Oncogene Proteins and the Insulin Receptor

References

• Hunter T, Cooper J A. Protein-tyrosine kinases. Ann Rev Biochem 1985; 54: 897–930
   PubMed Web of Science ®Google Scholar
• Heldin C, Westermark H. B. Growth factors: Mechanism of action and relation to oncogenes. Cell 1984; 37: 9–20
   PubMed Web of Science ®Google Scholar
• Hunter T. The proteins of oncogenes. Sci Am 1984; 251: 70–79
   PubMed Web of Science ®Google Scholar
• Bishop J M. Cellular oncogenes and retroviruses. Ann Rev Biochem 1983; 53: 301–354
   Google Scholar
• Sefton B M, Hunter T. Tyrosine protein kinases. Advances in Cyclic Nucleotide and Protein Phosphorylation Research, Vol 18, P Greengard, G A Robinson. Raven Press, New York 1984; 195–226
   Google Scholar
• Jakobovits E B, Majors J E, Varmus H E. Hormonal regulation of the Rous sarcoma virus src gene via a heterologous promoter defines a threshold dose for cellular transformation. Cell 1984; 38: 757–765
   PubMed Web of Science ®Google Scholar
• Parker R C, Varmus H E, Bishop J M. Expression of the v-src and chicken c-src in rat cells demonstrates qualitative differences between pp60v-src and pp60c-src. Cell 1984; 37: 131–139
   PubMed Web of Science ®Google Scholar
• Takeya T, Hanafusa H. DNA sequence of the viral and cellular src gene of chickens. J Virol 1982; 44: 12–18
   PubMed Web of Science ®Google Scholar
• Hanafusa T, Want L-H, Anderson S M, et al. Characterization of the transforming gene of Fujinami sarcoma virus. Proc Natl Acad Sci USA 1980; 77: 3009–3013
   PubMed Web of Science ®Google Scholar
• Feldman R A, Wang E, Hanafusa H. Cytoplasmic localization of the transforming protein of Fujinami sarcoma virus: salt-sensitive association with subcellular components. J Virol 1983; 45: 782–791
   PubMed Web of Science ®Google Scholar
• Shibuya M, Hanafusa H. Nucleotide sequence of Fujinami sarcoma virus: evolutionary relationship of its transforming gene with transforming genes of other sarcoma viruses. Cell 1982; 30: 787–795
   PubMed Web of Science ®Google Scholar
• Feldman R A, Hanafusa T, Hanafusa H. Characterization of protein kinase activity associated with the transforming gene product of Fujinami sarcoma virus. Cell 1980; 22: 757–765
   PubMed Web of Science ®Google Scholar
• Roussel M F, Rettenmier C W, Look A T, et al. Cell surface expression of v-fms-coded glycoproteins is required for transformation. Molec Cell Biol 1984; 4: 1999–2009
   PubMed Web of Science ®Google Scholar
• Rettenmier C W, Roussel M F, Quinn C O, et al. Transmembrane orientation of glycoproteins encoded by the v-fms oncogene. Cell 1985; 40: 971–981
   PubMed Web of Science ®Google Scholar
• Witte O N, Rosenberg N, Baltimore D. Preparation of syngeneic tumor regressor serum reactive with the unique determinants of the Abelson murine leukemia virus-encoded PI20 protein at the cell surface. J Virol 1979; 31: 776–784
   PubMed Web of Science ®Google Scholar
• Witte O N, Dasgupta A, Baltimore D. Abelson murine leukemia virus protein is phosphorylated in vitro to form phosphotyrosine. Nature 1980; 283: 826–828
   PubMed Web of Science ®Google Scholar
• Wang J YJ. From c-abl to v-abl. Nature 1983; 304: 400
   PubMed Web of Science ®Google Scholar
• Reddy E P, Smith M J, Srinivasan A. Nucleotide sequence of abelson murine leukemia virus genome: structural similarity of its transforming gene product to other one gene products with tyrosine-specific kinase activity. Proc Natl Acad Sci USA 1983; 80: 3623–3627, 1983 (and correction in80:7372
   PubMed Web of Science ®Google Scholar
• Gilmore T, DeClue J E, Martin G S. Protein phosphorylation at tyrosine is induced by the v-verb B gene product in vivo and in vitro. Cell 1985; 40: 609–618
   PubMed Web of Science ®Google Scholar
• Courtneidge S A, Levinson A D, Bishop J M. The protein encoded by the transforming gene of avian sarcoma virus (pp60src) and a homologous protein in normal cells (pp60Proto-src) are associated with the plasma membrane. Proc Natl Acad Sci USA 1980; 77: 3783–3787
   PubMed Web of Science ®Google Scholar
• Kawai S, Yoshida M, Segawa K, et al. Characterization of Y73. an avian sarcoma virus: A unique transforming gene and its product. a phosphopolyprotein with protein kinase activity. Proc Natl Acad Sci USA 1980; 77: 6199–6203
   PubMed Web of Science ®Google Scholar
• Kitamura N, Kitamura A, Toyoshima K, et al. Avian sarcoma virus Y73 genome sequence and structural similarity of its transforming gene product to that of Rous sarcoma virus. Nature 1982; 297: 205–208
   PubMed Web of Science ®Google Scholar
• Barbacid M, Lauver A V, Devare S G. Biochemical and immunological characterization of polyprotcins coded for by the McDonough. Gardner-Arnstein and Snyder Theilen strains of feline sarcoma virus. J Virol 1980; 33: 196–207
   PubMed Web of Science ®Google Scholar
• Hampe A, Laprevotte I, Galiben F, et al. Nucleotide sequences of feline retroviral oncogenes (v-fes) provide evidence for a family of tyrosine-specific protein kinase genes. Cell 1982; 30: 775–785
   PubMed Web of Science ®Google Scholar
• Feldman R A, Wang L H, Hanafusa H, et al. Avian sarcoma virus UR2 encodes a transforming protein which is associated with a unique protein kinase activity. J Virol 1982; 42: 228–236
   PubMed Web of Science ®Google Scholar
• Neckameyer W S, Wang L-H. Nucleotide sequence of avian sarcoma virus UR2 and comparison of its transforming gene with other members of the tyrosine protein kinase oncogene family. J Virol 1985; 53: 879–884
   PubMed Web of Science ®Google Scholar
• Naharro G, Dunn C Y, Robbins K C. Analysis of the primary translational product and integrated DNA of a new feline sarcoma virus, GR-FeSV. Virology 1983; 125: 502–507
   PubMed Web of Science ®Google Scholar
• Naharro G, Robbins K C, Reddy E P. Gene product of v-fgr one: hybrid protein containing a portion of actin and a tyrosine-specific protein kinase. Science 1984; 223: 63–66
   PubMed Web of Science ®Google Scholar
• Willingham M C, Jay Pastan G. I. Localization of the src gene product of the Harvey strain of MSV to the plasma membrane of transformed cells by electron microscopic immunocytochemistry. Cell 1980; 19: 1005–1014
   PubMed Web of Science ®Google Scholar
• Levinson A D, Courtneidge S A, Bishop J M. Structural and functional domains of the Rous sarcoma virus transforming protein (pp60src). Proc Natl Acad Sci USA 1981; 78: 1624–1628
   PubMed Web of Science ®Google Scholar
• Glenn K, Bowen-Pope D F, Ross R. Platelet-derived growth factor. II. Identification of a platelet-derived growth factor receptor by affinity labeling. J Biol Chem 1982; 257: 5172–5176
   PubMed Web of Science ®Google Scholar
• Heldin C-H, Ek Ronnstrand B. L. Characterization of the receptor for platelet-derived growth factor on human fibroblasts. Demonstration of an intimate relationship with a 185,000 dalton substrate for the platelet-derived growth factor-stimulated kinase J Biol Chem 1983; 258: 10054–10061
   Google Scholar
• Ek Westermark B. B, Wasteson A, et al. Stimulation of tyrosine-specific phosphorylation by platelet-derived growth factor. Nature 1982; 295: 419–420
   PubMed Web of Science ®Google Scholar
• Das Miyakawa M. T, Fox C F, et al. Specific radiolabeling of a cell surface receptor for epidermal growth factor. Proc Natl Acad Sci USA 1977; 74: 2790–2794
   PubMed Web of Science ®Google Scholar
• Cohen S, Ushiro H, Stoseheck C, et al. A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles. J Biol Chem 1982; 257: 1523–1531
   PubMed Web of Science ®Google Scholar
• Buhrow S A, Cohen S, Staros J V. Affinity labeling of the protein kinase associated with the epidermal growth factor receptor in membrane vesicles from A431 cells. J Biol Chem 1982; 257: 4019–4022
   PubMed Web of Science ®Google Scholar
• Kasuga M, Zick Y, Blithe D L, et al. Insulin stimulation of phosphorylation of the β-subunit of the insulin receptor. Formation of both phosphoserine and phosphotyrosine. J Biol Chem 1982; 257: 9891–9894
   PubMed Web of Science ®Google Scholar
• Kasuga M, Hedo J A, Yamada K M, et al. The structure of insulin receptor and its subunits. Evidence for multiple nonreduced forms and a 210,000 possible proreceptor. J Biol Chem 1982; 257: 10392–10399
   PubMedGoogle Scholar
• Petruzzelli L M, Ganguly S, Smith C J, et al. Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta. Proc Natl Acad Sci USA 1982; 79: 6792–6796
   PubMed Web of Science ®Google Scholar
• Kasuga M, Van Obberghen E, Nissley S P, et al. Demonstration of two subtypes of insulin-like growth factor receptors by affinity cross-linking. J Biol Chem 1981; 256: 5305–5308
   PubMed Web of Science ®Google Scholar
• Jacobs S, Kull F C, Jr., Earp H S, et al. Somatomedin-C stimulates the phosphorylation of the β-subunit of its own receptor. J Biol Chem 1983; 258: 9581–9584
   PubMed Web of Science ®Google Scholar
• Sherr C J, Rettenmier C W, Sacca R, et al. The e-fms proto-oncogene product is related to the receptor for the mononuclear phagocyte growth factor. CSF-1. Cell 1985; 41: 665–676
   PubMed Web of Science ®Google Scholar
• Downward J, Yarden Y, Mayes E, et al. Close similarity of epidermal growth factor receptor and v-erb B oncogene protein sequences. Nature 1984; 307: 521–527
   PubMed Web of Science ®Google Scholar
• Ullrich A, Coussens L, Hayflick J, et al. Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature 1984; 309: 418–425
   PubMed Web of Science ®Google Scholar
• Frykberg L, Palmieri S, Beug H, et al. Transforming capacities of avian erythroblastosis virus mutants deleted in the erb A or erb B oncogenes. Cell 1983; 32: 227–238
   PubMed Web of Science ®Google Scholar
• Sealy L, Moscovici G, Moscovici C, et al. Site-specific mutagenesis of avian erythroblastosis virus: v-erb A is not required for transformation of fibroblasts. Virology 1983; 130: 179–194
   PubMed Web of Science ®Google Scholar
• Sealy L, Privalsky M, Moscoviei G, et al. Site-specific mutagenesis of avian erythroblastosis virus: erb B is required for oncogenicity. Virology 1983; 130: 155–178
   PubMed Web of Science ®Google Scholar
• Hayman M, Ramsay G, Savin K, et al. Identification and characterization of the avian erythroblastosis virus erb B gene product as a membrane glycoprotein. Cell 1983; 32: 579–588
   PubMed Web of Science ®Google Scholar
• Privalsky M, Sealy L, Bishop J M, et al. The product of the avian erythroblastosis virus erb B locus is a glycoprotein. Cell 1983; 32: 1257–1267
   PubMed Web of Science ®Google Scholar
• Hayman M, Beug H. Identification of a form of the avian erythroblastosis erh B gene product at the cell surface. Nature 1984; 309: 460–462
   PubMed Web of Science ®Google Scholar
• Radke K, Gilmore T, Martin G S. Transformation by Rous sarcoma virus: A cellular substrate for transformation-specific protein phosphorylation contains phosphotyrosine. Cell 1980; 21: 821–828
   PubMed Web of Science ®Google Scholar
• Erikson E, Erikson R. Identification of a cellular protein substrate phosphorylated by the avian sarcoma virus transforming gene product. Cell 1980; 21: 829–836
   PubMed Web of Science ®Google Scholar
• Pierce J H, Paolo DiFiore P, Aaronson S A, et al. Neoplastic transformation of mast cells by Abelson-MuLV: Abrogation of IL.-3 dependence by a non-autocrine mechanism. Cell 1985; 41: 685–693
   PubMed Web of Science ®Google Scholar
• Jacobs S, Cuatrecasas P. Insulin receptors. Ann Rc Pharmacol Toxicol 1983; 23: 461–479
   PubMed Web of Science ®Google Scholar
• Flier J S. Insulin receptors and insulin resistance. Ann Rev Med 1983; 34: 145–160
   PubMed Web of Science ®Google Scholar
• Shia M A, Rubin J B, Pilch P F. The insulin receptor protein kinase. Physicochemical requirements for activity. J Biol Chem 1983; 258: 14450–14455
   PubMedGoogle Scholar
• Cobb M H, Rosen O M. The insulin receptor and tyrosine kinase activity. Biochim Biophys Acta 1984; 738: 1–8
   PubMed Web of Science ®Google Scholar
• Ullrich A, Bell J R, Chen E Y, et al. Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature 1985; 31.3: 756–761
   Google Scholar
• Ebina Y, Ellis L, Jarnagin K, et al. The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling. Cell 1985; 40: 747–758
   PubMed Web of Science ®Google Scholar
• Czech M P. Molecular basis of insulin action. Ann Rev Biochem 1977; 46: 359–384
   PubMed Web of Science ®Google Scholar
• Jacobs S, Cuatrecasas P. Insulin receptor: Structure and function. Endocr Rev 1981; 2: 251–263
   PubMed Web of Science ®Google Scholar
• Kahn C R, Baud K L, Flier J S, et al. Insulin receptors, receptor antibodies and the mechanism ot insulin action. Rec Progr Horm Res 1981; 37: 477–538
   PubMedGoogle Scholar
• Molecular Basis of Insulin Action, M P Czech. Plenum Press, New York 1985
   Google Scholar
• Schneider J A, Diamond J, Rozengurt E. Glycolysis in quiescent cultures of 3T3 cells. J Biol Chem 1973; 253: 872–877
   Google Scholar
• Diamond J, Legg A, Schneider J A, et al. Glycolysis in quiescent cultures of 3T3 cells. J Biol Chem 1978; 253: 866–871
   PubMedGoogle Scholar
• Michell R H. Inositol phospholipids and cell surface receptor function. Biochim Biophys Acta 1975; 415: 81–147
   PubMed Web of Science ®Google Scholar
• Stein J M, Hales C N. The effect of insulin on 32Pi incorporation into rat fat cell phospholipids. Biochim Biophys Acta 1974; 337: 41–49
   PubMed Web of Science ®Google Scholar
• Moore R D. Intracellular pH in insulin action. Molecular Basis of Insulin Action, M P Czech. Plenum Press, New York 1985; 145–170
   Google Scholar
• Resh M D. Insulin action on the (Na +.K +)ATPase. Molecular Basis of Insulin Action, M P Czech. Plenum Press, New York 1985; 451–464
   Google Scholar
• Allen W R, Nilsen-Hamilton M, Hamilton R T. Insulin and growth factors stimulate rapid posttranslational changes in glucose transport in ovarian granulosa cells. J Cell Physiol 1981; 108: 15–24
   PubMed Web of Science ®Google Scholar
• Granner D, Andreone T, Sasaki K, et al. Inhibition of transcription of the phosphoenolpyruvate carboxykinase gene by insulin. Nature 1983; 305: 549–551
   PubMed Web of Science ®Google Scholar
• Cuatrecasas P. Interaction of concanavalin A and wheat germ agglutinin with the insulin receptor of fat cells and liver. J Biol Chem 1973; 248: 3528–3534
   PubMed Web of Science ®Google Scholar
• Massague J, Pilch P F, Czech M P. Electrophoretic resolution of three major insulin receptor structures with unique subunit stoichiometries. Proc Natl Acad Sci USA 1980; 77: 7137–7141
   PubMed Web of Science ®Google Scholar
• Massague J, Pilch P, Czech M P. A unique proteolytic cleavage site on the β subunit of the insulin receptor. J Biol Chem 1981; 256: 3182–3190
   PubMed Web of Science ®Google Scholar
• Pilch P F, Czech M P. The subunit structure of the high affinity insulin receptor. J Biol Chem 1980; 255: 1722–1731
   PubMed Web of Science ®Google Scholar
• Pilch P F, Czech M P. Interaction of cross-linking agents with the insulin effector systems of isolated fat cells. J Biol Chem 1979; 254: 3375–3381
   PubMed Web of Science ®Google Scholar
• Siegel T, Ganguly S, Jacobs S, et al. Purification and properties of the human placental insulin receptor. J Biol Chem 1981; 256: 9266–9273
   PubMed Web of Science ®Google Scholar
• Deutsch P J, Wan C F, Rosen O M, et al. Latent insulin receptors and possible receptor precursors in 3T3-L1 adipocytes. Proc Natl Acad Sci USA 1983; 80: 133–136
   PubMed Web of Science ®Google Scholar
• Ronnett G V, Knutson V P, Kohanski R A, et al. Role of glycosylation in the processing of newly translated insulin proreceptor in 3T3-L1 adipocytes. J Biol Chem 1984; 259: 4566–4575
   PubMed Web of Science ®Google Scholar
• Yip C C, Yeung C WT, Moule M C. Photoaffinity labeling of insulin receptor of rat adipocyte plasma membrane. J Biol Chem 1978; 253: 1743–1745
   PubMed Web of Science ®Google Scholar
• Jacobs S, Hazum E, Schechter Y, et al. Insulin receptor: Covalent labeling and identification of subunits. Proc Natl Acad Sci USA 1979; 76: 4918–4921
   PubMed Web of Science ®Google Scholar
• Pilch P F, Czech M. Interaction of cross-linking agents with the insulin effector system of isolated fat cells. J Biol Chem 1979; 254: 3375–3381
   PubMed Web of Science ®Google Scholar
• Van Obberghen E, Kowalski A. Phosphorylation of the hepatic-insulin receptor. FEBS Lett 1982; 143: 179–182
   PubMed Web of Science ®Google Scholar
• Haring H U, Kasuga M, Kahn C R. Insulin receptor phosphorylation in intact adipocytes and in a cell-free system. Biochem Biophys Res Commun 1982; 108: 1538–1545
   PubMed Web of Science ®Google Scholar
• Zick Y, Kasuga M, Kahn C R, et al. Characterization of insulin-mediated phosphorylation of the insulin receptor in a cell-free system. J Biol Chem 1983; 258: 75–80
   PubMed Web of Science ®Google Scholar
• Avruch J, Nemenoff R A, Blackshear P F, et al. Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes. J Biol Chem 1982; 257: 15162–15166
   PubMedGoogle Scholar
• Roth R A, Cassell D J. Insulin receptor: Evidence that it is a pro-teiirkinase. Science 1983; 219: 299–301
   PubMed Web of Science ®Google Scholar
• Kasuga M, Fujita-Yamaguchi Y, Blithe D L, et al. Tyrosine-specific protein kinase activity is associated with the purified insulin receptor. Proc Natl Acad Sci USA 1983; 80: 2137–2141
   PubMed Web of Science ®Google Scholar
• Shia M A, Pilch P F. The β subunit of the insulin receptor is an insulin-activated protein kinase. Biochemistry 1983; 22: 717–721
   PubMed Web of Science ®Google Scholar
• Van Obberghen E, Ross B, Kowlaski A, et al. Receptor-mediated phosphorylation of the hepatic insulin receptor: Evidence that the Mr 95,000 receptor subunit is its own kinase. Proc Natl Acad Sci USA 1983; 80: 945–949
   PubMed Web of Science ®Google Scholar
• Petruzzelli L, Herrera R, Rosen O M. Insulin receptor is an insulin-dependent tyrosine protein kinase. Copurification of insulin-binding activity and protein kinase activity to homogeneity from human placenta. Proc Natl Acad Sci USA 1984; 81: 3327–3331
   PubMed Web of Science ®Google Scholar
• Rosen O M, Herrera R, Olowe Y, et al. Phosphorylation activates the insulin receptor tyrosine protein kinase. Proc Natl Acad Sci USA 1983; 80: 3237–3240
   PubMed Web of Science ®Google Scholar
• Kasuga M, Zick Y, Blithe D L, et al. Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system. Nature 1982; 298: 667–669
   PubMed Web of Science ®Google Scholar
• Zick Y, Whittaker J, Roth J. Insulin stimulated phosphorylation of its own receptor. J Biol Chem 1983; 258: 3431–3434
   PubMed Web of Science ®Google Scholar
• Stadtmauer L, Rosen O M. Phosphorylation of exogenous substrates by the insulin receptor-associated protein kinase. J Biol Chem 1983; 258: 6682–6685
   PubMed Web of Science ®Google Scholar
• Zick Y, Grunberger G, Rees-Jones R W, et al. Use of tyrosine-containing polymers to characterize the substrate specificity of insulin and other hormone-stimulated tyrosine kinases. Eur J Biochem 1985; 148: 177–182
   PubMedGoogle Scholar
• Kadowaki T, Fujita-Yamaguchi Y, Nishida E, et al. Phosphorylation of tubulin and microtubule-associated proteins by the purified insulin receptor kinase. J Biol Chem 1985; 260: 4016–4020
   PubMed Web of Science ®Google Scholar
• Klein H H, Friedenberg G R, Cordera R, et al. Substrate specificities of insulin and epidermal growth factor receptor kinases. Biochem Biophys Res Commun 1985; 127: 254–263
   PubMed Web of Science ®Google Scholar
• Pike L J, Kuenzel E A, Casnellie J E, et al. A comparison of the insulin-and epidermal growth factor-stimulated protein kinases from human placenta. J Biol Chem 1984; 259: 9913–9921
   PubMed Web of Science ®Google Scholar
• Richert N D, Blithe D L, Pastan I. Properties of the src kinase purified from Rous sarcoma virus-induced rat tumors. J Biol Chem 1982; 257: 7143–7150
   PubMed Web of Science ®Google Scholar
• Yu K-T, Werth D K, Pastan I H, et al. src kinase catalyzes the phosphorylation and activation of the insulin receptor kinase. J Biol Chem 1985; 260: 5838–5846
   PubMed Web of Science ®Google Scholar
• Foulkes J G. Phosphotyrosyl-protein phosphatases. Curr Top Micro Immunol 1983; 107: 163–180
   PubMed Web of Science ®Google Scholar
• Shriner C L, Brautigan D L. Cytosolic protein phosphotyrosine phosphatases from rabbit kidney. J Biol Chem 1984; 259: 11383–11390
   PubMedGoogle Scholar
• Brautigan D L, Bornstein P, Gallis B. Phosphotyrosyl-protein phosphatase. J Biol Chem 1981; 256: 6519–6522
   PubMed Web of Science ®Google Scholar
• Grigorescu F, Flier J S, Kahn C R. Defect in insulin receptor phosphorylation in erythrocytes and fibroblasts associated with severe insulin resistance. J Biol Chem 1984; 259: 15003–15006
   PubMed Web of Science ®Google Scholar
• Collett M S, Wells S K, Purchio A F. Physical modification of purified Rous sarcoma virus pp60src protein after incubation with ATP/Mg2+. Virology 1983; 128: 285–297
   PubMed Web of Science ®Google Scholar
• Purchio A F. Evidence that pp60v-src, the product of the Rous sarcoma virsus src gene, undergoes autophosphorylation. J Virol 1982; 41: 1–7
   PubMed Web of Science ®Google Scholar
• Smart J E, Oppermann H, Czernilofsky A P, et al. Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src). Proc Natl Acad Sci USA 1981; 78: 6013–6017
   PubMed Web of Science ®Google Scholar
• Collett M S, Erikson E, Erikson R L. Structural analysis of the avian sarcoma virus transforming protein: sites of phosphorylation. J Virol 1979; 29: 770–781
   PubMed Web of Science ®Google Scholar
• Collett M S, Purchio A F, Erikson R L. Avian sarcoma virus-transforming protein. pp60v-src. shows protein kinase activity specific for tyrosine. Nature 1980; 285: 167–169
   PubMed Web of Science ®Google Scholar
• Cross F R, Hanafusa H. Local mutagenesis of Rous sarcoma virus: the major sites of tyrosine and serine phosphorylation of p60src are dispensable for transformation. Cell 1983; 34: 597–607
   PubMed Web of Science ®Google Scholar
• Snyder M A, Bishop J M, Colby W W, et al. Phosphorylation of tyrosine-416 is not required for the transforming properties and kinase activity of pp60v-src. Cell 1983; 32: 891–901
   PubMed Web of Science ®Google Scholar
• Collett M S, Belzer S K, Purchio A F. Structurally and functionally modified forms of pp60v-src in Rous sarcoma virus-transformed cell lysates. Molec Cell Biol 1984; 4: 1213–1220
   PubMed Web of Science ®Google Scholar
• Purchio A F, Wells S K, Collett M S. Increase in the phosphotransferase specific activity of purified Rous sarcoma virus pp60v-src protein after incubation with ATP plus Mg2+. Molec Cell Biol 1983; 3: 1589–1597
   PubMed Web of Science ®Google Scholar
• Collett M S, Belzer S K, Kamp L E. Enzymatic characteristics of pp60v-src isolated from vanadium-treated transformed cells. J Cell Biochem 1984; 26: 95–106
   PubMed Web of Science ®Google Scholar
• Yamamoto Y, Davis C G, Brown M S, et al. The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its RNA. Cell 1984; 39: 27–38
   PubMed Web of Science ®Google Scholar
• Sabatini D D, Kreibich G, Morimoto T, et al. Mechanisms for the incorporation of proteins in membranes and organelles. J Cell Biol 1982; 92: 1–22
   PubMed Web of Science ®Google Scholar
• Hampe A, Gobet M, Sherr C J, et al. Nucleotide sequence of the feline retroviral oncogene v-fms shows unexpected homology with oncogenes encoding tyrosine-specific protein kinases. Proc Natl Acad Sci USA 1984; 81: 85–89
   PubMed Web of Science ®Google Scholar
• Hunter T. The epidermal growth factor receptor gene and its product. Nature 1984; 311: 414–416
   PubMed Web of Science ®Google Scholar
• Kamps M P, Taylor S S, Sefton B M. Direct evidence that oncogenic tyrosine kinases and cAMP-dependent protein kinase have homologous ATP-binding sites. Nature 1984; 310: 589–591
   PubMed Web of Science ®Google Scholar
• Czernilofsky A P, Levinson A D, Varmus H E, et al. Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed amino acid sequence for gene product. Nature 1980; 287: 198–203, (with correction in Nature 301:736–738. 1983)
   PubMed Web of Science ®Google Scholar
• Buss J E, Sefton B M. Myristic acid, a rare fatty acid, is the lipid attached to the transforming protein of Rous sarcoma virus and its cellular homolog. J Virol 1985; 53: 7–12
   PubMed Web of Science ®Google Scholar
• Cross F R, Garber E A, Pellman D, et al. A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation. Molec Cell Biol 1984; 4: 1834–1842
   PubMed Web of Science ®Google Scholar
• Schultz A M, Henderson L E, Oroszlan S, et al. Amino terminal myristylation of the protein kinase p60src. a retroviral transforming protein. Science 1985; 227: 427–429
   PubMed Web of Science ®Google Scholar
• White M F, Haring H U, Kasuga M, et al. Kinetic properties and sites of autophosphorylation of the partially purified insulin receptor from hepatoma cells. J Biol Chem 1984; 259: 255–264
   PubMed Web of Science ®Google Scholar
• Cooper J A, Hunter T. Regulation of cell growth and transformation by tyrosine-specific protein kinases: The search for important cellular substrate proteins. Curr Top Microbiol Immunol 1983; 107: 125–162
   PubMed Web of Science ®Google Scholar
• Klarlund J K. Transformation of cells by an inhibitor of phosphatases acting on phosphotyrosinc in proteins. Cell 1985; 41: 707–717
   PubMed Web of Science ®Google Scholar
• Sefton B M, Hunter T, Beemon K, et al. Evidence that the phosphorylation of tyrosine is essential for cellular transformation by Rous sarcoma virus. Cell 1980; 20: 807–816
   PubMed Web of Science ®Google Scholar
• Beemon K, Ryden T, McNelly E A. Transformation by avian sarcoma viruses leads to phosphorylation of multiple cellular proteins on tyrosine residues. J Virol 1982; 42: 742–747
   PubMed Web of Science ®Google Scholar
• Cochet C, Gill G N, Meisenhelder J, et al. C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity. J Biol Chem 1984; 259: 2553–2558
   PubMed Web of Science ®Google Scholar
• Iwashita S, Fox C F. Epidermal growth factor and potent phorbol tumor promoters induce epidermal growth factor receptor phosphorylation in a similar but distinctively different manner in human epidermoid carcinoma A431 cells. J Biol Chem 1984; 259: 2559–2567
   PubMed Web of Science ®Google Scholar
• Radke K, Martin G S. Transformation by Rous sarcoma virus: Effects of src gene expression on the synthesis and phosphorylation of cellular polypeptides. Proc Natl Acad Sci USA 1979; 76: 5212–5216
   PubMed Web of Science ®Google Scholar
• Sefton B M, Hunter T, Ball E H, et al. Vinculin: a cytoskeletal target of the transforming protein of Rous sarcoma virus. Cell 1981; 24: 165–174
   PubMed Web of Science ®Google Scholar
• Hunter T, Sefton B M. The transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc Natl Acad Sci USA 1980; 77: 1311–1315
   PubMed Web of Science ®Google Scholar
• Brugge J S, Erikson E, Erikson R L. The specific interaction of the Rous sarcoma virus transforming protein. pp60src and two cellular proteins. Cell 1981; 25: 363–372
   PubMed Web of Science ®Google Scholar
• Cooper J A, Sefton B M, Hunter T. Diverse mitogenic agents induce the phosphorylation of two related 42,000 dalton proteins on tyrosine in quiescent chick cells. Molec Cell Biol 1984; 4: 30–37
   PubMed Web of Science ®Google Scholar
• Takai Y, Kishimoto A, Iwasa Y, et al. Calcium-dependent activation of a multifunctional protein kinase by membrane phospholipids. J Biol Chem 1979; 254: 3692–3695
   PubMed Web of Science ®Google Scholar
• Streb H, Irvine R F, Berridge M J, et al. Release of Ca2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate. Nature 1983; 306: 67–69
   PubMed Web of Science ®Google Scholar
• Sawyer S T, Cohen S. Enhancement of calcium uptake and phosphatidylinositiol turnover by epidermal growth factor in A431 cells. Biochemistry 1981; 20: 6280–6286
   PubMed Web of Science ®Google Scholar
• Machicao E, Wieland O H. Evidence that the insulin receptor-associated protein kinase acts as a phosphatidylinositol kinase. FEBS Lett 1984; 175: 113–116
   PubMed Web of Science ®Google Scholar
• Sugimoto Y, Whitman M, Cantley L C, et al. Evidence that the Rous sarcoma virus transforming gene product phosphorvlates phosphatidylinositol and diacylglycerol. Proc Natl Acad Sci USA 1984; 81: 2117–2121
   PubMed Web of Science ®Google Scholar
• Macara I G, Marinetti G V, Balduzzi P C. Transforming protein of avian sarcoma virus UR2 is associated with phosphatidylinositol kinase activity: possible role in tumorigenesis. Proc Natl Acad Sci USA 1984; 81: 2728–2732
   PubMed Web of Science ®Google Scholar
• Graziani Y, Erikson E, Erikson R L. Evidence that the Rous sarcoma virus transforming gene product is associated with glycerol kinase activity. J Biol Chem 1983; 258: 2126–2129
   PubMed Web of Science ®Google Scholar
• MacDonald M L, Kuenzel E A, Glomset J A, et al. Evidence from two transformed cell lines that the phosphorylations of peptide tyrosine and phosphatidylinositol are catalyzed by different proteins. Proc. Natl Acad Sci USA 1985; 82: 3993–3997
   PubMed Web of Science ®Google Scholar
• Thompson D M, Cochet C, Chambaz E M, et al. Separation and characterization of a phosphatidylinositol kinase activity that co-purifies with the epidermal growth factor receptor. J Biol Chem 1985; 260: 8824–8830
   PubMed Web of Science ®Google Scholar
• Moolenaar W H, Joosen L, deLaat S W. Ionic signal transduction by growth factors. Peptide hormones, Biomembranes and Cell Growth, L Bolis, R Verna, L Frati. Plenum, New York 1984; 215–231
   Google Scholar
• L'Allemain G, Franchi A, Cragoe E, Jr, et al. Blockade of the Na+ /H+ antiport abolishes growth factor-induced DNA synthesis in fibroblasts. J Biol Chem 1984; 259: 4313–4319
   PubMed Web of Science ®Google Scholar
• L'Allemain G, Paris S, Pouyssegur J. Growth factor action and intracellular pH regulation in fibroblasts. J Biol Chem 1984; 259: 5809–5815
   PubMed Web of Science ®Google Scholar
• Rothenberg P, Glaser L, Schlessinger P, et al. Activation of Na+ /H+ exchange by epidermal growth factor elevates intracellular pH in A431 cells. J Biol Chem 1983; 258: 12644–12653
   PubMedGoogle Scholar
• Wong T W, Goldberg A R. Tyrosyl protein kinases in normal rat liver: Identification and partial characterization. Proc Natl Acad Sci USA 1983; 80: 2529–2533
   PubMed Web of Science ®Google Scholar
• Tse-Dinh Y-C, Wong T W, Goldberg A R. Virus-and cell-encoded tyrosine protein kinases inactivate DNA topoisomerases in vitro. Nature 1984; 312: 785–786
   PubMed Web of Science ®Google Scholar
• Tse Y-C, Kirkegaard K, Wang J C. Covalent bonds between protein and DNA. J Biol Chem 1980; 255: 5560–5565
   PubMed Web of Science ®Google Scholar
• Champoux J J. DNA is linked to the rat liver DNA nicking-closing enzyme by a phosphodiester bond to tyrosine. J Biol Chem 1981; 256: 4805–4809
   PubMed Web of Science ®Google Scholar
• Glaser V M, Luchnik A N. Decrease in the density of DNA topological turns during in vitro aging of Syrian hamster cells. Expl Cell Res 1982; 139: 249–255
   PubMed Web of Science ®Google Scholar
• Huleihel M, Aboud M. Inhibition of retrovirus DNA supercoiling in interferon-treated cells. J Virol 1983; 48: 120–126
   PubMed Web of Science ®Google Scholar
• Cooper J A, Esch F S, Taylor S S, et al. Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro. J Biol Chem 1984; 259: 7835–7841
   PubMed Web of Science ®Google Scholar
• Nimmo H G, Cohen P. Hormonal control of protein phosphorylation. Adv Cyc Nucl Res 1977; 8: 145–266
   PubMedGoogle Scholar