3
Views
16
CrossRef citations to date
0
Altmetric
Research Article

Oncogenic Activation of p185neu Stimulates Tyrosine Phosphorylation In Vivo

, &
Pages 3969-3973 | Received 18 Apr 1988, Accepted 14 Jun 1988, Published online: 31 Mar 2023

LITERATURE CITED

  • Akiyama, T., T. Saito, H. Ogawara, K. Toyoshima, and T. Yamamoto. 1988. Tumor promoter and epidermal growth factor stimulate phosphorylation of the c-erbB-2 gene product in MKN-7 human adenocarcinoma cells. Mol. Cell. Biol. 8:1019–1026.
  • Akiyama, T., C. Sudo, H. Ogawara, K. Toyoshima, and T. Yamamoto. 1986. The product of the human c-erbB-2 gene: a 185-kilodalton glycoprotein with tyrosine kinase activity. Science 232:1644–1646.
  • Bargmann, C. I., M.-C. Hung, and R. A. Weinberg. 1986. Multiple independent activations of the neu oncogene by a point mutation altering the transmembrane domain of pl85. Cell 45:649–657.
  • Bargmann, C. I., M.-C. Hung, and R. A. Weinberg. 1986. The neu oncogene encodes an epidermal growth factor receptor-related protein. Nature (London) 319:226–230.
  • Bertics, P. J., and G. N. Gill. 1985. Self-phosphorylation enhances the protein-tyrosine kinase activity of the epidermal growth factor receptor. J. Biol. Chem. 260:14642–14647.
  • Brown, D. J., and J. A. Gordon. 1984. The stimulation of pp60v-src kinase activity by vanadate in intact cells accompanies a new phosphorylation state of the enzyme. J. Biol. Chem. 259:9580–9586.
  • Carlin, C. R., and B. B. Knowles. 1984. Biosynthesis of the epidermal growth factor receptor in human epidermoid carcinoma-derived A431 cells. J. Biol. Chem. 259:7902–7098.
  • Collett, M. S., S. K. Belzer, and A. F. Purchio. 1984. Structurally and functionally modified forms of pp60v-src in Rous sarcoma virus-transformed cell lysates. Mol. Cell. Biol. 4:1213–1220.
  • Cooper, J. A., B. M. Sefton, and T. H. Hunter. 1983. Detection and quantification of phosphotyrosine in proteins. Methods Enzymol. 99:387–402.
  • Courtneidge, S. A. 1985. Activation of pp60c-src kinase by middle T antigen binding or by dephosphorylation. EMBO J. 4:1471–1477.
  • Coussens, L., T. L. Yang-Feng, Y.-C. Liao, E. Chen, A. Gray, J. McGrath, P. H. Seeburg, T. A. Libermann, J. Schlessinger, U. Francke, A. Levinson, and A. Ullrich. 1985. Tyrosine kinase receptor with extensive homology to EGF receptor shares chromosomal location with neu oncogene. Science 230:1132–1139.
  • Davis, R. J., and M. P. Czech. 1985. Platelet-derived growth factor mimics phorbol diester action on epidermal growth factor receptor phosphorylation at threonine-654. Proc. Natl. Acad. Sci. USA 82:4080–4084.
  • Decker, S. J. 1984. Effects of epidermal growth factor and 12-O-tetradecanoylphorbol-13-acetate on metabolism of the epidermal growth factor receptor in normal human fibroblasts. Mol. Cell. Biol. 4:1718–1724.
  • Di Fiore, P. P., J. H. Pierce, T. P. Fleming, R. Hazan, A. Ullrich, C. R. King, J. Schlessinger, and S. A. Aaronson. 1987. Overex-pression of the human EGF receptor confers an EGF-dependent transformed phenotype to NIH 3T3 cells. Cell 51:1068–1070.
  • Di Fiore, P. P., J. H. Pierce, M. H. Kraus, O. Segatto, C. R. King, and S. A. Aaronson. 1987. erbB-2 is a potent oncogene when overexpressed in NIH/3T3 cells. Science 237:178–182.
  • Downward, J., P. Parker, and M. D. Waterfield. 1984. Auto-phosphorylation sites on the epidermal growth factor receptor. Nature (London) 311:483–485.
  • Drebin, J. A., D. F. Stern, V. C. Link, R. A. Weinberg, and M. I. Greene. 1984. Monoclonal antibodies identify a cell-surface antigen associated with an activated cellular oncogene. Nature (London) 312:545–548.
  • Gilmore, T., J. E. DeClue, and G. S. Martin. 1985. Protein phosphorylation at tyrosine is induced by the v-erbB gene product in vivo and in vitro. Cell 40:609–618.
  • Glenney, J. R., Jr., W. S. Chen, C. S. Lazar, G. M. Walton, L. M. Zokas, M. G. Rosenfeld, and G. N. Gill. 1988. Ligand-induced endocytosis of the EGF receptor is blocked by mutational inactivation and by microinjection of anti-phosphotyro-sine antibodies. Cell 52:675–664.
  • Honegger, A. M., T. J. Dull, S. Felder, E. Van Obberghen, F. Bellot, D. Szapary, A. Schmidt, A. Ullrich, and J. Schlessinger. 1987. Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing. Cell 51:199–209.
  • Hung, M.-C., A. Schechter, P.-Y. Chevray, D. F. Stern, and R. A. Weinberg. 1986. Molecular cloning of the neu gene: absence of gross structural alterations in oncogenic alleles. Proc. Natl. Acad. Sci. USA 83:261–264.
  • Hunter, T., and J. A. Cooper. 1981. Epidermal growth factor induces rapid tyrosine phosphorylation of proteins in A431 human tumor cells. Cell 24:741–752.
  • 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 2:305–316.
  • King, C. R., M. H. Kraus, and S. A. Aaronson. 1985. Amplification of a novel v-erbB-related gene in a human mammary carcinoma. Science 229:974–976.
  • Kmiecik, T. E., and D. Shalloway. 1987. Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49:65–73.
  • Kraus, M. H., N. C. Popescu, S. C. Amsbaugh, and C. R. King. 1987. Overexpression of the EGF receptor-related proto-onco-gene erbB-2 in human mammary tumor cell lines by different molecular mechanisms. EMBO J. 6:605–610.
  • Padhy, L. C., C. Shih, D. Cowing, R. Finkelstein, and R. A. Weinberg. 1982. Identification of a phosphoprotein specifically induced by the transforming DNA of rat neuroblastomas. Cell 28:865–871.
  • Parker, R. C., H. E. Varmus, and J. M. Bishop. 1984. Expression of v-src and chicken c-src in rat cells demonstrates qualitative differences between pp60v-src and pp60c-src. Cell 37:131–139.
  • Piwnica-Worms, H., K. B. Saunders, T. M. Roberts, A. E. Smith, and S. H. Cheng. 1987. Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src. Cell 49:75–82.
  • Rosen, O. M., R. Herrera, Y. Olowe, L. M. Petruzzelli, and M. H. Cobb. 1983. Phosphorylation activates the insulin receptor tyrosine protein kinase. Proc. Natl. Acad. Sci. USA 80:3237–3240.
  • Roussel, M. F., T. J. Dull, C. W. Rettenmier, P. Ralph, A. Ullrich, and C. J. Sherr. 1987. Transforming potential of the c-fms proto-oncogene (CSF-1 receptor). Nature (London) 325:549–552.
  • Schechter, A. L., M. C. Hung, L. Vaidyanathan, R. A. Weinberg, T. L. Yang-Feng, U. Francke, A. Ullrich, and L. Coussens. 1985. The neu gene: an erbB-homologous gene distinct from and unlinked to the gene encoding the EGF receptor. Science 229:976–978.
  • Schechter, A. L., D. F. Stern, L. Vaidyanathan, S. J. Decker, J. A. Drebin, M. I. Greene, and R. A. Weinberg. 1984. The neu oncogene: an erbB-related gene encoding a 185,000-Mr tumour antigen. Nature (London) 312:513–516.
  • Schubert, D., S. Heinemann, W. Carlisle, H. Tarikas, B. Kimes, J. Patrick, and J. H. Steinbach. 1974. Clonal cell lines from the rat central nervous system. Nature (London) 249:224–227.
  • Sefton, B. M., K. Beemon, and T. Hunter. 1978. Comparison of the expression of the src gene of Rous sarcoma virus in vitro and in vivo. J. Virol. 28:957–971.
  • Sefton, B. M., T. Hunter, K. Beemon, and W. Eckhart. 1980. Evidence that the phosphorylation of tyrosine is essential for cellular transformation by Rous sarcoma virus. Cell 20:807–816.
  • Semba, K., N. Kamata, K. Toyoshima, and T. Yamamoto. 1985. A v-erbB-related protooncogene, c-erbB-2, is distinct from the c-erbB-1/epidermal growth factor receptor gene and is amplified in a human salivary gland adenocarcinoma. Proc. Natl. Acad. Sci. USA 82:6497–6501.
  • Shalloway, D., P. M. Coussens, and P. Yaciuk. 1984. Overex-pression of the c-src protein does not induce transformation of NIH 3T3 cells. Proc. Natl. Acad. Sci. USA 81:7071–7075.
  • Shin, C., L. C. Padhy, M. Murray, and R. A. Weinberg. 1981. Transforming genes of carcinomas and neuroblastomas introduced into mouse fibroblasts. Nature (London) 290:261–263.
  • Slamon, D. J., G. M. Clark, S. G. Wong, W. J. Levin, A. Ullrich, and W. L. McGuire. 1987. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 235:177–182.
  • Stern, D. F., P. A. Heffernan, and R. A. Weinberg. 1986. pl85, a product of the neu proto-oncogene, is a receptorlike protein associated with tyrosine kinase activity. Mol. Cell. Biol. 6:1729–1740.
  • Stern, D. F., and M. P. Kamps. 1988. EGF-stimulated tyrosine phosphorylation of pl85neu: a potential model for receptor interactions. EMBO J. 7:995–1001.
  • Stern, D. F., A. B. Roberts, N. S. Roche, M. B. Sporn, and R. A. Weinberg. 1986. Differential responsiveness of myc- and ras-transfected cells to growth factors: selective stimulation of myc-transfected cells by epidermal growth factor. Mol. Cell. Biol. 6:870–877.
  • Stimuli, E., R. Zippel, L. Toschi, L. Morello, P. M. Comoglio, and L. Alberghina. 1988. Kinetics and regulation of the tyrosine phosphorylation of epidermal growth factor receptor in intact A431 cells. Mol. Cell. Biol. 8:1345–1351.
  • Velu, T. J., L. Beguinot, W. C. Vass, M. C. Willingham, G. T. Merlino, I. Pastan, and D. R. Lowry. 1987. Epidermal growth factor-dependent transformation by a human EGF receptor proto-oncogene. Science 238:1408–1410.
  • Venter, D. R., N. L. Tuzi, S. Dumar, and W. J. Gullick. 1987. Overexpression of the c-erbB-2 oncoprotein in human breast carcinomas: immunohistochemical assessment correlates with gene amplification. Lancet ii:69–72.
  • Yamamoto, T., S. Ikawa, T. Akiyama, K. Semba, N. Nomura, N. Miyajima, T. Saito, and K. Toyoshima. 1986. Similarity of protein encoded by the human c-erb-B-2 gene to epidermal growth factor receptor. Nature (London) 319:230–234.
  • Yokota, J., T. Yamamoto, K. Toyoshima, M. Terada, T. Sugi-mura, H. Battifora, and M. J. Cline. 1986. Amplification of c-erbB-2 oncogene in human adenocarcinomas in vivo. Lancet i:765–767.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.