Insulin receptor-associated protein tyrosine phosphatase(s): Role in insulin action

Molecular and Cellular Biochemistry

Volumn 182, Issue 1-2, 1998, Pages 79-89

  Drake, Paul G ^a   Posner, Barry I ^a,b  

^a MCGILL UNIVERSITY   (Canada)

^b Polypeptide Hormone Laboratory   (Canada)

Author keywords

Diabetes mellitus; Endosome; Insulin receptor; Peroxovanadium; Protein tyrosine phosphatase; Tyrosine kinase

Indexed keywords

GLUCOSE; INSULIN; INSULIN RECEPTOR; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; VANADIUM DERIVATIVE;

ARTICLE; DEPHOSPHORYLATION; DIABETES MELLITUS; ENDOSOME; ENZYME ACTIVITY; ENZYME REGULATION; GLUCOSE BLOOD LEVEL; INTERNALIZATION; LIVER; PROTEIN PHOSPHORYLATION; RECEPTOR BINDING; SIGNAL TRANSDUCTION;

ANIMALS; HUMANS; INSULIN; MODELS, BIOLOGICAL; PROTEIN-TYROSINE-PHOSPHATASE; RECEPTOR, INSULIN; SIGNAL TRANSDUCTION;

EID: 0031942406     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1006808100755     Document Type: Article

References (87)

1. Kahn CR: Insulin action, diabetogenes, and the cause of type 2 diabetes. Diabetes 43: 1066-1084, 1994
2. Waters SB, Pessin JE: Insulin receptor substrate 1 and 2 (IRS1 and IRS2): What a tangled web we weave. Trends Cell Biol 6: 1-4, 1996
3. Lee J, Pilch PF: The insulin receptor: Structure, function and signalling. Am J Physiol 266: C319-C334, 1994
4. White MF, Livingston JN, Backer JM, Lauris V, Dull TJ, Ullrich A: Mutation of the insulin receptor at tyrosine 960 inhibits signal transmission but does not effect its tyrosine kinase activity. Cell 54: 641-649, 1988
5. Backer JM, Schroeder GG, Kahn CR, Myers J, Wilden PA, Cahill DA, White MF: Insulin stimulation of phosphatidylinositol 3-kinase maps to insulin receptor regions required for endogenous substrate phosphorylation. J Biol Chem 267: 1367-1374, 1992
6. Danielsen G, Roth RA: Role of the juxtamembrane tyrosine in insulin receptor-mediated tyrosine phosphorylation of p60 endogenous substrates. Endocrinology 137: 5326-5331, 1996
7. White MF, Shoelson SE, Keutmann H, Kahn CR: A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor. J Biol Chem 263: 2969-2980, 1988
8. Herrera R, Rosen O: Autophosphorylation of the insulin receptor in vitro: Designation of phosphorylation sites and correlation with receptor kinase activation. J Biol Chem 261: 11980-11985, 1986
9. Kwok YC, Nemenoff RA, Powers AC, Avruch J: Kinetic properties of the insulin receptor tyrosine protein kinase: Activation through an insulin-stimulated tyrosine specific, intramolecular autophosphorylation. Arch Biochem Biophys 244: 102-113, 1986
10. Wei L, Hubbard SR, Hendrickson WA, Ellis L: Expression, characterization, and crystallization of the catalytic core of the human insulin receptor protein-tyrosine kinase domain. J Biol Chem 270: 8122-8130, 1995
11. Hubbard SR, Wei L, Ellis L, Hendrickson WA: Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372: 746-754, 1994
12. Levy-Toledano R, Taouis M, Blaettler DH, Gorden P, Taylor SI: Insulin-induced activation of phosphatidyl inositol 3-kinase. Demonstration that the p85 subunit binds directly to the COOH terminus of the insulin receptor in intact cells. J Biol Chem 269: 31178-31182, 1994
13. Hansen H, Svensson U, Zhu J, Laviola L, Giorgino F, Wolf G, Smith RJ, Riedel H: Interaction between the Grb10 SH2 domain and the insulin receptor carboxyl terminus. J Biol Chem 271: 8882-8886, 1996
14. Ugi S, Maegawa A, Olefsky JM, Shigeta Y, Kashiwagi A: Src homology 2 domains of protein tyrosine phosphatase are associated in vitro with both the insulin receptor and insulin receptor substrate-1 via different phosphotyrosine motifs. FEBS Lett 340: 216-220, 1994
15. Staubs PA, Reichart DR, Saltiel AR, Milarsky KM, Maegawa H, Berhanu P, Olefsky JM, Seely BL: Localization of the insulin receptor binding sites for the SH2 domain proteins p85, Syp, and GTPase activating protein. J Biol Chem 269: 27186-27192, 1994
16. Kharintonenov A, Schnekenburger J, Chen Z, Knyazev P, Ali S, Zwick E, White M, Ullrich A: Adapter function of protein phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction. J Biol Chem 270: 29189-29193, 1995
17. Theis RS, Ullrich A, McClain DA: Augmented mitogenesis and impaired metabolic signalling mediated by a truncated insulin receptor. J Biol Chem 264: 12820-12825, 1989
18. Takata Y, Webster NJG, Olefsky JM: Mutation of the two carboxyl-terminal tyrosines results in an insulin receptor with normal metabolic signalling but enhanced mitogenic signalling properties. J Biol Chem 266: 9135-9139, 1991
19. Baron V, Gautier N, Kalliman P, Dolais-Kitabgi J, Van Obberghen E: The carboxy-terminal domain of the insulin receptor: Its potential role in growth promoting effects. Biochemistry 30: 9365-9370, 1991
20. Takata Y, Webster NJG, Olefsky JM: Intracellular signalling by a mutant human insulin receptor lacking the carboxy-terminal tyrosine. J Biol Chem 267: 9065-9070, 1992
21. Ando A, Momomura K, Tobe K, Yamamoto-Honda R, Sakura H, Tamori Y, Kaburagi Y, Koshio O, Akunuma Y, Yazaki Y, Kasuga M, Kadowaki T: Enhanced insulin-induced mitogenesis and mitogen-activated protein kinase activities in mutant insulin receptors with substitution of two COOH-terminal tyrosine autophosphorylation sites by phenylalanine. J Biol Chem 267: 12788-12796, 1992
22. Maegawa H, McClain DA, Freidenberg G, Olefsky JM, Napier M, Lipari T, Dull TJ, Lee J, Ullich A: Properties of a human insulin receptor with a COOH-terminal truncation. 2. Truncated receptors have normal kinase activity but are defective in signalling metabolic effects. J Biol Chem 263: 8912-8917, 1988
23. Cheatham B, Kahn CR: Insulin action and the insulin signalling network. Endocrine Rev 16: 117-142, 1995
24. Sale G: Serine/threonine kinases and tyrosine phosphatases that act on the insulin receptor. Biochem Soc Trans 20: 664-670, 1992
25. Carter WG, Sullivan AC, Asamoah KA, Sale GJ: Purification and characterization of an insulin-stimulated insulin receptor serine kinase. Biochemistry 35: 14340-14351, 1996
26. Baltensperger K, Lewis RE, Woon CW, Vissavajjhala AH, Ross AH, Czech MP: Catalysis of serine and tyrosine autophosphorylation by the human insulin receptor. Proc Natl Acad Sci USA 89: 7885-7889, 1992
27. Tauer TJ, Volle DJ, Rhode SL, Lewis RE: Expression of the insulin receptor with a recombinant vaccinia virus. Biochemical evidence that the insulin receptor has intrinsic serine kinase activity. J Biol Chem 271: 331-336, 1996
28. Burgess JW, Bevan AP, Bergeron JJM, Posner BI: Intracellular trafficking and processing of ligand receptor complexes in the endosomal system. Exp Clin Endocrinol 11: 67-78, 1992
29. Baass PC, Di Guglielmo GM, Authier F, Posner BI, Bergeron JJM: Compartmentalized signal transduction by receptor tyrosine kinases. Trends Cell Biol 5: 465-470, 1995
30. Bevan AP, Drake PG, Bergeron JJM, Posner BI: Intracellular signal transduction: The role of endosomes. TEM 7: 13-21, 1996
31. Authier F, Posner BI, Bergeron JJM: Hepatic endosomes are the major physiological locus of insulin and glucagon degradation in vivo. Cell Prot Sys: 89-113, 1994
32. Authier F, Posner BI, Bergeron JJM: Insulin-degrading enzyme. Clin Invest Med 19: 149-160, 1996
33. Khan MN, Savoie S, Bergeron JJM, Posner BI: Characterization of rat liver endosomal structures. In vivo activation of insulin-stimulable receptor kinase in these structures. J Biol Chem 261: 8462-8472, 1986
34. Khan MN, Baquiran G, Brule C, Burgess J, Foster B, Bergeron JJM, Posner BI: Internalization and activation of the rat liver insulin receptor kinase in vivo. J Biol Chem 264: 12931-12940, 1989
35. Backer JM, Kahn CR, White MF: Tyrosine phosphorylation of the insulin receptor during insulin-stimulated internalization in rat hepatomacells. J Biol Chem294: 1694-1701, 1989
36. Klein HH, Freidenberg GR, Matthaei S, Olefsky JM: Insulin receptor kinase following internalization in isolated rat adipocytes. J Biol Chem 262: 10557-10564, 1987
37. Kublaoui B, Lee J, Pilch PF: Dynamics of signalling during insulin-stimulated endocytosis of its receptor in adipocytes. J Biol Chem 270: 59-65, 1995
38. Wang B, Balba Y, Knutson VP: Insulin-induced in situ phosphorylation of the insulin receptor located in the plasma membrane versus endosomes. BBRC 227: 27-34, 1996
39. Burgess JW, Wada I, Ling N, Khan MN, Bergeron JJM, Posner BI: Decrease in β- subunit phosphotyrosine correlates with internalization and activation of the endosomal insulin receptor kinase. J Biol Chem 267: 10077-10086, 1992
40. Bevan AP, Burgess JW, Drake PG, Shaver A, Bergeron JJM, Posner BI: Selective activation of the rat hepatic endosomal insulin receptor kinase. Role for the endosome in insulin signalling. J Biol Chem 270: 10784-10791, 1995
41. Kelly KL, Ruderman NB: Insulin-stimulated phosphatidylinositol 3-kinase: Association with a 185 kDa tyrosine phosphorylated protein (IRS-1) and localization in a low density membrane vesicle. J Biol Chem 268: 4391-4398, 1993
42. Rosen OM, Herrera R, Olowe Y, Petruzzelli LM, Cobb MH: Phosphorylation activates the IR tyrosine protein kinase. Proc Natl Acad Sci USA 80: 3237-3240, 1983
43. Mooney RA, Anderson DL: Phosphorylation of the insulin receptor in permeablized adipocytes is coupled to a rapid dephosphorylation reaction. J Biol Chem 264: 6850-6857, 1989
44. Mooney RA, Bordwell KL: Differential dephosphorylation of the insulin receptor and its 160 kDa substrate (pp160) in rat adipocytes. J Biol Chem 267: 14054-14060, 1992
45. Bernier M, Liotta AS, Kole HK, Shock DD, Roth J: Dynamic regulation of intact and C-terminal truncated insulin receptor phosphorylation in permeablized cells. Biochemistry 33: 4343-4351, 1994
46. Goldstein BJ: Protein-tyrosine phosphatases and the regulation of insulin action. J Cell Biochem 48: 33-42, 1992
47. Faure R, Posner BI: Differential intracellular compartmentalization of phosphotyrosine phosphatases in a glial cell line: TC-PTP Versus PTP- 1B. GLIA 9: 311-314, 1993
48. Mauro LJ, Dixon JE: 'Zip codes' direct intracellular protein tyrosine phosphatases to the correct cellular 'address'. TIBS 19: 151-155, 1994
49. Lammers R, Bossenmaier B, Cool DE, Tonks NK, Schlessinger J, Fischer EH, Ullrich A: Differential activities of protein tyrosine phosphatases in intact cells. J Biol Chem 268: 22456-22462, 1993
50. King MJ, Sale GJ: Insulin-receptor phosphotyrosyl-protein phosphatases. Biochem J 256: 893-902, 1988
51. Ahmad F, Goldstein BJ: Purification, identification and subcellular distribution of three predominant protein-tyrosine phosphatase enzymes in skeletal muscle tissue. Biochim Biophys Acta 1248: 57-69, 1995
52. Meyerovitch J, Backer JM, Csermely P, Shoelson SE, Kahn CR: Insulin differentially regulates protein phosphotyrosine phosphatase activity in rat hepatoma cells. Biochemistry 31: 10338-10344, 1992
53. Faure R, Baquiran G, Bergeron JJM, Posner BI: The dephosphorylation of insulin and epidermal growth factor receptors. The role of endosome-associated phosphotyrosine phosphatase(s). J Biol Chem 267: 11215-11221, 1992
54. Posner BI, Faure R, Burgess JW, Bevan AP, Lachance D, Zhang-Sun G, Fantus IG, Ng JN, Hall DA, Soo Lum B, Shaver A: Peroxovanadium compounds. A new class of potent phosphotyrosine phosphatase inhibitors which are insulin mimetics. J Biol Chem 269: 4596-4604, 1994
55. Bevan AP, Burgess JW, Yale J-F, Drake PG, Lachance D, Baquiran G, Shaver A, Posner BI: In vivo insulin mimetic effects of pV compounds: Role for tissue targeting in determining potency. Am J Physiol 268: E60-E66, 1995
56. Bevan AP, Drake PG, Yale J-F, Shaver A, Posner BI: Peroxovanadium compounds: Biological actions and mechanism of insulin-mimesis. Mol Cell Biochem 153: 49-58, 1995
57. Huyer G, Liu S, Kelly J, Moffat J, Payette P, Kennedy B, Tsaprailis G, Gresser MJ, Ramachandran C: Mechanism of inhibition of protein-tyrosine phosphatases by vanadate and pervanadate. J Biol Chem 272: 843-851, 1997
58. Fantus IG, Kadota S, Deragon G, Foster B, Posner BI: Pervanadate [peroxides of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor kinase. Biochemistry 28: 8864-8871, 1989
59. 2. J Biol Chem 262: 8252-8256, 1987
60. Drake PG, Bevan AP, Burgess JW, Bergeron JJM, Posner BI: A role for tyrosine phosphorylation in both activation and inhibition of the insulin receptor tyrosine kinase in vivo. Endocrinology 137: 4960-4968, 1996
61. Tavare JM, Ramos P, Ellis L: An assessment of human insulin receptor phosphorylation and exogenous kinase activity following deletion of 69 residues from the carboxy-terminus of the receptor β-subunit. Biochem Biophys Res Comm 188: 86-93, 1992
62. Kaliman P, Baron V, Alengrin F, Takata Y, Webster NJG, Olefsky JM, Van Obberghen E: The insulin receptor C-terminus is involved in the regulation of the receptor kinase activity. Biochemistry 32: 9539-9544, 1993
63. Shechter Y: Insulin-mimetic effects of vanadate: Possible implications for future treatment of diabetes. Diabetes 39: 1-5, 1990
64. Shechter Y, Li J, Meyerovitch J, Gefel D, Bruck R, Elberg G, Miller DS, Shisheva A: Insulin-like actions of vanadate are mediated in an insulin-receptor-independent manner via non-receptor protein tyrosine kinases and protein phosphotyrosine phosphatases. Mol Cell Biochem 153: 39-47, 1995
65. Tracey AS, Gressner MJ: Interaction of vanadate with phenol and tyrosine: Implications for the effects of vanadate on systems regulated by tyrosine phosphorylation. Proc Natl Acad Sci US A 83: 609-613, 1986
66. Domingo JL, Gomez M, Sanchez DJ, Llobet JM, Keen CL: Toxicology of vanadium compounds in diabetic rats: The action of chelating agents on vanadium accumulation. Mol Cell Biochem 153: 233-240, 1995
67. Yale J-F, Lachance D, Bevan AP, Vigeant C, Shaver A, Posner BI: Hypoglycemic effects of peroxovanadium compounds in Sprague-Dawley and diabetic BB rats. Diabetes 44: 1274-1279, 1995
68. Eriksson JW, Lonnroth P, Smith U: Vanadate increases cell surface insulin binding and improves insulin sensitivity in both normal and insulin-resistant rat adipocytes. Diabetologia 35: 510-516, 1992
69. Lonnroth P, Eriksson JW, Posner BI, Smith U: Peroxovanadate but not vanadate exerts insulin-like effects in human adipocytes. Diabetologia 36: 113-116, 1993
70. Eriksson JW, Lonnroth P, Posner BI, Shaver A, Wesslau C, Smith UPG: A stable peroxovanadium compound with insulin-like action in human fat cells. Diabetologia 39: 235-242, 1996
71. Hashimoto N, Feener EP, Zhang W-R, Goldstein BJ: Insulin receptor protein tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain. J Biol Chem 267: 13811-13814, 1992
72. Ramachandran C, Aebersold R, Tonks NK, Pot DA: Sequential dephosphorylation of a multiply phosphorylated insulin receptor peptide by protein tyrosine phosphatases. Biochemistry 31: 4232-4238, 1992
73. Zhang ZY, Thieme-Sefler AM, Maclean D, McNamara DJ, Dobrusin EM, Sawyer TK, Dixon JE: Substrate specificity of the protein tyrosine phosphatases. Proc Natl Acad Sci USA 90: 4446-4450, 1993
74. Cho H, Krishnaraj R, Itoh M, Kitas E, Bannwarth W, Saito H, Walsh CT: Substrate specificity's of catalytic fragments of protein tyrosine phosphatases (HPTP beta, LAR, and CD45) toward phosphotyrosylpeptide substrates and thiophosphotyrosylated peptides as inhibitors. Protein Science 2: 977-984, 1993
75. Liotta AS, Kole HK, Fales HM, Roth R, Bernier M: A synthetic tris-sulfotyrosyl dodecapeptide analogue of the insulin receptor 1146-kinase domain inhibits tyrosine dephosphorylation of the insulin receptor in situ. J Biol Chem 269: 22996-23001, 1994
76. Kole HK, Garant MJ, Kole S, Bernier M: A peptide based protein-tyrosine phosphatase inhibitor specifically enhances insulin receptor function in intact cells. J Biol Chem 271: 14302-14307, 1996
77. Tonks NK, Neel BJ: From form to function: Signalling by protein tyrosine phosphatases. Cell 87: 365-368, 1996
78. Goldstein BJ: Regulation of insulin receptor signalling by protein-tyrosine dephosphorylation. Receptor 3: 1-15, 1993
79. Zhang W-R, Li P-M, Oswald MA, Goldstein BJ: Modulation of insulin signal transduction by eutopic overexpression of the receptor-type protein tyrosine phosphatase LAR. Mol Endocrinol 10: 575-584, 1996
80. Moller NPH, Moller KB, Lammers R, Kharitonenkov A, Hoppe E, Wiberg FC, Sures I, Ullrich A: Selective down-regulation of the insulin receptor signal by protein-tyrosine phosphatases α and ∈. J Biol Chem 270: 23126-23131, 1995
81. Kenner KA, Anyanwu E, Olefsky JM, Kusari J: Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-1-stimulated signalling. J Biol Chem 271: 19810-19816, 1996
82. Kulas DT, Zhang W-R, Goldstein BJ, Furianetto RW, Mooney RA: Insulin receptor signalling is augmented by antisense inhibition of the protein tyrosine phosphatase LAR. J Biol Chem 270: 2435-2438, 1995
83. Ahmad F, Li P-M, Meyerovitch J, Goldstein BJ: Osmotic loading of neutralizing antibodies demonstrates a role for protein-tyrosine phosphatase 1B in negative regulation of insulin action pathway. J Biol Chem 270: 20503-20508, 1995
84. Rocchi S, Tartare-Deckert S, Swaka-Verhelle D, Gamha A, Van Obberghen E: Interaction of SH2-containing protein tyrosine phosphatase -2 with the insulin receptor and the insulin-like growth factor-1 receptor: Studies of the domains involved using the yeast two-hybrid system. Endocrinology 137: 4944-4952, 1996
85. Arrandale JM, Gore-Wilise A, Rocks S, Ren J-M, Zhu J, Davis A, Livingston JN, Rabin DU: Insulin signalling in mice expressing reduced levels of Syp. J Biol Chem 271: 21353-21358, 1996
86. Ahmad F, Goldstein BJ: Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells. J Biol Chem 272: 448-457, 1997
87. King GL, Johnson SM: Receptor-mediated transport of insulin across endothelial cells. Science 227: 1583-1586, 1985