ER protein quality control and proteasome-mediated protein degradation

Seminars in Cell and Developmental Biology

Volumn 10, Issue 5, 1999, Pages 507-513

  Brodsky, Jeffrey L ^a   McCracken, Ardythe A ^b  

^a UNIVERSITY OF PITTSBURGH   (United States)

^b UNIVERSITY OF NEVADA   (United States)

Author keywords

Molecular chaperones; Retro translocation ubiquitination; Yeast

Indexed keywords

CHAPERONE; CYSTEINE PROTEINASE; FUNGAL PROTEIN; MEMBRANE PROTEIN; MULTIENZYME COMPLEX; PROTEASOME; UBIQUITIN;

ENDOPLASMIC RETICULUM; GENE TRANSLOCATION; GENETICS; HUMAN; METABOLISM; REVIEW; YEAST;

CYSTEINE ENDOPEPTIDASES; ENDOPLASMIC RETICULUM; FUNGAL PROTEINS; HUMANS; MEMBRANE PROTEINS; MOLECULAR CHAPERONES; MULTIENZYME COMPLEXES; PROTEASOME ENDOPEPTIDASE COMPLEX; TRANSLOCATION, GENETIC; UBIQUITINS; YEASTS;

EID: 0033208984     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1999.0321     Document Type: Article

References (66)

1. Thomas PJ, Qu BH, Pedersen PL. Defective protein folding as a basis of human disease. Trends Biochem Sci. 20:1995;456-459.
2. Brodsky JL. Translocation of proteins across the ER membrane. Int Rev Cytol. 178:1998;277-328.
3. Gething, M-J, Sambrook J. Protein folding in the cell. Nature 35. 5:1992;33-45.
4. Hartl FU. Molecular chaperones in cellular protein folding. Nature. 381:1996;571-580.
5. McMillan DR, Gething M-J, Sambrook J. The cellular response to unfolded proteins: intercompartmental signaling. Curr Opin Biotechnol. 5:1994;5404-5545.
6. Shamu CE, Cox JS, Walter P. The unfolded protein response pathway in yeast. Trends Cell Biol. 4:1994;56-60.
7. Shamu CE. Splicing: Hacking into the unfolded protein response. Curr Biol. 8:1998;121-123.
8. Hong E, Davidson AR, Kaiser CA. A pathway for targeting soluble misfolded proteins to the yeast vacuole. J Cell Biol. 135:1996;623-633.
9. Stafford FJ, Bonifacino JS. A permeabilized cell system identifies the endoplasmic reticulum as a site of protein degradation. J Cell Biol. 115:1991;1225-1236.
10. Otsu M, Urade R, Kito M, Omura F, Kikuchi M. A possible role of ER-60 protease in the degradation of misfolded proteins in the endoplasmic reticulum. J Biol Chem. 270:1995;14958-14961.
11. McGee TP, Cheng HH, Kumagai H, Omura S, Simoni RD. Degradation of 3-hydroxymethyl-3-glutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. J Biol Chem. 271:1996;25630-25638.
12. Oliver JD, van der Wal FJ, Bulleid NJ, High S. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science. 275:1997;86-88.
13. Ward CL, Omura S, Kopito RR. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell. 83:1995;121-127.
14. Jensen TJ, Loo MA, Pind S, Williams DB, Goldberg AL, Riordan JR. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell. 83:1995;129-135.
15. Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17:1998;7151-7160.
16. Hochstrasser M. Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr Opin Cell Biol. 7:1995;215-223.
17. McCracken AA, Kruse KB. Selective protein degradation in the yeast exocytic pathway. Mol Biol Cell. 4:1993;729-736.
18. Finger A, Knop M, Wolf DH. Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Eur J Biochem. 218:1993;565-574.
19. Biederer T, Volkwein C, Sommer T. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J. 15:1996;2069-2076.
20. Hampton RY, Gardner RG, Rine J. Role of the 26s proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol Cell. 7:1996;2029-2044.
21. Hiller MM, Finger A, Schweiger M, Wolf DH. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science. 273:1996;1725-1728.
22. Werner ED, Brodsky JL, McCracken AA. Proteasome-dependent ER-ass ociated protein degradation: an unconventional route to a familiar fate. Proc Natl Acad Sci USA. 93:1996;13797-13801.
23. McCracken AA, Werner ED, Brodsky JL. Endoplasmic reticulum-assoc iated protein degradation: an unconventional route to a familiar fate. Adv Mol Cell Biol. 27:1998;165-200.
24. Qu D, Teckman JH, Perlmutter DH. Alpha 1-antitrypsin deficiency associated liver disease. J Gastroenterol Hepatol. 1:1997;404-416.
25. Liu Y, Choudhury P, Cabral CM, Sifers RN. Intracellular disposal of incompletely folded human alpha 1-antitrypsin involves release from calnexin and post-translational trimming of asparagine-linked oligosaccharides. J Biol Chem. 272:1997;7946-7951.
26. Hampton RY. Genetic analysis of hydroxymethylglutaryl-coenzyme A reductase regulated degradation. Curr Opin Lipidol. 9:1998;93-97.
27. Schubert U, Ant-n LC, Co JH, Bour S, Bennink JR, Orlowski M, Strebel K, Yewdell JW. CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway. J Virol. 72:1998;2280-2288.
28. Wiertz EJ, Jones TR, Sun L, Bogyo M, Geuze HJ, Ploegh HL. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell. 84:1996;769-779.
29. Wiertz EJ, Tortorella D, Bogyo M, Yu J, Mothes W, Jones TR, Rapoport TA, Ploegh HL. Sec61p-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature. 384:1996;432-438.
30. Hampton RY, Bhakta H. Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase. Proc Natl Acad Sci USA. 94:1997;12944-12948.
31. Plemper RK, Böhmler S, Bordallo J, Sommer T, Wolf DH. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature. 388:1997;891-895.
32. 2+required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation. Mol Biol Cell. 9:1998;1149-1162.
33. 2+transport in Saccharomyces cerevisiae. J Exp Biol. 196:1994;157-166.
34. Knop M, Finger A, Braun T, Hellmuth K, Wolf DH. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J. 15:1996;753-763.
35. Bordallo J, Plemper RK, Finger A, Wolf DH. Der3p/Hrd1p is required for endoplasmic reticulum associated degradation of misfolded lumenal and integral membrane proteins. Mol Biol Cell. 9:1998;209-222.
36. Biederer T, Volkwein C, Sommer T. Role of Cue1 in ubiquitination and degradation at the ER surface. Science. 278:1997;1806-1809.
37. McCracken AA, Karpichev IV, Ernaga JE, Werner ED, Dillin AG, Courchesne WE. Yeast mutants deficient in ER-associated protein degradation of the Z variant of alpha-1 protease inhibitor. Genetics. 144:1996;1355-1362.
38. Brodsky JL, Werner ED, Dubas ME, Goeckeler JL, Kruse KB, McCracken AA. The requirement for molecular chaperones during ER associated protein degradation (ERAD) demonstrates that protein import and export are mechanistically distinct. J Biol Chem. 274:1999;3453-3460.
39. McCracken AA, Brodsky JL. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J Cell Biol. 132:1996;291-298.
40. Caplan S, Green R, Rocco J, Kurjan J. Glycosylation and structure of the yeast MFα1 α-factor precursor is important for efficient transport through the secretory pathway. J Bacteriol. 173:1991;627-635.
41. Pilon M, Schekman R, Römisch K. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 16:1997;4540-4548.
42. Plemper RK, Egner R, Kuchler K, Wolf DH. Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome. J Biol Chem. 273:1998;32848-32856.
43. Hamman BD, Hendershot LM, Johnson AE. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocation pore before and early in translocation. Cell. 92:1998;747-758.
44. Wileman T, Carson GR, Shih FF, Concino MF, Terhorst C. The transmembrane anchor of the T-cell antigen receptor beta chain contains a structural determinant of pre-Golgi proteolysis. Cell Regul. 1:1990;907-919.
45. Skowronek MH, Hendershot LM, Haas IG. The variable domain of non-assembled Ig light chains determines both their half-life and binding to the chaperone BiP. Proc Natl Acad Sci USA. 95:1998;1574-1578.
46. Loo MA, Jensen TJ, Cui L, Hou Yx, Chang XB, Riordan JR. Perturbation of hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J. 17:1998;6879-6887.
47. Tortorella D, Story CM, Huppa JB, Wiertz EJ, Jones TR, Ploegh HL. Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential. J Cell Biol. 142:1998;365-376.
48. Kumagai H, Chun KT, Simoni RD. Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Biol Chem. 270:1995;19107-19113.
49. Gardner R, Cronin S, Leder B, Rine J, Hampton R. Sequence determi nants for regulated degradation of yeast 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol Cell. 9:1998;2611-2626.
50. Brodsky JL, McCracken AA. ER-associated and proteasome mediated p rotein degradation: how two topologically restricted events came together. Trends Cell Biol. 7:1997;151-156.
51. de Virgilio M, Weninger H, Ivessa NE. Ubiquitination is required for the retro-translocation of short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J Biol Chem. 273:1998;9734-9743.
52. Mayer TU, Braun T, Jentsch S. Role of the proteasome in membrane extraction of a short-lived ER transmembrane protein. EMBO J. 17:1998;3251-3257.
53. Bebök Z, Mazzochi C, King SA, Hong JS, Sorscher EJ. The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61β and a cytosolic, deglycosyated intermediary. J Biol Chem. 273:1998;29873-29878.
54. Johnston JA, Ward CL, Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol. 143:1998;1883-1898.
55. Qu BH, Strickland E, Thomas PJ. Cystic fibrosis: a disease of altered protein folding. J Bioenerg Biomembr. 29:1997;483-490.
56. Imamura T, Haruta T, Takata Y, Usui I, Iwata M, Ishihara H, Ishiki M, Ishibashi O, Ueno E, Sasaoka T, Kobayashi M. Involvement of heat shock protein 90 in the degradation of mutant insulin receptors by the proteasome. J Biol Chem. 273:1998;11183-11188.
57. Goldstein JL, Brown MS. Regulation of the mevalonate pathway. Nature. 343:1990;425-430.
58. Esser V, Russell DW. 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. 263:1998;13276-13281.
59. Willnow TE, Rohlmann A, Horton J, Otani H, Braun JR, Hammer RE, Herz J. RAP, a specialized chaperone, prevents ligand-induced ER retention and degradation of LDL receptor-related endocytic receptors. EMBO J. 15:1996;2632-2639.
60. DeLeo, FR, Goedken, M, McCormick, SJ, Nauseef, WM. A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome-degradation. J Clin Invest. 101:1998;2900-2909.
61. Meerovitch K, Wing S, Goltzman D. Proparathyroid hormone-related protein is associated with the chaperone protein BiP and undergoes proteasome-mediated degradation. J Biol Chem. 273:1998;21025-21030.
62. Halaban R, Cheng E, Zhang Y, Moellmann G, Hanlon D, Michalak M, Setaluri V, Hebert DN. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proc Natl Acad Sci USA. 94:1997;6210-6215.
63. Lau MM, Neufeld EF. A frameshift mutation in a patient with Tay-Sachs disease causes premature termination and defective intracellular transport of the alpha subunit of beta-hexosaminidase. J Biol Chem. 264:1989;21376-21380.
64. Lamande SR, Chessler SD, Golub SB, Byers PH, Chan D, Cole WG, Sillence DO, Bateman JF. Endoplasmic reticulum-mediated quality control of type I collagen production by cells from osteogenesis imperfecta propeptide which impair subunit assembly. J Biol Chem. 270:1995;8642-8649.
65. Knop M, Hauser N, Wolf D. N -glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast. 12:1996;1229-1238.
66. Loayza D, Tam A, Schmidt WK, Michaelis S. Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway inSaccharomyces cerevisiae. Mol Biol Cell. 9:1998;2767-2784.