Post-Translational Acquisition of Ligand Binding-and Tyrosine Kinase-Domain Function by the Epidermal Growth Factor and Insulin Receptors

References

• Lane M. D. Life-cycle and regulation of the insulin receptor. Insulin: Its Receptor and Diabetes, M. D. Hollenberg. Marcel Dekker, Inc., New York, NY 1985; 237–264
   Google Scholar
• Stoscheck C. M., King L. E., Jr. Role of epidermal growth factor in carcinogenesis. Cancer Research 1986; 46: 1030–1037
   PubMed Web of Science ®Google Scholar
• Ullrich A., Coussens L., Hayflick J. S., Dull T. J., Gray A., Tam A. W., Lee J., Yarden Y., Libermann T. A., Schlessinger J., Downward J., Mayes E. L.V., Whittle N., Waterfield M. D., Seeburg P. H. Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature (Lond) 1984; 309: 418–425
   PubMed Web of Science ®Google Scholar
• Ullrich A., Bell J. R., Chen E. Y., Herrera R., Petruzzelli L. M., Dull T. J., Gray A., Coussens L., Liao Y.-C., Tsubokawa M., Mason A., Suburg P. H., Grunfeld C., Rosen O. M., Ramachandran J. Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature (Lond.) 1985; 313: 756–761
   PubMed Web of Science ®Google Scholar
• Ebina Y., Ellis L., Jarnagin K., Edery M., Graf L., Clauser E., Ou J-h., Masiarz F., Kan Y. W., Goldfine I. D., Roth R. A., Rutter W. J. The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling. Cell 1985; 40: 747–758
   PubMed Web of Science ®Google Scholar
• Kasuga M., Karlson F. A., Kahn C. R. Insulin stimulates the phosphorylation of the 95. 000 dalton subunit of its own receptor, Science 1982; 215: 185–187
   Google Scholar
• Ushiro H., Cohen S. Identification of phosphotyrosine as a producet of epidermal growth factor-activated protein kinase in A-431 cell membranes. J. Biol. Chem. 1980; 255: 8363–8365
   PubMed Web of Science ®Google Scholar
• Lane M. D., Kohanski R. A. (1986) Control of autophosphorylation and substrate phosphorylation by the insulin receptor-protein kinase. Proceedings of the Eric K. Fernstron Symposium on Mechanisms of Insulin Action. 1986, P. Belfrage, J. Donner, P. Stralfors. Elsevier, Amsterdam, 59–73
   Google Scholar
• Kohanski R. A., Lane M. D. Kinetic evidence for activating and non-activating components of autophosphorylation of the insulin receptor protein kinase. Biochem. Biophys. Res. Communs. 1986; 134: 1312–1318
   PubMed Web of Science ®Google Scholar
• Ronnett G. V., Knutson V. P., Kohanski R., Simpson T. L., Lane M. D. 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
• Slieker L. J., Lane M. D. Post-translational processing of the epidermal growth factor receptor: glycosylation-dependent acquisition of ligand binding capacity. J. Biol. Chem. 1985; 260: 687–690
   PubMed Web of Science ®Google Scholar
• Slieker L. J., Martensen T. M., Lane M. D. Synthesis of epidermal growth factor receptor in A431 cells: glycosylation-dependent acquisition of ligand binding activity occurs post-translationally in the endoplasmic reticulum. J. Biol. Chem. 1986, In press
   PubMed Web of Science ®Google Scholar
• Reed B. C., Lane M. D. Insulin receptor synthesis and turnover in differentiating 3T3-L1 preadipocytes, Proc. Natl. Acad. Sci. USA 1980; 77: 285–289
   PubMed Web of Science ®Google Scholar
• Olson T. L., Lane M. D. Post-translational acquisition of insulin binding activity by its proreceptor: correlation to recognition by autoimmune antibody. 1986, Submitted for publication
   Google Scholar
• Balch W. E., Rothman J. Characterization of protein transport between successive compartments of the Golgi apparatus: asymmetric properties of donor and acceptor activities in a cell-free system, Arch. Biochem. Biophys. 1985; 240: 413–425
   Google Scholar
• Reed B. C., Ronnett G. V., Lane M. D. Role of glycosylation and protein synthesis in insulin receptor metabolism, Proc. Natl. Acad. Sci. USA 1981; 78: 2908–2912
   PubMed Web of Science ®Google Scholar
• Krupp M. N., Lane M. D. On the mechanism of ligand-induced down-regulation of insulin receptor level in the liver cell. J. Biol. Chem. 1981; 256: 1689–1694
   PubMed Web of Science ®Google Scholar
• Knutson V. P., Ronnett G. V., Lane M. D. Control of insulin receptor level in 3T3 cells: effect of insulin-induced down-regulation and dexamethasone-induced up-regulation on rate of receptor inactivation, Proc. Natl. Acad. Sci. USA 1982; 79: 2822–2826
   PubMed Web of Science ®Google Scholar
• Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides, Ann. Rev. Biochem. 1985; 54: 631–664
   PubMed Web of Science ®Google Scholar
• Ronnett G. V., Lane M. D. Post-translational glycosylation-induced activation of aglyco-insulin receptor accumulated during tunicamycin treatment. J. Biol. Chem. 1981; 256: 4704–4707
   PubMed Web of Science ®Google Scholar
• Olden K., Parent J. B., White S. L. Carbohydrate moieties of glycoproteins. A re-evaluation of their function, Biochim. Biophys. Acta. 1982; 650: 209–232
   PubMed Web of Science ®Google Scholar
• Flier J. S., Kahn C. R., Roth J., Bar R. S. Antibodies that impair insulin receptor binding in an unusual diabetic syndrome with severe insulin resistance. Science 1975; 190: 63–65
   PubMed Web of Science ®Google Scholar
• Kahn C. R, Flier J. S., Bar R. S., Archer J. A., Gorden P., Martin M. M., Roth J. The syndromes of insulin resistance and acanthosis nigricans. Insulin-receptor disorders in man, N. Engl. J. Med. 1976; 294: 739–745
   PubMed Web of Science ®Google Scholar
• Zick Y., Rees-Jones R. W., Taylor S. I., Gorden P., Roth J. The role of anti-receptor antibodies in stimulating phosphorylation of the insulin receptor. J. Biol. Chem. 1984; 259: 4396–4400
   PubMed Web of Science ®Google Scholar
• Breitfeld P. P., Rup D., Schwartz A. L. Influence of the N-linked oligosaccharides on the biosynthesis, intracellular routing, and function of the human asialoglycoprotein receptor. J. Biol. Chem. 1984; 259: 10414–10421
   PubMed Web of Science ®Google Scholar
• Prives J. M., Olden K. Carbohydrate requirement for expression and stability of acetylcholine receptor on the surface of embryonic muscle cells in culture, Proc. Natl. Acad. Sci. USA 1980; 77: 5263–5267
   PubMed Web of Science ®Google Scholar
• Lemansky P., Gieselmann V., Hasilik A., Von Figura K. Cathepsin D and ß-hexosaminidase synthesized in the presence of 1-deoxynojirimycin accumulate in the endoplasmic reticulum. J. Biol. Chem. 1984; 259: 10129–10135
   PubMed Web of Science ®Google Scholar
• Lodish H. F., Kong N. Glucose removal from N-linked oligosaccharides is required for efficient maturation of certain secretory glycoproteins from the rough endoplasmic reticulum to the Golgi complex. J. Cell. Biol. 1984; 98: 1720–1729
   PubMed Web of Science ®Google Scholar
• Stoscheck C. M., Sodequist A. M., Carpenter G. Biosynthesis of the epidermal growth factor receptor in cultured human cells. Endocrinology 1985; 116: 528–535
   PubMed Web of Science ®Google Scholar
• Sefton B. M., Trowbridge I. S., Cooper J. A., Scolnick E. M. The transforming proteins of Rous sarcoma virus. Harvey sarcoma virus and Abelson virus contain tightly bound lipid, Cell 1982; 31: 465–475
   Google Scholar
• Freedman R. B. Native disulfphide bond formation in protein biosynthesis: evidence for the role of protein disulphide isomerase, Trends Biochem. Sci. 1984; 9: 438–441
   Google Scholar
• Macdonald R. G., Czech M. P. Biosynthesis and processing of the Type II insulin-like growth factor receptor in H-35 hepatoma cells. J. Biol. Chem. 1985; 260: 11357–11365
   PubMed Web of Science ®Google Scholar
• Kris R. M., Lax I., Gullick W., Waterfield M. D., Ullrich A., Fridkin M., Schelssinger J. Antibodies against a synthetic peptide as a probe for the kinase activity of the avian EGF receptor and v-erbB protein. Cell 1985; 40: 619–625
   PubMed Web of Science ®Google Scholar
• Basu M., Biswas R., Das M. 42. 000-molecular weight epidermal growth factor receptor has protein kinase activity, Nature (Lond.) 1984; 311: 477–480
   Google Scholar