Folding of secretory and membrane proteins

New England Journal of Medicine

Volumn 339, Issue 23, 1998, Pages 1688-1695

  Kuznetsov, Galina ^a,b   Nigam, Sanjay K ^a,c  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b EISAI RESEARCH INSTITUTE   (United States)

^c HARVARD INSTITUTES OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; BINDING PROTEIN; BLOOD CLOTTING FACTOR 7; CALNEXIN; CALRETICULIN; CARBOHYDRATE; CHAPERONE; CHORIONIC GONADOTROPIN; COLLAGEN; DISULFIDE; FIBRILLIN; FIBRINOGEN RECEPTOR; GLYCOPROTEIN; GROWTH FACTOR; HEAT SHOCK PROTEIN; HORMONE; IMMUNOGLOBULIN; LOW DENSITY LIPOPROTEIN RECEPTOR; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MEMBRANE PROTEIN; MESSENGER RNA; PROTEIN C; RECEPTOR; SCLEROPROTEIN; SECRETORY PROTEIN; THROMBOSPONDIN; THYROGLOBULIN; TRANSMEMBRANE CONDUCTANCE REGULATOR; UNINDEXED DRUG; VON WILLEBRAND FACTOR;

ALPHA 1 ANTITRYPSIN DEFICIENCY; CYSTIC FIBROSIS; ENDOPLASMIC RETICULUM; HUMAN; ISCHEMIA; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW;

ALPHA 1-ANTITRYPSIN DEFICIENCY; CYSTIC FIBROSIS; ENDOPLASMIC RETICULUM; HUMANS; ISCHEMIA; MEMBRANE PROTEINS; METABOLISM, INBORN ERRORS; MOLECULAR CHAPERONES; PROTEIN FOLDING;

EID: 0000437518     PISSN: 00284793     EISSN: None     Source Type: Journal    
DOI: 10.1056/NEJM199812033392307     Document Type: Review

References (69)

1. Anfinsen CB, Scheraga HA. Experimental and theoretical aspects of protein folding. Adv Protein Chem 1975;29:205-300.
2. Gething M-J, Sambrook J. Protein folding in the cell. Nature 1992;355: 33-45.
3. Ellis RJ. The general concept of molecular chaperones. Philos Trans R Soc Lond B Biol Sci 1993;339:257-61.
4. Haas IG. BiP - a heat shock protein involved in immunoglobulin chain assembly. Curr Top Microbiol Immunol 1991;167:71-82.
5. Nigam SK, Goldberg AL, Ho S, Rohde MF, Bush KT, Sherman MY. A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily. J Biol Chem 1994;269:1744-9.
6. Mazzarella RA, Srinivasan M, Haugejorden SM, Green M. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J Biol Chem 1990; 265:1094-101.
7. Mazzarella RA, Marcus N, Haugejorden SM, et al. Erp61 is GRP58, a stress-inducible luminal endoplasmic reticulum protein, but is devoid of phosphatidylinositide-specific phospholipase C activity. Arch Biochem Biophys 1994;308:454-60.
8. Lin H, Masso-Welch P, Di Y, Cai JW, Shen JW, Subjeck JR. The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin. Mol Biol Cell 1993;4:1109-19.
9. Freedman RB, Hawkins HC, McLaughlin SH. Protein disulfideisomerase. Methods Enzymol 1995;251:397-406.
10. Bush KT, Goldberg AL, Nigam SK. Proteasome inhibition leads to heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance. J Biol Chem 1997;272:9086-92.
11. Bergeron JJM, Brenner MB, Thomas DY, Williams DB. Calnexin: a membrane-bound chapcrone of the endoplasmic reticulum. Trends Biochem Sci 1994;19:124-8.
12. Michalak M, Milner RE, Burns K, Opas M. Calreticulin. Biochem J 1992;285:681-92.
13. Helenius A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol Biol Cell 1994;5:253-65.
14. Tatu U, Helenius A. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J Cell Biol 1997;136:555-65.
15. Lee AS. Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells. Trends Biochem Sci 1987;12:20-3.
16. Idem. Mammalian stress response: induction of the glucose-regulated protein family. Curr Opin Cell Biol 1992;4:267-73.
17. Bush KT, Hendrickson BA, Nigam SK. Induction of the FK506-binding protein, FKPB13, under conditions which misfold proteins in the endoplasmic reticulum. Biochem J 1994;303:705-8. [Erratum, Biochem J 1995;305:1031.]
18. Kuznetsov G, Bush KT, Zhang PL, Nigam SK. Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia. Proc Natl Acad Sci U S A 1996;93:8584-9.
19. Shamu CE, Cox JS, Walter P. The unfolded-protein-response pathway in yeast. Trends Cell Biol 1994;4:56-60.
20. Sidrauski C, Walter P. The transmembrane kinase Irelp is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 1997;90:1031-9.
21. Shamu CE. Splicing together the unfolded-protein response. Curr Biol 1997;7:R67-R70.
22. Melnick J, Dul JL, Argon Y. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 1994;370:373-5.
23. Blond-Elguindi S, Cwirla SE, Dower WJ, et al. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 1993;75:717-28.
24. Elliott JG, Oliver JD, High S. The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J Biol Chem 1997;272:13849-55. [Erratum, J Biol Chem 1997;272:20312.]
25. Kuznetsov G, Chen LB, Nigam SK. Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation. J Biol Chem 1994;269:22990-5.
26. Wagar G. Effect of actinomycin D on TSH-induced stimulation of thyroidal protein synthesis in the rat. Acta Endocrinol (Copenh) 1974;77:64-70.
27. Adams JC, Lawler J. Cell-type specific adhesive interactions of skeletal myoblasts with thrombospondin-1. Mol Biol Cell 1994;5:423-37.
28. Kirn PS, Arvan P. Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J Cell Biol 1995;128:29-38.
29. Kuznetsov G, Chen LB, Nigam SK. Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. J Biol Chem 1997;272:3057-63.
30. Hammond C, Helenius A. Quality control in the secretory pathway. Curr Opin Cell Biol 1995;7:523-9.
31. Hammond C, Braakman I, Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci U S A 1994;91:913-7.
32. Mellman I. Endocytosis and molecular sorting. Annu Rev Cell Dev Biol 1996;12:575-625.
33. Coux O, Tanaka K, Goldberg AL. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem 1996;65:801-47.
34. Fra A, Sitia R. The endoplasmic reticulum as a site of protein degradation. Subcell Biochem 1993;21:143-68.
35. Kopito RR. ER quality control: the cytoplasmic connection. Cell 1997;88:427-30.
36. Mitch WE, Goldberg AL. Mechanisms of muscle wasting: the role of the ubiquitin-proteasome pathway. N Engl J Med 1996;335:1897-905.
37. Werner ED, Brodsky JL, McCracken AA. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc Nad Acad Sci U S A 1996;93:13797-801.
38. Ward CL, Omura S, Kopito RR. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 1995;83:121-7.
39. 1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J Biol Chem 1996;271:22791-5.
40. Wiertz EJHJ, Tortorella D, Bogyo M, et al. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 1996;384:432-8.
41. Fisher EA, Zhou M, Mitchell DM, et al. The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70. J Biol Chem 1997;272:20427-34.
42. Doctor RB, Bacallao R, Mandel LJ. Method for recovering ATP content and mitochondrial function after chemical anoxia in renal cell cultures. Am J Physiol 1994;266:C1803-C1811.
43. Gonzalez-Flecha B, Cutrin JC, Boveris A. Time course and mechanism of oxidative stress and tissue damage in rat liver subjected to in vivo ischemia-reperfusion. J Clin Invest 1993;91:456-64.
44. Fish EM, Molitoris BA. Alterations in epithelial polarity and the pathogenesis of disease states. N Engl J Med 1994;330:1580-8.
45. 1-antitrypsin deficiency. Ann Allergy 1994;72:105-20. [Erratum, Ann Allergy 1994;72:305.]
46. Ockner RK, Boyer J, eds. Progress in liver diseases. Vol. 11. Philadelphia: W.B. Saunders, 1993:139-65.
47. Thomas PJ, Qu B-H, Pedersen PL. Defective protein folding as a basis of human disease. Trends Biochem Sci 1995;20:456-9.
48. Sferra TJ, Collins FS. The molecular biology of cystic fibrosis. Annu Rev Med 1993;44:133-44.
49. Welsh MJ, Smith AE. Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. Cell 1993;73:1251-4.
50. Yang Y, Janich S, Cohn JA, Wilson JM. The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment. Proc Natl Acad Sci U S A 1993;90:9480-4.
51. Pind S, Riordan JR, Williams DB. Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J Biol Chem 1994;269:12784-8.
52. Ward CL, Kopito RR. Intracellular turnover of cystic fibrosis transmembrane conductance regulator: inefficient processing and rapid degradation of wild-type and mutant proteins. J Biol Chem 1994;269: 25710-8.
53. - channel is functional when retained in endoplasmic reticulum of mammalian cells. J Biol Chem 1995;270:12347-50.
54. Chessler SD, Byers PH. BiP binds type I procollagen pro a chains with mutations in the carboxy-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. J Biol Chem 1993;268:18226-33.
55. Ramirez F. Fibrillin mutations in Marfan syndrome and related phenotypes. Curr Opin Genet Dev 1996;6:309-15.
56. Kielty CM, Shuttleworth CA. Fibrillin-containing microfibrils: structure and function in health and disease. Int J Biochem Cell Biol 1995;27: 747-60.
57. Aoyama T, Tynan K, Dietz HC, Francke U, Furthmayr H. Missense mutations impair intracellular processing of fibrillin and microfibril assembly in Marfan syndrome. Hum Mol Genet 1993;2:2135-40.
58. Kato A, Yamamoto K, Miyazaki S, Jung SM, Moroi M, Aoki N. Molecular basis for Glanzmann's thrombasthenia (GT) in a compound heterozygote with glycoprotein IIb gene: a proposal for the classification of GT based on the biosynthetic pathway of glycoprotein IIb-IIIa complex. Blood 1992;79:3212-8.
59. Lyons SE, Bruck ME, Bowie EJW, Ginsburg D. Impaired intracellular transport produced by a subset of type IIA von Willebrand disease mutations. J Biol Chem 1992;267:4424-30.
60. 359 Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule. Blood 1996;87:5085-94.
61. Katsumi A, Senda T, Yamashita Y, et al. Protein C Nagoya, an elongated mutant of protein C, is retained within the endoplasmic reticulum and is associated with GRP78 and GRP94. Blood 1996;87:4164-75.
62. Kaushal S, Khorana HG. Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmentosa. Biochemistry 1994;33:6121-8.
63. Lomas DA, Evans DL, Finch JT, Carrell RW. The mechanism of Z α1-antitrypsin accumulation in the liver. Nature 1992;357:605-7.
64. Hobbs HH, Russell DW, Brown MS, Goldstein JL. The LDL receptor locus in familial hypercholesterolemia: mutational analysis of a membrane protein. Annu Rev Genet 1990;24:133-70.
65. Djordjevic JT, Bieri S, Smith R, Kroon PA. A deletion in the first cysteine-rich repeat of the low-density-lipoprotein receptor leads to the formation of multiple misfolded isomers. Eur J Biochem 1996;239:214-9.
66. Deen PMT, Crocs H, van Aubel RAMH, Ginsel LA, van Os CH. Water channels encoded by mutant aquaporin-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing. J Clin Invest 1995; 95:2291-6.
67. Oksche A, Schülein R, Rutz C, et al. Vasopressin V2 receptor mutants that cause X-linked nephrogenic diabetes insipidus: analysis of expression, processing, and function. Mol Pharmacol 1996;50:820-8.
68. Marquardt T, Ullrich K, Zimmer P, Hasilik A, Deufel T, Harms E. Carbohydrate-deficient glycoprotein syndrome (CDGS) - glycosylation, folding and intracellular transport of newly synthesized glycoproteins. Eur J Cell Biol 1995;66:268-73.
69. Medeiros-Neto G, Kim PS, Yoo SE, et al. Congenital hypothyroid goiter with deficient thyroglobulin: identification of an endoplasmic reticulum storage disease with induction of molecular chaperones. J Clin Invest 1996; 98:2838-44.