wheelock, J. Wu, and Z. Zhang. 1994. Identification of a new catenin: the tyrosine kinase substrate p120cas associates with E-cadherin complexes. Mol. Cell. Biol. 14:8333–8342.
  • Reynolds, A. B., L. Herbert, J. L. Cleveland, S. T. Berg, and J. R. Gaut. 1992. p120, a novel substrate of protein tyrosine kinase receptors and of p60c-src, is related to cadherin-binding factors β-catenin, plakoglobin and armadillo. Oncogene 7:2439–2445.
  • Rubinfeld, B., B. Souza, I. Albert, O. Muller, S. H. Chamberlain, R. R. Masiarz, S. Munemitsu, and P. Polakis. 1993. Association of the APC gene product with β-catenin. Science 262:1731–1734.
  • Ruff-Jamison, S., K. Chen, and S. Cohen. 1993. Induction by EGF and interferon gamma of tyrosine phosphorylated DNA binding proteins in mouse liver nuclei. Science 261:1733–1736.
  • Scheller, M. D., A. H. Bouton, D. C. Flynn, and J. T. Parsons. 1993. Purifi-cation and characterization of novel substrates of protein tyrosine kinases. Prog. Nucleic Acid Res. 44:205–227.
  • Schlaepfer, D. D., S. K. Hanks, T. Hunter, and P. van der Geer. 1994. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature (London) 372:786–791.
  • Seifert, R. A., C. E. Hart, P. E. Phillips, J. W. Forstrom, R. Ross, M. J. Murray, and D. F. Bowen-Pope. 1989. Two different subunits associate to create isoform-specific platelet derived growth factor receptors. J. Biol. Chem. 264:8771–8778.
  • Soler, C., L. Beguinot, A. Sorkin, and G. Carpenter. 1993. Tyrosine phos-phorylation of ras GTPase-activating protein does not require association with the epidermal growth factor receptor. J. Biol. Chem. 268:22010–22019.
  • Su, L.-K., B. Vogelstein, and K. W. Kinzler. 1993. Association of the APC tumor suppressor protein with catenins. Science 262:1734–1736.
  • Weinmaster, G., M. J. Zoller, M. Smith, E. Hinze, and T. Pawson. 1984. Mutagenesis of Fujinami sarcoma virus: evidence that tyrosine phosphory-lation modulates its biological activity. Cell 37:559–568.

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