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Research Article

Antibody Bingling Boyding to the Juxtamembr are Ahch of the Insulin Receptor Alters Reotr Affinity

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Pages 381-398 | Published online: 26 Sep 2008

References

  • Pessin J. E., Treadway J. L. Structural basis for ligand-dependent transmembrane signalling of the insulin and IGF-1 receptor kinases. Molecular & cellular biology of insulin-like growth factors & their receptors, D. LeRoith, M. K. Raizada. Plenum Press, NY 1989; 261–281
  • Shoelson S. E., White M. F., Kahn C. R. Tryptic activation of the insulin receptor Proteolytic truncation of the alpha-subunit releases the beta-subunit from inhibitory control. J. Biol. Chem. 1988; 263: 4852–4860
  • Rosen O. M. After insulin binds. Science 1987; 237: 1452–1458
  • Larner J. Banting Lecture 1987 Insulin-Signaling Mechanisms. Lessons from the Old Testament of glycogen metabolism and the New Testament of molecular biology. Diabetes 1988; 37: 262–275
  • Rosen O. M., Herrera R., Olowe Y., Petruzzelli L. M., Cobb M. H. Phosphorylation activates the insulin receptor tyrosine protein kinase. Proc. Natl. Acad. Sci. U.S.A. 1983; 80: 3237–3240
  • Zhang B., Tavaré J. M., Ellis L., Roth R. A. The regulatory role of known tyrosine autophosphorylation sites of the insulin receptor kinase domain. J. Biol. Chem 1991; 266: 990–996
  • Murakami M. S., Rosen O. M. The role of insulin receptor autophosphorylation in signal transduction. J. Biol. Chem. 1991; 266: 22653–22660
  • Thies R. S., Ullrich A., McClain D. A. Augmented mitogenesis and impaired metabolic signaling mediated by a truncated insulin receptor. J. Biol. Chem. 1989; 264: 12820–12825
  • Myers M. G., Backer J. M., Siddle K., White M. F. The insulin receptor functions normally in chinese hamster ovary cells after truncation of the C terminus. J. Biol. Chem. 1991; 266: 10616–10623
  • White M. F., Livingston J. N., Backer J. M., Lauris V., Dull T. J., Ullrich A., Kahn C. R. Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not affect its tyrosine kinase activity. Cell 1988; 54: 641–649
  • Backer J. M., Schroeder G. G., Cahill D. A., Ullrich A., Siddle K., White M. F. Cytoplasmic juxtamemembrane region of the insulin receptor: A critical role in ATP binding, endogenous substrate phosphorylation, and insulin-stimulated bioeffects in CHO cells. Biochemistry 1991; 30: 6366–6372
  • Thies R. S., Webster N. J., McClain D. A. A Domain of the insulin receptor required for endocytosis in rat fibroblasts. J. Biol. Chem. 1990; 265: 10132–10137
  • Backer J. M., Shoelson S. E., Haring E., White M. F. Insulin receptors internalize by a rapid, saturable pathway requiring receptor autophosphorylation and an intact juxtamembrane region. J. Cell Biol. 1991; 115: 1535–1545
  • Kapeller R., Chen K. S., Yoakim M., Schaffhausen B. S., Backer J., White M. F., Cantley L. C., Ruderman N. B. Mutations in the juxtamembrane region of the insulin receptor impair activation of phosphatidylinositol 3-kinase by insulin. Mol. Endocrinol. 1991; 5: 769–777
  • Herrera R., Petruzzelli L., Thomas N., Bramson H. N., Kaiser E. T., Rosen O. M. An antipeptide antibody that specifically inhibits insulin receptor autophosphorylation and protein kinase activity. Proc. Natl. Acad. Sci. U.S.A. 1985; 82: 7899–7903
  • Frank B. H., Beckage M. J., Willey K. A. High-performance liquid chromatographic preparation of single-site carrier free pancreatic polypeptide hormone radiotracers. J. Chromatogr. 1983; 266: 239–248
  • Schaefer E. M., Siddle K., Ellis L. Deletion analysis of the human insulin receptor ectodomain reveals independently folded soluble subdomains and insulin binding by a monomeric α-subunit. J. Biol. Chem. 1990; 265: 13248–13253
  • Prigent S. A., Stanley K. K., Siddle K. Identification of epitopes on the human insulin receptor reacting with rabbit polyclonal antisera and mouse monoclonal antibodies. J. Biol. Chem. 1990; 265: 9970–9977
  • Cama A., Marcus-Samuels B., Taylor S. I. Immunological abnormalities in insulin receptors on cultured EBV-transformed lymphocytes from insulin resistant patients with lephrechaunism. Diabetes 1988; 37: 982–988
  • 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., Seeburg P. H., Grunfeld C., Rosen O. M., Ramachandran. The human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. J. Nature 1985; 313: 756–761
  • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976; 72: 248–254
  • Jett M., Seed T. M., Jamison G. A. Isolation and characterization of plasma membranes and intact nuclei from lymphoid cells. J. Biol. Chem. 1977; 252: 2134–2142
  • Torossian K., Freedman D., Fantus I. G. Vanadate down regulates cell surface insulin and growth hormone receptors and inhibits insulin receptor degradation in cultured human lymphocytes. J. Biol. Chem. 1988; 263: 9353–9359
  • Cuatrecasas P. Properties of insulin receptor isolated from liver and fat cell membranes. J. Biol. Chem. 1972; 247: 1980–1991
  • Wassler M., Jonasson I., Persson R., Fries E. Differential permeabilization of membranes by saponin treatment of isolated rat hepatocytes. Biochem J. 1987; 247: 407–415
  • Pilch P. F., Czech M. P. Hormone binding alters the conformation of the insulin receptor. Nature 1980; 210: 1152–1153
  • Donner D. B., Yonkers K. Hormone-induced conformational changes in the hepatic insulin receptor. J. Biol. Chem. 1983; 258: 9413–9418
  • Waugh S. M., Pilch P. F. Insulin binding changes the interface region between α subunits of the insulin receptor. Biochemistry 1989; 28: 2722–2727
  • Maddux B. A., Goldfine I. D. Evidence that insulin plus ATP may induce a conformational change in the β subunit of the insulin receptor without inducing receptor autophosphorylation. J. Biol. Chem. 1991; 266: 6731–6736
  • Baron V., Kaliman P., Gautier N., Van Obberghen E. Insulin binding to its receptor induces a conformational change in the receptor C-terminus. J. Biol. Chem. 1992; 267: 23290–23294

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