Phosphorylation and Activation of Epidermal Growth Factor Receptors in Cells Transformed by the src Oncogene

References

• Barker, K., A. Aderem, and H. Hanafusa. 1989. Modulation of arachidonic acid metabolism by Rous sarcoma virus. J. Virol. 63:2929–2935.
   PubMedGoogle Scholar
• Bertics, P. J., W. S. Chen, L. Hubler, C. S. Lazar, M. G. Rosenfeld, and G. N. Gill. 1988. Alteration of epidermal growth factor receptor activity by mutation of its primary carboxyl- terminal site of tyrosine self-phosphorylation. J. Biol. Chem. 263:3610–3617.
   PubMedGoogle Scholar
• 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.
   PubMedGoogle Scholar
• Bird, T. A., and J. Saklatvala. 1990. Down-modulation of epidermal growth factor receptor affinity in fibroblasts with interleukin 1 or tumor necrosis factor is associated with phosphorylation at a site other than threonine 654. J. Biol. Chem. 265:235–240.
   PubMed Web of Science ®Google Scholar
• Bolen, J. B., and A. Veillette. 1989. A function for the lc. proto-oncogene. Trends Biochem. Sci. 14:404–407.
   PubMedGoogle Scholar
• Boni-Schnetzler, M. and P. Pilch. 1987. Mechanism of epidermal growth factor receptor autophosphorylation and high-affinity binding. Proc. Natl. Acad. Sci. USA 84:7832–7836.
   PubMedGoogle Scholar
• Chiarugi, V., F. Porciatti, F. Pasquali, L. Magnelli, S. Giannelli, and M. Ruggiero. 1987. Polyphosphoinositide metabolism is rapidly stimulated by activation of a temperature-sensitive mutant of Rous sarcoma virus in rat fibroblasts. Oncogene 2:37–40.
   PubMedGoogle Scholar
• Cochet, C., G. N. Gill, J. Meisenhelder, J. A. Cooper, and T. Hunter. 1984. C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity. J. Biol. Chem. 259:2553–2558.
   PubMed Web of Science ®Google Scholar
• Cooper, J. A., and T. Hunter. 1981. Changes in protein phosphorylation in Rous sarcoma virus-transformed chicken embryo cells. Mol. Cell. Biol. 1:165–178.
   PubMed Web of Science ®Google Scholar
• Cooper, J. A., K. D. Nakamura, T. Hunter, and M. J. Weber. 1983. Phosphotyrosine-containing proteins and expression of transformation parameters in cells infected with partial transformation mutants of Rous sarcoma virus. J. Virol. 46:15–28.
   PubMed Web of Science ®Google Scholar
• Cooper, J. A., B. M. Sefton, and T. Hunter. 1983. Detection and quantitation of phosphotyrosine in proteins. Methods Enzymol. 99:387–405.
   PubMed Web of Science ®Google Scholar
• Countaway, J. L., P. McQuilkin, N. Girones, and R. J. Davis. 1990. Multisite phosphorylation of the epidermal growth factor receptor. J. Biol. Chem. 265:3407–3416.
   PubMedGoogle Scholar
• Countaway, J. L., I. C. Northwood, and R. J. Davis. 1989. Mechanism of phosphorylation of the epidermal growth factor receptor at threonine 669. J. Biol. Chem. 264:10828–10835.
   PubMedGoogle Scholar
• Davis, R. J. 1988. Independent mechanisms account for the regulation by protein kinase C of the epidermal growth factor receptor affinity and tyrosine-protein kinase activity. J. Biol. Chem. 263:9462–9469.
   PubMed Web of Science ®Google Scholar
• Davis, R. J., and M. P. Czech. 1985. Tumor-promoting phorbol diesters cause the phosphorylation of epidermal growth factor receptors in normal human fibroblasts at threonine-654. Proc. Natl. Acad. Sci. USA 82:1974–1978.
   PubMedGoogle Scholar
• Di Fiore, P. P., J. H. Piêrce, T. P. Fleming, R. Hazan, A. Ullrich, C. R. King, J. Schlessinger, and S. A. Aaronson. 1987. Overexpression of the human EGF receptor confers an EGF-dependent transformed phenotype to NIH 3T3 cells. Cell 51:1063–1070.
   PubMed Web of Science ®Google Scholar
• Diringer, H., and R. R. Friis. 1977. Changes in phosphatidylinositol metabolism correlated to growth state of normal and Rous sarcoma virus-transformed Japanese quail cells. Cancer Res. 37:2979–2984.
   PubMedGoogle Scholar
• Downward, J., P. Parker, and M. D. Waterfield. 1984. Autophosphorylation sites on the epidermal growth factor receptor. Nature (London) 311:483–485.
   PubMed Web of Science ®Google Scholar
• Downward, J., M. D. Waterfield, and P. J. Parker. 1985. Autophosphorylation and protein kinase C phosphorylation of the epidermal growth factor receptor. J. Biol. Chem. 260:14538–14546.
   PubMed Web of Science ®Google Scholar
• Downward, J., Y. Yarden, E. Mayes, G. Scrace, N. Totty, P. Stockwell, A. Ullrich, J. Schlessinger, and M. D. Waterfield. 1984. Close similarity of epidermal growth factor receptor and v-er.-B oncogene protein sequences. Nature (London) 307:521–527.
   PubMed Web of Science ®Google Scholar
• Gorga, F. R., C. E. Riney, and T. L. Benjamin. 1990. Inositol triphosphate levels in cells expressing wild-type and mutant polyomavirus middle T antigens: evidence for activation of phospholipase C via activation of pp60c-sr.. J. Virol. 64:105–112.
   PubMed Web of Science ®Google Scholar
• Gould, K. L., and T. Hunter. 1988. Platelet-derived growth factor induces multisite phosphorylation of pp60c-sr. and increases its protein-tyrosine kinase activity. Mol. Cell. Biol. 8:3345–3356.
   PubMed Web of Science ®Google Scholar
• Gray, G. M., and I. G. Macara. 1989. Serum-stimulated phosphatidylinositol turnover is enhanced in 3T3 cells with active pp60v-sr.. Oncogene 4:1213–1217.
   PubMedGoogle Scholar
• Heisermann, G. J., and G. N. Gill. 1988. Epidermal growth factor receptor threonine and serine residues phophorylated in vivo. J. Biol. Chem. 263:13152–13158.
   Google Scholar
• Heisermann, G. J., H. S. Wiley, B. J. Walsh, H. A. Ingraham, C. J. Fiol, and G. N. Gill. 1990. Mutational removal of the thr669 and ser671 phosphorylation sites alters substrate specificity and ligand-induced internalization of the epidermal growth factor receptor. J. Biol. Chem. 265:12820–12827.
   PubMed Web of Science ®Google Scholar
• Honegger, A., T. J. Dull, F. Bellot, E. Van Obberghen, D. Szepary, A. Schmidt, A. Ullrich, and J. Schlessinger. 1988. Biological activities of EGF-receptor mutants with individually altered autophosphorylation sites. EMBO J. 7:3045–3052.
   PubMedGoogle Scholar
• Honegger, A., T. J. Dull, D. Szapary, A. Komoriya, R. Kris, A. Ullrich, and J. Schlessinger. 1988. Kinetic parameters of the protein tyrosine kinase activity of EGF-receptor mutants with individually altered autophosphorylation sites. EMBO J. 7:3053–3060.
   PubMedGoogle Scholar
• Honegger, A. M., R. M. Kris, A. Ullrich, and J. Schlessinger. 1989. Evidence that autophosphorylation of solubilized receptors for epidermal growth factor is mediated by intermolecular cross-phosphorylation. Proc. Natl. Acad. Sci. USA 86:925–929.
   PubMed Web of Science ®Google Scholar
• Hsuan, J. J., N. Totty, and M. D. Waterfield. 1989. Identification of a novel autophosphorylation site (P4) on the epidermal growth factor receptor. Biochem. J. 262:659–663.
   PubMed Web of Science ®Google Scholar
• Hunter, T. Personal communication.
   Google Scholar
• Hunter, T., N. Ling, and J. A. Cooper. 1984. Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane. Nature (London) 311:480–483.
   PubMed Web of Science ®Google Scholar
• Johnson, M. L., and S. G. Frasier. 1985. Nonlinear least-squares analysis. Methods Enzymol. 117:301–342.
   Google Scholar
• Johnson, R. M., W. J. Wasilenko, R. R. Mattingly, M. J. Weber, and J. C. Garrison. 1989. Fibroblasts transformed with v-sr. show enhanced formation of an inositol tetrakisphosphate. Science 246:121–124.
   PubMedGoogle Scholar
• Kamps, M. P., J. E. Buss, and B. M. Sefton. 1986. Rous sarcoma virus transforming protein lacking myristic acid phosphorylates known polypeptide substrates without inducing transformation. Cell 45:105–112.
   PubMedGoogle Scholar
• Kamps, M. P., and B. M. Sefton. 1988. Identification of multiple novel polypeptide substrates of the v-sr., v-ye., v-fps. v-ros. and v-er.-B oncogenic tyrosine protein kinases utilizing antisera against phosphotyrosine. Oncogene 2:305–315.
   PubMedGoogle Scholar
• Kozma, L. M., A. B. Reynolds, and M. J. Weber. 1990. Glycoprotein tyrosine phosphorylation in Rous sarcoma virus- transformed chicken embryo fibroblasts. Mol. Cell. Biol. 10: 837–841.
   PubMedGoogle Scholar
• Kozma, L. M., and M. J. Weber. 1990. Constitutive phosphorylation of the receptor for insulinlike growth factor-I in cells transformed by the sr. oncogene. Mol. Cell. Biol. 10:3626–3634.
   PubMedGoogle Scholar
• Kypta, R. M., Y. Goldberg, E. T. Ulug, and S. A. Courtneidge. 1990. Association between the PDGF receptor and the sr. family of tyrosine kinases. Cell 62:481–492.
   PubMed Web of Science ®Google Scholar
• Leef, J. W., and M. J. Weber. Unpublished data.
   Google Scholar
• Lin, C. R., W. S. Chen, C. S. Lazar, C. D. Carpenter, G. N. Gill, R. M. Evans, and M. G. Rosenfeld. 1986. Protein kinase C phosphorylation at Thr 654 of the unoccupied EGF receptor and EGF binding regulate functional receptor loss by independent mechanisms. Cell 44:839–848.
   PubMedGoogle Scholar
• Linder, M. E., and J. G. Burr. 1988. Nonmyristoylated p60v-sr. fails to phosphorylate proteins of 115-120 kDa in chicken embryo fibroblasts. Proc. Natl. Acad. Sci. USA 85:2608–2612.
   PubMedGoogle Scholar
• Livneh, E., T. J. Dull, E. Berent, R. Prywes, A. Ullrich, and J. Schlessinger. 1988. Release of a phorbol ester-induced mitogenic block by mutation at Thr-654 of the epidermal growth factor receptor. Mol. Cell. Biol. 8:2302–2308.
   PubMed Web of Science ®Google Scholar
• Luttrell, D. K., L. M. Luttrell, and S. J. Parsons. 1988. Augmented mitogenic responsiveness to epidermal growth factor in murine fibroblasts that overexpress pp60c-sr.. Mol. Cell. Biol. 8:497–501.
   PubMed Web of Science ®Google Scholar
• Margolis, B., F. Bellot, A. M. Honegger, A. Ullrich, J. Schlessinger, and A. Zilberstein. 1990. Tyrosine kinase activity is essential for the association of phospholipase C-γ with the epidermal growth factor receptor. Mol. Cell. Biol. 10:435–441.
   PubMed Web of Science ®Google Scholar
• Margolis, B., S. G. Rhee, S. Felder, M. Mervic, R. Lyall, A. Levitzki, A. Ullrich, A. Zilberstein, and J. Schlessinger. 1989. EGF induces tyrosine phosphorylation of phospholipase C-II: a potential mechanism for EGF receptor signalling. Cell 57:1101–1107.
   PubMed Web of Science ®Google Scholar
• Margolis, B. L., I. Lax, R. Kris, M. Dombalagian, A. Honegger, R. Howk, D. Givol, A. Ullrich, and J. Schlessinger. 1989. All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/ne. are located in their carboxyl-terminaltails. J. Biol. Chem. 264:10667–10671.
   PubMed Web of Science ®Google Scholar
• Martinez, R., K. D. Nakamura, and M. J. Weber. 1982. Identification of phosphotyrosine-containing proteins in untransformed and Rous sarcoma virus-transformed chicken embryo fibroblasts. Mol. Cell. Biol. 2:653–665.
   PubMedGoogle Scholar
• Martins, T. J., Y. Sugimoto, and R. L. Erikson. 1989. Dissociation of inositol triphosphate from diacylglycerol production in Rous sarcoma virus-transformed fibroblasts. J. Cell Biol. 108: 683–691.
   PubMedGoogle Scholar
• Meek, J. L. 1980. Prediction of peptide retention times in high-pressure liquid chromatography on the basis of amino acid composition. Proc. Natl. Acad. Sci. USA 77:1632–1636.
   PubMed Web of Science ®Google Scholar
• Meisenhelder, J., P.-G. Suh, S. G. Rhee, and T. Hunter. 1989. Phospholipase C-γ is a substrate for the PDGF and EGF receptor protein-tyrosine kinases in viv. and in vitro. Cell 57:1109–1122.
   Google Scholar
• Montegaudo, C. A., D. L. Williams, G. A. Crabb, M. Tondravi, and M. J. Weber. 1984. Phosphotyrosine-containing membrane proteins in Rous sarcoma virus-transformed cells, p. 69–75. In Cancer Cells, vol. 2. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Nishibe, S., M. I. Wahl, S. G. Rhee, and G. Carpenter. 1989. Tyrosine phosphorylation of phospholipase C-II in vitr. by the epidermal growth factor receptor. J. Biol. Chem. 264:10335–10338.
   PubMed Web of Science ®Google Scholar
• Nori, M., L. K. Shawver, and M. J. Weber. A Swiss 3T3 variant cell line resistant to the effects of tumor promoters cannot be transformed by src. Mol. Cell. Biol. 10:4155-4162.
   PubMedGoogle Scholar
• Parsons, J. T., and M. J. Weber. 1989. Genetics of src. structure and functional organization of a protein tyrosine kinase. Curr. Top. Microbiol. Immunol. 147:80–127.
   Google Scholar
• Parsons, S. J. Personal communication.
   Google Scholar
• Parsons, S. J., D. J. McCarley, C. M. Ely, D. C. Benjamin, and J. T. Parsons. 1984. Monoclonal antibodies to Rous sarcoma virus pp60sr. react with enzymatically active cellular pp60sr. of avian and mammalian origin. J. Virol. 51:272–282.
   PubMedGoogle Scholar
• Prywes, R., E. Livneh, A. Ullrich, and J. Schlessinger. 1986. Mutations in the cytoplasmic domain of EGF receptor affect EGF binding and receptor internalization. EMBO J. 5:2179–2190.
   PubMedGoogle Scholar
• Ralston, R., and J. M. Bishop. 1985. The product of the proto-oncogene c-sr. is modified during the cellular response to platelet-derived growth factor. Proc. Natl. Acad. Sci. USA 82:7845–7849.
   PubMed Web of Science ®Google Scholar
• Ray, B. L., and T. W. Sturgill. 1987. Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein 2 in vitro. Proc. Natl. Acad. Sci. USA 84:1502–1506.
   PubMed Web of Science ®Google Scholar
• Reynolds, A. B., D. J. Roessel, S. B. Kanner, and J. T. Parsons. 1989. Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular sr. gene. Mol. Cell. Biol. 19:629–638.
   Google Scholar
• Riedel, H., S. Massoglia, J. Schlessinger, and A. Ullrich. 1988. Ligand activation of overexpressed epidermal growth factor receptors transforms NIH 3T3 mouse fibroblasts. Proc. Natl. Acad. Sci. USA. 85:1477–1481.
   PubMed Web of Science ®Google Scholar
• Rossomando, A. J., D. M. Payne, M. J. Weber, and T. W. Sturgill. 1989. Evidence that pp42, a major tyrosine kinase target protein, is a mitogen-activated serine/threonine protein kinase. Proc. Natl. Acad. Sci. USA 86:6940–6943.
   PubMed Web of Science ®Google Scholar
• Rossomando, A. J., T. W. Sturgill, and M. J. Weber. Unpublished data.
   Google Scholar
• Scatchard, G. 1949. The attractions of proteins for small molecules and ions. Ann. N.Y. Acad. Sci. 51:660–672.
   Web of Science ®Google Scholar
• Schlessinger, J. 1986. Allosteric regulation of the epidermal growth factor receptor kinase. J. Cell Biol. 103:2067–2072.
   PubMed Web of Science ®Google Scholar
• Spangler, R., C. Joseph, S. A. Qureshi, K. L. Berg, and D. A. Foster. 1989. Evidence that v-sr. and v-fp. gene products use a protein kinase C-mediated pathway to induce expression of a transformation-related gene. Proc. Natl. Acad. Sci. USA. 86: 7017–7021.
   PubMedGoogle Scholar
• Sturani, 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.
   PubMed Web of Science ®Google Scholar
• Sugimoto, Y., M. Whitman, L. C. Cantley, and R. L. Erikson. 1984. Evidence that the Rous sarcoma virus transforming gene product phosphorylates phosphatidylinositol and diacylglycerol. Proc. Natl. Acad. Sci. USA 81:2117–2121.
   PubMed Web of Science ®Google Scholar
• Velu, T. J., L. Beguinot, W. C. Vass, M. C. Willingham, G. T. Merlino, I. Pastan, and D. R. Lowy. 1987. Epidermal growth factor-dependent transformation by a human EGF receptor proto-oncogene. Science 238:1408–1410.
   PubMed Web of Science ®Google Scholar
• Velu, T. J., W. C. Vass, D. R. Lowy, and L. Beguinot. 1989. Functional heterogeneity of proto-oncogene tyrosine kinases: the C terminus of the human epidermal growth factor receptor facilitates cell proliferation. Mol. Cell. Biol. 9:1772–1778.
   PubMedGoogle Scholar
• Wahl, M. L., T. O. Daniel, and G. Carpenter. 1988. EGF treatment of A-431 cells results in antiphosphotyrosine recovery of phospholipase activity. Science 241:968–970.
   PubMedGoogle Scholar
• Wahl, M. L., S. Nishibe, P.-G. Suh, S. G. Rhee, and G. Carpenter. 1989. Epidermal growth factor stimulates tyrosine phosphorylation of phospholipase C-II independently of receptor internalization and extracellular calcium. Proc. Natl. Acad. Sci. USA 86:1568–1572.
   PubMed Web of Science ®Google Scholar
• Wahl, M. L., N. E. Olashaw, S. Nishibe, S. G. Rhee, and G. Carpenter. 1989. Platelet-derived growth factor induces rapid and sustained tyrosine phosphorylation of phospholipase c-γ in quiescent BALB/c 3T3 cells. Mol. Cell. Biol. 9:2934–2943.
   PubMedGoogle Scholar
• Walton, G. M., W. S. Chen, M. G. Rosenfeld, and G. N. Gill. 1990. Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in viv. tyrosine phosphorylation of cell substrates. J. Biol. Chem. 265:1750–1754.
   PubMedGoogle Scholar
• Wasilenko, W. J., M. Nori, N. Testerman, and M. J. Weber. 1990. Inhibition of epidermal growth factor receptor biosynthesis caused by the sr. oncogene product, pp60v-sr.. Mol. Cell. Biol. 10:1254–1258.
   PubMedGoogle Scholar
• Wasilenko, W. J., L. K. Shawver, and M. J. Weber. 1987. Down-modulation of EGF receptors in cells transformed by the sr. oncogene. J. Cell. Physiol. 131:450–457.
   PubMedGoogle Scholar
• Wilson, L. K., D. K. Luttrell, J. T. Parsons, and S. J. Parsons. 1989. pp60c-sr. tyrosine kinase, myristylation, and modulatory domains are required for enhanced mitogenic responsiveness to epidermal growth factor seen in cells overexpressing c-src. Mol. Cell. Biol. 9:1536–1544.
   Google Scholar
• Wyke, J. A., and A. W. Stoker. 1987. Genetic analysis of the form and function of the viral sr. oncogene product. Biochim. Biophys. Acta 907:47–69.
   PubMedGoogle Scholar
• Yu, K., D. K. Werth, I. H. Pastan, and M. P. Czech. 1985. sr. kinase catalyzes the phosphorylation and activation of the insulin receptor kinase. J. Biol. Chem. 260:5838–5846.
   PubMed Web of Science ®Google Scholar