A Truncated K-sam Product Lacking the Distal Carboxyl-Terminal Portion Provides a Reduced Level of Autophosphorylation and Greater Resistance against Induction of Differentiation

REFERENCES

• Adamou, J., and J. Bag. 1992. Alteration of translation and stability of mRNA for the poly(A)-binding protein during myogenesis. Eur. J. Biochem. 209:803–812.
   PubMedGoogle Scholar
• Akiyama, T., S. Matsuda, Y. Namba, T. Saito, K. Toyoshima, and T. Yamamoto. 1991. The transforming potential of the c-erbB-2 protein is regulated by its autophosphorylation at the carboxyl-terminal domain. Mol. Cell. Biol. 11:833–842.
   PubMedGoogle Scholar
• Caravatti, M., A. Minty, B. Robert, D. Montarras, A. Weydert, A. Cohen, P. Daubas, and M. Buckingham. 1982. Regulation of muscle gene expression. The accumulation of messenger RNAs coding for muscle-specific proteins during myogenesis in a mouse cell line. J. Mol. Biol. 160:59–76.
   Google Scholar
• Champion-Arnaud, P., C. Ronsin, E. Gilbert, M. C. Gesnel, E. Houssaint, and R. Breathnach. 1991. Multiple mRNAs code for proteins related to the BEK fibroblast growth factor receptor. Oncogene 6:979–987.
   PubMedGoogle Scholar
• Clegg, C. H., T. A. Linkhart, B. B. Olwin, and S. D. Hauschka. 1987. Growth factor control of skeletal muscle differentiation: commitment to terminal differentiation occurs in G1 phase and is repressed by fibroblast growth factor. J. Cell Biol. 105:949–956.
   PubMed Web of Science ®Google Scholar
• Crumley, G., F. Bellot, J. M. Kaplow, J. Schlessinger, M. Jaye, and C. A. Dionne. 1991. High-affinity binding and activation of a truncated FGF receptor by both aFGF and bFGF. Oncogene 6:2255–2262.
   PubMedGoogle Scholar
• Dionne, C. A., G. Crumley, F. Bellot, J. M. Kaplow, G. Searfoss, M. Ruta, W. H. Burgess, M. Jaye, and J. Schlessinger. 1990. Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors. EMBO J. 9:2685–2692.
   PubMed Web of Science ®Google Scholar
• Finch, P. W., J. S. Rubin, T. Miki, D. Ron, and S. A. Aaronson. 1989. Human KGF is FGF-related with properties of a paracrine effector of epithelial cell growth. Science 245:752–755.
   PubMed Web of Science ®Google Scholar
• Florini, J. R., and D. Z. Ewton. 1988. Actions of transforming growth factor-β on muscle cells. J. Cell. Physiol. 135:301–308.
   PubMedGoogle Scholar
• Gotoh, N., A. Tojo, K. Muroya, Y. Hashimoto, S. Hattori, S. Nakamura, T. Takenawa, Y. Yazaki, and M. Shibuya. 1994. Epidermal growth factor-receptor mutant lacking the autophosphorylation sites induces phosphory-lation of Sch protein and Sch-Grb2/ASH association and retains mitogenic activity. Proc. Natl. Acad. Sci. USA 91:167–171.
   PubMedGoogle Scholar
• Hattori, Y., and T. Masaaki. Unpublished data.
   Google Scholar
• Hattori, Y., H. Odagiri, O. Katoh, H. Sakamoto, T. Motita, K. Shimotohno, K. Tobinai, T. Sugimura, and M. Terada. 1992. K-sam-related-gene, N-sam, encodes fibroblast growth factor receptor and is expressed in T-lymphocytic tumors. Cancer Res. 52:3367–3371.
   PubMedGoogle Scholar
• Hattori, Y., H. Odagiri, H. Nakatani, K. Miyagawa, K. Naito, H. Sakamoto, O. Katoh, T. Yoshida, T. Sugimura, and M. Terada. 1990. K-sam, an amplified gene in stomach cancer, is a member of the heparin-binding growth factor receptor genes. Proc. Natl. Acad. Sci. USA 87:5983–5987.
   PubMed Web of Science ®Google Scholar
• Iida, S., O. Katoh, A. Tokunaga, and M. Terada. 1994. Expression of fibroblast growth factor gene family and its receptor gene family in the human upper gastrointestinal tract. Biochem. Biophys. Res. Commun. 199:1113–1119.
   PubMed Web of Science ®Google Scholar
• Ishii, H., Y. Hattori, H. Itoh, T. Kishi, T. Yoshida, H. Sakamoto, H. Oh, S. Yoshida, T. Sugimura, and M. Terada. 1994. Preferential expression of the third immunoglobulin-like domain of K-sam product provides keratinocyte growth factor-dependent growth in carcinoma cell lines. Cancer Res. 54:518–522.
   PubMedGoogle Scholar
• Ishii, H., and M. Terada. Unpublished data.
   Google Scholar
• Itoh, H., Y. Hattori, H. Sakamoto, H. Ishii, T. Kishi, H. Sasaki, T. Yoshida, M. Koono, T. Sugimura, and M. Terada. 1994. Preferential alternative splicing in cancer generates a K-sam messenger RNA with higher transforming activity. Cancer Res. 54:3237–3241.
   PubMed Web of Science ®Google Scholar
• Izuhara, K., and N. Harada. 1993. Interleukin-4 (IL-4) induces protein tyrosine phosphorylation of the IL-4 receptor and association of phosphati-dylinositol 3-kinase to the IL-4 receptor in a mouse T cell line, HT2. J. Biol. Chem. 268:13097–13102.
   PubMedGoogle Scholar
• Jamieson, J. C., S. Wayne, and R. S. Belo. 1992. The importance of N-linked glycoproteins and dolichyl phosphate synthesis for fusion of L6 myoblasts. Biochem. Cell Biol. 70:408–412.
   PubMedGoogle Scholar
• Jaye, M., J. Schlessinger, and C. A. Dionne. 1992. Fibroblast growth factor receptor tyrosine kinases: molecular analysis and signal transduction. Bio-chim. Biophys. Acta 1135:185–199.
   PubMed Web of Science ®Google Scholar
• Johnson, D. E., J. Lu, H. Chen, S. Werner, and L. T. Williams. 1991. The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain. Mol. Cell. Biol. 11:4627–4634.
   PubMed Web of Science ®Google Scholar
• Johnson, D. E., and L. T. Williams. 1993. Structural and functional diversity in the FGF receptor multigene family. Adv. Cancer Res. 60:1–41.
   PubMed Web of Science ®Google Scholar
• Katoh, M., Y. Hattori, H. Sasaki, M. Tanaka, K. Sugano, Y. Yazaki, T. Sugimura, and M. Terada. 1992. K-sam gene encodes secreted as well as transmembrane receptor tyrosine kinase. Proc. Natl. Acad. Sci. USA 89: 2960–2964.
   PubMed Web of Science ®Google Scholar
• Katoh, O., Y. Hattori, H. Sasaki, H. Sakamoto, K. Fujimoto, T. Fujii, T. Sugimura, and M. Terada. 1993. Isolation of the complementary DNA encoding a mouse heparin-binding growth factor receptor with the use of a unique kinase insert sequence. Cancer Res. 53:1136–1141.
   PubMedGoogle Scholar
• Kingston, R. E. 1987. Introduction of DNA into mammmalian cells, p. 9.0.1–9.9.3. In F. M. Ausubel, R. Brent, and R. E. Kingston (ed.), Current protocols in molecular biology. John Wiley & Sons, Inc., New York.
   Google Scholar
• Kishi, T., T. Yoshida, and M. Terada. 1994. A soluble form of K-sam/FGFR2 protein in the culture medium of human gastric cancer cells. Biochem. Biophys. Res. Commun. 202:1387–1394.
   PubMedGoogle Scholar
• Miki, T., D. P. Bottaro, T. P. Fleming, C. L. Smith, W. H. Burgess, A. M.-L. Chan, and S. A. Aaronson. 1992. Determination of ligand-binding specificity by alternative splicing: two distinct growth factor receptors encoded by a single gene. Proc. Natl. Acad. Sci. USA 89:246–250.
   PubMed Web of Science ®Google Scholar
• Miyagawa, K., H. Sakamoto, T. Yoshida, Y. Yamashita, Y. Mitsui, M. Fu-rusawa, S. Maeda, F. Takaku, T. Sugimura, and M. Terada. 1988. hst-1 transforming protein: expression in silkworm cells and characterization as a novel heparin-binding growth factor. Oncogene 3:383–389.
   PubMed Web of Science ®Google Scholar
• Mohammadi, M., C. A. Dionne, W. Li, N. Li, T. Spivak, A. M. Honegger, M. Jaye, and J. Schlessinger. 1992. Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis. Nature (London) 358:681–684.
   PubMed Web of Science ®Google Scholar
• Mohammadi, M., A. M. Honegger, D. Rotin, R. Fischer, F. Bellot, W. Li, C. A. Dionne, M. Jaye, M. Rubinstein, and J. Schlessinger. 1991. A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-γ1. Mol. Cell. Biol. 11:5068–5078.
   PubMed Web of Science ®Google Scholar
• Nadal-Ginard, B. 1978. Commitment, fusion and biochemical differentiation of a myogenic cell line in the absence of DNA synthesis. Cell 15:855–864.
   PubMed Web of Science ®Google Scholar
• Nakatani, H., H. Sakamoto, T. Yoshida, J. Yokota, E. Tahara, T. Sugimura, and M. Terada. 1990. Isolation of an amplified DNA sequence in stomach cancer. Jpn. J. Cancer Res. 81:707–710.
   PubMedGoogle Scholar
• Nakatani, H., E. Tahara, T. Yoshida, H. Sakamoto, T. Suzuki, H. Watanabe, M. Sekiguchi, Y. Kaneko, M. Sakurai, M. Terada, and T. Sugimura. 1986. Detection of amplified DNA sequences in gastric cancers by a DNA rena-turation method in gel. Jpn. J. Cancer Res. 77:849–853.
   PubMedGoogle Scholar
• Nudel, U., D. Zuk, P. Einat, E. Zeelon, Z. Levy, S. Neuman, and D. Yaffe. 1989. Duchenne muscular dystrophy gene product is not identical in muscle and brain. Nature (London) 337:76–78.
   PubMed Web of Science ®Google Scholar
• Pampusch, M. S., J. R. Hembree, M. R. Hathaway, and W. R. Dayton. 1990. Effect of transforming growth factor beta on proliferation of L6 and embryonic porcine myogenic cells. J. Cell. Physiol. 143:524–528.
   PubMed Web of Science ®Google Scholar
• Parfett, C. L. J., J. C. Jamieson, and J. A. Wright. 1981. A correlation between loss of fusion potential and defective formation of mannose-linked lipid intermediates in independent concanavalin A-resistant myoblast cell lines. Exp. Cell Res. 136:1–14.
   PubMedGoogle Scholar
• Peters, K. G., J. Marie, E. Wilson, H. E. Ives, J. Escobedo, M. Del Rosario, D. Mirda, and L. T. Williams. 1992. Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca21 flux but not mitogenesis. Nature (London) 358:678–681.
   PubMed Web of Science ®Google Scholar
• Rao, S., C. Chu, and D. S. Kohtz. 1994. Ectopic expression of cyclin D1 prevents activation of gene transcription by myogenic basic helix-loop-helix regulators. Mol. Cell. Biol. 14:5259–5267.
   PubMedGoogle Scholar
• Sakamoto, H., M. Mori, M. Taira, T. Yoshida, S. Matsukawa, K. Shimizu, M. Sekiguchi, M. Terada, and T. Sugimura. 1986. Transforming gene from human stomach cancers and a noncancerous portion of stomach mucosa. Proc. Natl. Acad. Sci. USA 83:3997–4001.
   PubMed Web of Science ®Google Scholar
• Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Sherr, C. J. 1993. Mammalian G1 cyclins. Cell 73:1059–1065.
   PubMed Web of Science ®Google Scholar
• Sorokin, A., M. Mohammadi, J. Huang, and J. Schlessinger. 1994. Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766. J. Biol. Chem. 269:17056–17061.
   PubMed Web of Science ®Google Scholar
• Spearman, M. A., J. C. Jamieson, and J. A. Wright. 1987. Studies on the effect of glycoprotein processing inhibitors on fusion of L6 myoblast cell lines. Exp. Cell Res. 168:116–126.
   PubMedGoogle Scholar
• Spizz, G., D. Roman, A. Strauss, and E. N. Olson. 1986. Serum and fibroblast growth factor inhibit myogenic differentiation through a mechanism dependent on protein synthesis and independent of cell proliferation. J. Biol. Chem. 261:9483–9488.
   PubMed Web of Science ®Google Scholar
• Thinakaran, G., J. Ojala, and J. Bag. 1993. Expression of c-jun/AP-1 during myogenic differentiation in mouse C2C12 myoblasts. FEBS Lett. 319:271–276.
   PubMedGoogle Scholar
• Tsuruta, H., H. Sakamoto, M. Onda, and M. Terada. 1993. Amplification and overexpression of EXP1 and EXP2/cyclin D1 genes in human esophageal carcinomas. Biochem. Biophys. Res. Commun. 196:1529–1536.
   PubMedGoogle Scholar
• Yayon, A., Y. Zimmer, S. Guo-Hong, A. Avivi, Y. Yarden, and D. Givol. 1992. A confined variable region confers ligand specificity on fibroblast growth factor receptors: implications for the origin of the immunoglobulin fold. EMBO J. 11:1885–1890.
   PubMedGoogle Scholar
• Zimmer, Y., D. Givol, and A. Yayon. 1993. Multiple structural elements determine ligand binding of fibroblast growth factor receptors. J. Biol. Chem. 268:7899–7903.
   PubMedGoogle Scholar