Role of proline 193 in the insulin receptor post-translational processing

Diabetologia

Volumn 42, Issue 4, 1999, Pages 435-442

  Maggi, D ^a   Barbetti, F ^b   Cordera, R ^a,c  

^a UNIVERSITY OF GENOA   (Italy)

^b SAN RAFFAELE HOSPITAL   (Italy)

^c NONE   (Italy)

Author keywords

Calnexin; GRP78; Insulin receptor processing; Insulin resistance; P193L mutation

Indexed keywords

CALNEXIN; INSULIN RECEPTOR; PROLINE; PROTEIN TYROSINE KINASE;

ALPHA CHAIN; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; DIMERIZATION; ENDOPLASMIC RETICULUM; INSULIN BINDING; INSULIN RESISTANCE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PROCESSING; RECEPTOR UPREGULATION; STEM CELL;

AMINO ACID SUBSTITUTION; ANIMALS; BIOTINYLATION; CALCIUM-BINDING PROTEINS; CALNEXIN; CARRIER PROTEINS; COS CELLS; HEAT-SHOCK PROTEINS; INSULIN; MOLECULAR CHAPERONES; POINT MUTATION; PROLINE; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECEPTOR, INSULIN; RNA, MESSENGER; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0033054610     PISSN: 0012186X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s001250051176     Document Type: Article

References (35)

1. Rosen OM (1987) After insulin binds. Science 237: 1452-1458
2. Olson TS, Bamberger MJ, Lane MD (1988) Post-translational changes in tertiary and quaternary structure of the insulin proreceptor. Correlation with acquisition of function. J Biol Chem 263: 7342-7351
3. Accili D, Kadowaki T, Kadowaki H, Mosthaf L, Ullrich A, Taylor SI (1992) Immunoglobulin heavy chain-binding protein binds to misfolded mutant insulin receptors with mutations in the extracellular domain. J Biol Chem 267: 586-590
4. Sawa T, Imamura T, Haruta T et al. (1996) Hsp70 family molecular chaperones and mutant insulin receptor: differential binding specificities of BiP and Hsp70/Hsc70 determines accumulation or degradation of insulin receptor. Biochem Biophys Res Commun 218: 449-453
5. Bass J, Chiu G, Argon Y, Steiner DF (1998) Folding of insulin receptors monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization. J Cell Biol 141: 637-646
6. Ruddon RW, Bedows E (1997) Assisted protein folding. J Biol Chem 272: 3125-3128
7. Ou W-J, Cameron PH, Thomas DY, Bergeron JJM (1993) Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364: 771-776
8. Taylor SI, Cama A, Accili D et al. (1992) Mutations in the Insulin Receptor Gene. Endocrine Reviews 13: 566-595
9. Taylor SI, Wertheimer E, Accili D et al. (1994) Mutations in the insulin receptor gene: Update 1994. In: Negro-Vilar A, Underwood LE (eds) Endocrine Review Monographs, The Endocrine Society Press, Bethesda, Maryland, pp 58-65
10. Carrera P, Cordera R, Ferrari M et al. (1993) Substitution of Leu for Pro 193 in the insulin receptor in a patient with a genetic form of severe insulin resistance. Hum Mol Genet 2: 1437-1441
11. Takata Y, Imamura T, Haruta T et al. (1994) Leu 193 mutation in the cysteine rich region of the insulin receptor inhibits the cleavage of the insulin receptor precursor but not insulin binding. Biochem Biophys Res Commun 203: 763-772
12. Gluzman Y (1981) SV40-transformed simian cells support the replication of early SV40 mutants. Cell 23: 175-182
13. Maggi D, Andraghetti G, Carpentier J-L, Cordera R (1998) Cys 860 in the extracellular domain of insulin receptor β-subunit is critical for internalization and signal transduction. Endocrinology 139: 496-504
14. Ebina Y, Ellis L, Jarmagin K et al. (1985) The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signaling. Cell 40: 747-758
15. Ullrich A, Bell JR, Chen EY et al. (1985) Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature 313: 756-761
16. 2 microglobulin: primary structure and definition of the transcription unit. J Immunol 139: 3132-3138
17. Hammond C, Helenius A (1994) Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266: 456-458
18. Kim PS, Arvan P (1995) Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J Cell Biol 128: 29-38
19. Maggi D, Cordera R (1998) Cys 786 in the insulin receptor β subunit is required for the production of α-β dimers. Program of the 58th Annual Meeting and Scientific Session of American Diabetes Association. Diabetes, p 330A
20. Kim PS, Arvan P (1998) Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: disorders of protein trafficking and the role of ER molecular chaperones. Endocrine Reviews 19: 173-202
21. Lamandé SR, Chessler SD, Golub SB et al. (1995) Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta patients with mutations in the proal(I) chain carboxy-terminal propeptide which impair subunit assembly. J Biol Chem 270: 8642-8649
22. Arbini AA, Mannucci PM, Bauer KA (1996) A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule. Blood 87: 5085-5094
23. Katsumi A, Senda T, Yamashita Y et al. (1996) Protein C Nagoya, an elongated mutant of protein C, is retained within the endoplasmic reticulum and is associated with GRP78 and GRP94. Blood 87: 4164-4175
24. Pind S, Riordan JR, Williams DB (1994) Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 269: 12784-12788
25. Colley NJ, Cassill JA, Baker EK, Zuker CS (1995) Defective intracellular transport is the molecular basis of rhodopsin-dependent dominant retinal degeneration. Proc Natl Acad Sci USA 92: 3070-3074
26. Maassen JA, Van der Vorm ER, Van der Zon GCM, Klinkhamer MP, Krans HMJ, Moller W (1991) A leucine to proline mutation at position 233 in the insulin receptor inhibits cleavage of the proreceptor and transport to the cell surface. Biochemistry 30: 10778-10783
27. Van der Vorm ER, van der Zon GCM, Moller W, Krans HMJ, Lindhout D, Maassen JA (1992) An Arg for Gly substitution at position 31 in the insulin receptor, linked to insulin resistance, inhibits receptor processing and transport. J Biol Chem 267: 66-71
28. Wertheimer E, Barbetti F, Muggeo M, Roth J, Taylor SI (1994) Two mutations in a conserved structural motif in the insulin receptor inhibit normal folding of the insulin binding domain and intracellular transport of the receptor. J Biol Chem 269: 7587-7592
29. Yamamoto T, Bishop RW, Brown MS, Goldstein JL, Russell DW (1986) Deletion in cysteine rich region of LDL receptor impedes transport to cell surface in WHHL rabbit. Science 232: 1230-1237
30. Esser V, Russell DW (1988) Transport-deficient mutations in the low density lipoprotein receptor. Alterations in the cysteine-rich and cysteine-poor regions of the protein block intracellular transport. J Biol Chem 263: 13276-13281
31. Kim PS, Kwon O-Y, Arvan P (1996) An endoplasmic reticulum storage disease causing congenital goiter with hypothyroidism. J Cell Biol 133: 517-527
32. Hurtley SM, Bole DG, Hoover-Litty H, Helenius A, Copeland CS (1989) Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J Cell Biol 108: 2117-2126
33. Reddy P, Sparvoli A, Fagioli C, Fassina G, Sitia R (1996) Formation of reversible disulfide bonds with the matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains. EMBO J 15: 2077-2085
34. Pashmforoush M, Chan SJ, Steiner DF (1996) Structure and expression of the insulin-like peptide receptor from amphioxus. Mol Endocrinol 10: 857-866
35. Ward CW, Hoyne PA, Flegg RH (1995) Insulin and epidermal growth factor receptors contain the cysteine repeat motif found in the tumor necrosis factor receptor. Proteins 22: 141-153