Metabolism - Clinical and Experimental
Volume 44 , Pages 2-11 , October 1995

Role of the time factor in signaling specificity: Application to mitogenic and metabolic signaling by the insulin and insulin-like growth factor-I receptor tyrosine kinases

References 

  1. De Meyts P, Wallach B, Christoffersen CT, et al.  The insulin-like growth factor-I receptor. In: Structure, ligand binding mechanism and signal transduction. ed 2. Horm Res. 42:1994;p. 152–169
  2. Krebs EG, Beavo JA. Phosphorylation-dephosphorylation of enzymes. Annu Rev Biochem. 1979;48:923–959
  3. Hunter T. A thousand and one protein kinases. Cell. 1987;50:823–829
  4. Hunter T, Sefton BM. The transforming gene product of Rous sarcoma virus phosphorylates tyrosine. In: ed 2. Proc Natl Acad Sci USA. 77:1980;p. 1311–1315
  5. Hunter T. Protein-tyrosine phosphatases: The other side of the coin. Cell. 1989;58:1013–1016
  6. Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem. 1989;58:453–508
  7. Tonks NK, Yang Q, Flint AJ, et al.  Protein tyrosine phosphatases: The problems of a growing family. In: ed 2. Cold Spring Harbor Symp Quant Biol. 17:1992;p. 87–94
  8. Wilks AF. Structure and function of the protein tyrosine kinases. Prog Growth Factor Res. 1990;2:97–111
  9. Hunter T, Lindberg RA, Middlemas DS, et al.  Receptor protein tyrosine kinases and phosphatases. In: ed 2. Cold Spring Harbor Symp Quant Biol. 17:1992;p. 25–41
  10. Cantley LC, Auger KR, Carpenter C, et al.  Oncogenes and signal transduction. Cell. 1991;64:281–302
  11. Argetsinger LS, Campbell GS, Yang X, et al.  Identification of JAK2 as a growth hormone receptor-associated tyrosine kinase. Cell. 1993;74:237–244
  12. Cadena DL, Gill GN. Receptor tyrosine kinases. FASEB J. 1992;6:2332–2337
  13. Ullrich A, Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell. 1990;61:203–212
  14. Yarden Y, Ullrich A. Growth factor receptor tyrosine kinases. Annu Rev Biochem. 1988;57:443–478
  15. Tavaré JM, Siddle K. Mutational analysis of insulin receptor function: Consensus and controversy. Biochim Biophys Acta. 1993;1178:21–39
  16. Hubbard SR, Wei L, Ellis L, et al.  Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature. 1994;372:746–754
  17. White MF, Livingston JN, Backer JM, et al.  Mutation of the insulin receptor at tyrosine 960 inhibits signal transduction but does not affect its tyrosine kinase activity. Cell. 1988;54:641–649
  18. Schlessinger J. Signal transduction by allosteric receptor oligomerization. TIBS. 1988;13:443–447
  19. Williams LT. Signal transduction by the platelet-derived growth factor receptor. Science. 1989;243:1564–1570
  20. De Meyts P. The structural basis of insulin and insulin-like growth factor-I (IGF-I) receptor binding and negative cooperativity, and its relevance to mitogenic versus metabolic signaling. Diabetologia. 1994;37(suppl 2):S135–S148
  21. Blechman JM, Lev S, Barg J, et al.  The fourth immunoglobulin domain of the stem cell factor receptor couples ligand binding to signal transduction. Cell. 1995;80:103–113
  22. de Vos AM, Ultsch M, Kossiakoff AA. Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex. Science. 1992;255:306–312
  23. Stahl N, Yancopoulos GD. The alphas, betas, and kinases of cytokine receptor complexes. Cell. 1993;74:587–590
  24. Kishimoto T, Taga T, Akira S. Cytokine signal transduction. Cell. 1994;76:253–262
  25. Shuldiner AR, Barbetti F, Raben N, et al.  Insulin. In:  LeRoith D editors. Insulin-Like Growth Factors: Molecular and Cellular Aspects. Boca Raton, FL: CRC; 1991;p. 181–219
  26. Gammeltoft S. Insulin receptors: Binding kinetics and structure-function relationships of insulin. Physiol Rev. 1984;64:1321–1378
  27. Gammeltoft S, Van Obberghen E. Protein kinase activity of the insulin receptor. Biochem J. 1986;235:1–11
  28. Zick Y. The insulin receptor: Structure and function. Crit Rev Biochem Mol Biol. 1989;24:217–269
  29. De Meyts P, Gu J-L, Smal J, et al.  The insulin receptor gene and its product: Structure and function. In:  Nerup J,  Mandrup-Poulsen T,  Hökfelt B editor. Genes and Genes Products in the Pathogenesis of Diabetes Mellitus. Amsterdam, The Netherlands: Elsevier; 1989;p. 185–203
  30. Siddle K. The insulin receptor. In:  Ashcroft FM,  Ashcroft SJH editor. Insulin: Molecular Biology to Pathology. Oxford, UK: IRL Press; 1993;p. 191–234
  31. Siddle K. The insulin receptor and type I IGF receptor: Comparison of structure and function. Prog Growth Factor Res. 1992;4:301–320
  32. Pessin JE, Treadway JL. Structural basis for ligand-dependent transmembrane signaling of the insulin and IGF-I receptor kinases. In:  LeRoith D,  Raizada MK editor. Molecular and Cellular Biology of Insulin-Like Growth Factors and Their Receptors. New York, NY: Plenum; 1989;p. 261–284
  33. Moxham C, Jacobs S. Insulin-like growth factor receptors. In:  Schofield PN editors. The Insulin-Like Growth Factors. ed 2. Structure and Biological Functions. Oxford, UK: Oxford University Press; 1992;p. 80–109
  34. Lee J, Pilch PF. The insulin receptor: Structure, function and signaling. Am J Physiol. 1994;266:C319–C334
  35. Piron MA, Michiels-Place M, Waelbroeck M, et al.  Structure-activity of insulin-induced negative cooperativity among receptor sites. In:  Brandenburg D,  Wollmer A editor. Insulin Chemistry. ed 2. Structure and Function of Insulin and Related Hormones. Berlin, Germany: de Gruyter; 1980;p. 371–391
  36. Harrington EA, Bennett MR, Fanidi A, et al.  c-Myc-induced apoptosis in fibroblasts is inhibited by specific cytokines. EMBO J. 1994;13:3286–3295
  37. Nissley P, Kiess W, Sklar MM. The insulin-like growth factor II/mannose-6-phosphate receptor. In:  LeRoith D editors. Insulin-Like Growth Factors: Molecular and Cellular Aspects. Boca Raton, FL: CRC; 1991;p. 111–150
  38. Clemmons D. Insulin-like growth factor binding proteins. In:  LeRoith D editors. Insulin-Like Growth Factors: Molecular and Cellular Aspects. Boca Raton, FL: CRC; 1991;p. 151–179
  39. Ullrich A, Bell JR, Chen EY, et al.  Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature. 1985;313:756–761
  40. Ebina Y, Ellis L, Jarnagin K, et al.  The human insulin receptor cDNA: The structural basis for hormone-activated trans-membrane signalling. Cell. 1985;40:747–758
  41. Ullrich A, Gray A, Tam AW, et al.  Insulin-like growth factor-I receptor primary structure: Comparison with insulin receptor suggests structural determinants that define functional specificity. EMBO J. 1986;5:2503–2512
  42. Czech M. Structural and functional homologies in the receptors for insulin and the insulin-like growth factors. Cell. 1982;31:8–10
  43. Bajaj M, Waterfield MD, Schlessinger J, et al.  On the tertiary structure of the extracellular domains of the epidermal growth factor and insulin receptors. Biochim Biophys Acta. 1987;916:220–226
  44. Andersen AS, Kjeldsen T, Wiberg FC, et al.  Identification of determinants that confer ligand specificity on the insulin receptor. J Biol Chem. 1992;267:13681–13686
  45. Kjeldsen T, Andersen AS, Wiberg FC, et al.  The ligand specificities of the insulin receptor and the insulin-like growth factor-I receptor reside in different regions of a common binding site. In: ed 2. Proc Natl Acad Sci USA. 88:1991;p. 4404–4408
  46. Schumacher R, Mosthaf L, Schlessinger J, et al.  Insulin and insulin-like growth factor-I binding specificity is determined by distinct regions of their cognate receptors. J Biol Chem. 1991;266:19288–19295
  47. De Meyts P, Gu J-L, Shymko RM, et al.  Identification of a ligand-binding region of the human insulin receptor encoded by the second exon of the gene. Mol Endocrinol. 1990;4:409–416
  48. Williams PF, Mynarcik DC, Qin YG, et al.  Mapping of an NH2-terminal ligand binding site of the insulin receptor by alanine scanning mutagenesis. J Biol Chem. 1995;270:1–5
  49. Wedekind F, Baer Pontzen K, Bala Mohan S, et al.  Hormone binding site of the insulin receptor: An analysis using photoaffinity-mediated avidin complexing. Biol Chem Hoppe Seyler. 1989;370:251–258
  50. Zhang B, Roth RA. A region of the insulin receptor important for ligand binding (residues 450–601) is recognized by patients' autoimmune antibodies and inhibitory monoclonal antibodies. In: ed 2. Proc Natl Acad Sci USA. 88:1991;p. 9858–9862
  51. Kadowaki H, Kadowaki T, Cama A, et al.  Mutagenesis of lysine 460 in the human insulin receptor. Effect upon receptor recycling and cooperative interactions among binding sites. J Biol Chem. 1990;265:21285–21296
  52. Schumacher R, Soos MA, Schlessinger J, et al.  Signaling-competent chimeras allow mapping of major insulin receptor binding domains determinants. J Biol Chem. 1993;268:1087–1094
  53. Christoffersen CT, Bornfeldt KE, Rotella CM, et al.  Negative cooperativity in the insulin-like growth factor-I (IGF-I) receptor and a chimeric IGF-I/insulin receptor. Endocrinology. 1994;135:472–475
  54. Kurose T, Pamshforoush M, Yshimasa Y, et al.  Cross-linking of a B25 azidophenylalanine insulin derivative to the carboxyl-terminal region of the a-subunit of the insulin receptor. J Biol Chem. 1994;269:29190–29197
  55. Stoddard BL, Biemann HP, Koshland DE. Receptors and transmembrane signaling. In: ed 2. Cold Spring Harbor Symp Quant Biol. 17:1992;p. 1–15
  56. Lee J, O'Hare T, Pilch P, et al.  Insulin receptor autophosphorylation occurs asymmetrically. J Biol Chem. 1993;268:4092–4098
  57. De Meyts P, Roth J, Neville DM, et al.  Insulin interactions with its receptors: Experimental evidence for negative cooperativity. Biochem Biophys Res Commun. 1973;55:154–161
  58. De Meyts P, Roth J. Cooperativity in ligand binding: A new method of graphic analysis. Biochem Biophys Res Commun. 1975;66:1118–1126
  59. De Meyts P, Bianco AR, Roth J. Site-site interactions among insulin receptors: Characterization of the negative cooperativity. J Biol Chem. 1976;251:1877–1888
  60. De Meyts P, Van Obberghen E, Roth J, et al.  Mapping of the residues of the receptor binding region of insulin responsible for the negative cooperativity. Nature. 1978;273:504–509
  61. Schäffer L. A model for insulin binding to the insulin receptor. Eur J Biochem. 1994;221:1127–1132
  62. Soos MA, Field CE, Siddle K. Purified hybrid insulin/insulin-like growth factor-I receptors bind insulin-like growth factor-I, but not insulin, with high affinity. Biochem J. 1993;290:419–426
  63. Zhong P, Cara JF, Tager HS. Importance of receptor occupancy, concentrations differences, and ligand exchange in the insulin-like growth factor-I receptor system. In: ed 2. Proc Natl Acad Sci USA. 90:1993;p. 11451–11455
  64. Tollefsen SE, Thompson K. The structural basis for insulin-like growth factor-I receptor high affinity binding. J Biol Chem. 1988;263:16267–16273
  65. Gu J-L, Goldfine ID, Forsayeth JR, et al.  Reversal of insulin-induced negative cooperativity by monoclonal antibodies that stabilize the slowly dissociating (“Ksuper”) state of the insulin receptor. Biochem Biophys Res Commun. 1988;150:640–701
  66. Drejer K. The bioactivity of insulin analogues from in vitro receptor binding to in vivo glucose uptake. Diabetes Metab Rev. 1992;8:259–286
  67. Chao MV. Growth factor signaling: Where is the specificity?. Cell. 1992;68:995–997
  68. Moses AC. Is insulin a growth factor?. In:  LeRoith D editors. Insulin-Like Growth Factors: Molecular and Cellular Aspects. Boca Raton, FL: CRC; 1991;p. 245–270
  69. Koontz JW, Iwahashi M. Insulin as a potent, specific growth factor in a rat hepatoma cell line. Science. 1981;211:947–949
  70. Petersen B, Blecher M. Insulin receptors and functions in normal and spontaneously transformed cloned rat hepatocytes. Exp Cell Res. 1979;120:119–125
  71. Hofmann C, Marsh JW, Miller B, et al.  Cultured hepatoma cells as a model system for studying insulin processing and biologic responsiveness. Diabetes. 1980;29:865–874
  72. Pillemer G, Lugasi-Evgi H, Scharovski G, et al.  Insulin dependence of murine lymphoid T-cell leukemia. Int J Cancer. 1992;50:80–85
  73. Skolnik EY, Lee CH, Batzer A, et al.  The domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS 1 and She: Implications for insulin control of ras signalling. EMBO J. 1993;12:1929–1936
  74. Prager D, Melmed S. Insulin and insulin-like growth factor I receptors: Are there functional differences?. Endocrinology. 1993;132:1419–1420 (editorial)
  75. Lamphere L, Lienhard GE. Components of signaling pathways for insulin and insulin-like growth factor-I in muscle myoblasts and myotubes. Endocrinology. 1992;132:2196–2202
  76. Myers MG, Sun XJ, Cheatham B, et al.  IRS-I is a common element in insulin and insulin-like growth factor-I signaling to the phosphatidylinositol 3′-kinase. Endocrinology. 1993;132:1421–1430
  77. Myers MG, Backer JM, Sun XJ, et al.  IRS-I activates phosphatidylinositol 3′-kinase by associating with src homology 2 domains of p85. In: ed 2. Proc Natl Acad Sci USA. 89:1992;p. 10350–10354
  78. Bourne H: G proteins as signaling machines, in Progress in Endocrinology. Ninth International Congress of Endocrinology, Nice, France. London, UK, Parthenon
  79. Metzger H. Transmembrane signaling: The joy of aggregation. J Immunol. 1992;149:1477–1487
  80. DeLisi C. The biophysics of ligand-receptor interactions. Q Rev Biophys. 1980;13:201–230
  81. De Meyts P, Christoffersen CT, Ursø B, et al.  Insulin potency as a mitogen is determined by the half-life of the insulin-receptor complex. Exp Clin Endocrinol. 1993;101:22–23
  82. Traverse S, Gomez N, Paterson H, et al.  Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor. Biochem J. 1992;288:351–355
  83. Nguyen TT, Scimeca JC, Filloux C, et al.  Co-regulation of the mitogen-activated protein kinase, extracellular signal-regulated kinase 1, and the 90 kDa ribosomal S6 kinase in PC12 cells. In: Distinct effects of the neurotrophic factor, nerve growth factor, and the mitogenic factor, epidermal growth factor. ed 2. J Biol Chem. 268:1993;p. 9803–9810
  84. Qiu MS, Green SH. NGF and EGF rapidly activate p21ras in PC12 cells by distinct, convergent pathways involving tyrosine phosphorylation. Neuron. 1991;7:937–946
  85. Traverse S, Seedorf K, Paterson H, et al.  EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor. Curr Biol. 1994;4:694–701
  86. Thomas R. Boolean formalisation of genetic control circuits. J Theor Biol. 1973;42:563–585
  87. Thomas R, D'Ari R. Biological Feedback. Boca Raton, FL: CRC; 1989;
  88. Thomas R. Regulatory networks seen as asynchronous automata: A logical description. J Theor Biol. 1991;153:1–23

PII: 0026-0495(95)90214-7

Metabolism - Clinical and Experimental
Volume 44 , Pages 2-11 , October 1995

Article Tools