Endoplasmic Reticulum-Associated Protein degradation: An Unconventional Route to a Familiar Fate

Advances in Molecular and Cell Biology

Volumn 27, Issue C, 1998, Pages 165-200

  McCracken, Ardythe A ^a   Werner, Eric D ^a   Brodsky, Jeffrey L ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0003818556     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(08)60461-0     Document Type: Article

References (208)

1. Amara J.F., Lederkremer G., and Lodish H.F. Intracellular degradation of unassembled asialoglycoprotein receptor subunits: a pre-Golgi, non-lysosomal endoproteolytic cleavage. J. CellBiol. 109 (1989) 3315-3324
2. Amitay R., Bar-Nun S., Haimovich J., Rabinovich E., and Shachar I. Post-translational regulation of IgM expression in B-lymphocytes. Selective nonlysosomal degradation of assembled secretory IgM is temperature-dependent and occurs prior to the trans-Golgi. J. Biol. Chem. 266 (1991) 12568-12573
3. Bachhawat A.K., and Pillai S. Distinct intracellular fates of membrane and secretory immunoglobulin heavy chains in a pre-B cell line. J. Cell Biol. 115 (1991) 619-624
4. Bergeron J.J.M., Brenner M.B., Thomas D.Y., and Williams D.B. Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Trends Biochem. Sci. 19 (1994) 124-128
5. Biederer T., Volkwein C., and Sommer T. Role of Cuelp in ubiquitination and degradation at the ER surface. Science 278 (1997) 1806-1809
6. Bienkowski R.S. Intracellular degradation of newly synthesized secretory proteins. Biochem. J. 214 (1983) 1-10
7. Blount P., and Merlie J.P. Mutational analysis of muscle nicotinic acetylcholine receptor subunit assembly. J. Cell Biol. 111 (1990) 2613-2622
8. Bonifacino J.S., Yuan L., and Sandoval I.V. Internalization and recycling to serotonin-containing granules of the 80K integral membrane protein exposed on the surface of secreting rat basophilic leukaemia cells. J. Cell Sci. 92 (1989) 701-712
9. Bonifacino J.S., Cosson P., and Klausner R.D. Colocalized transmembrane determinants for ER degradation and subunit assembly explain the intracellular fate of TCR chains. Cell 63 (1990) 503-513
10. Bonifacino J.S., and Klausner R.D. Degradation of proteins retained in the endoplasmic reticulum. In: Ciechanover A.J., and Schwartz A.L. (Eds). Cellular Proteolytic Systems (1994), John Wiley, New York 137-139
11. Bonnardel J.A., and Davis R.A. In HepG2 cells, translocation, not degradation, determines the fate of the de novo synthesized apolipoprotein B. J. Biol. Chem. 270 (1995) 28892-28896
12. Borchardt R.A., and Davis R.A. Intrahepatic assembly of very low density lipoproteins. Rate of transport out of the endoplasmic reticulum determines rate of secretion. J. Biol. Chem. 262 (1987) 16394-16402
13. Boren J., Wettesten M., Rustaeus S., Anderson M., and Olofsson S.O. The assembly and secretion of apoB-100 containing lipoproteins. Biochem. Soc. Trans. 21 (1993) 4487-4493
14. Bour S., Schubert U., and Strebel K. The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation. J. Virol. 69 (1995) 1510-1520
15. Brodsky J.L. Post-translational protein translocation: not all hsc70s are created equal. Trends Biochem. Sci. 21 (1996) 122-126
16. Brodsky J.L., and McCracken A.A. ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends in Cell Biol 7 (1997) 151-156
17. Brodsky J.L., and Schekman R. Heat shock cognate proteins and polypeptide translocation across the endoplasmic reticulum membrane. In: Morimoto R.I., Tissieres A., and Georgopoulos C. (Eds). The Biology of Heat Shock Proteins and Molecular Chaperones (1994), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY 85-110
18. Brodsky, J.L., Werner, E.D., Dubas, M.E., and McCracken, A.A. Chaperone Requirements During ER-Associated Protein Degradation Indicates that Protein Import and Export are Mechanistically Distinct. (Submitted).
19. Cannon K.S., Hebert D.N., and Helenius A. Glycan-dependent and independent association of vesicular stomatitis virus G protein with calnexin. J. Biol. Chem. 271 (1996) 14280-14284
20. Caplan S., Green R., Rocco J., and Kurjan J. Glycosylation and structure of the yeast MF1 -factor precursor is important for efficient transport through the secretory pathway. J. Bacteriol. 173 (1991) 627-635
21. Chen C., Bonifacino J.S., Yuan L.C., and Klausner R.D. Selective degradation of T cell antigen receptor chains retained in a pre-Golgi compartment. J. Cell Biol. 107 (1988) 2149-2161
22. Chen M.Y., Maldarelli F., Karczewski M.K., Willey R.L., and Strebel K. Human immunodeficiency virus type 1 vpu protein induces degradation of CD4 in vitro: the cytoplasmic domain of CD4 contributes to vpu sensitivity. J. Virol. 67 (1993) 3877-3884
23. Cheng S.H., Gregory R.J., Marshall J., Paul S., Souza D.W., White G.A., O'Riordan C.R., and Smith A.E. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 63 (1990) 827-834
24. Chin D.J., Gil G., Faust J.R., Goldstein J.L., Brown M.S., and Luskey K.L. Sterols accelerate degradation of hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase encoded by a constitutively expressed cDNA. Mol. Cell Biol. 5 (1985) 634-641
25. Chirico W.J., Waters M.G., and Blobel G. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 332 (1988) 805-809
26. Coukell M.B., Cameron A.M., and Adames N.R. Involvement of intracellular calcium in protein secretion in Dictyostelium discoideum. J. Cell Sci. 103 (1992) 371-380
27. Craig E.A., Gambill B.D., and Nelson R.J. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57 (1993) 402-414
28. Craig E.A., Weissman J.S., and Horwich A.L. Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell. Cell 78 (1994) 365-372
29. Danishefsky K., Hartwig R., Banerjee D., and Redman C. Intracellular fate of fibrinogen B beta chain expressed in COS cells. Biochim. Biophys. Acta 1048 (1990) 202-208
30. Danoff A., Cutler D.F., and Shields D. Heterologous expression of preprosomatostatin. Intracellular degradation of prosomatostatin-II. J. Biol. Chem. 266 (1991) 10004-10010
31. Davis R.A., Thrift R.N., Wu C.C., and Howell K.E. Apolipoprotein B is both integrated into and translocated across the endoplasmic reticulum membrane. Evidence for two functionally distinct pools. J. Biol. Chem. 265 (1990) 10005-10011
32. Davis E.C., and Mecham R.P. Selective degradation of accumulated secretory proteins in the endoplasmic reticulum. J. Biol. Chem. 271 (1996) 3787-33794
33. DeMartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X., Hisamatsu H., Tanaka K., and Slaughter C.A. Identification, purification, and characterization of a PA700-dependent activator of the proteasome. J. Biol. Chem. 271 (1996) 3112-3118
34. Deshaies R.J., Koch B.D., Werner-Washburne M.E., Craig A., and Schekman R. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332 (1988) 800-805
35. Dick L.R., Aldrich C., Jameson S.D., Moomaw C.R., Pramanik B.C., Doyle C.K., DeMartino G.N., Bevan J.J., Formen J.M., and Slaughter C.A. Proteolytic processing of ovalbumin and b-galactosidase by the proteasome to yield antigenic peptides. J. Immunol. 152 (1994) 3884-3894
36. Dixon J.L., Furukawa S., and Ginsberg H.N. Oleate stimulates secretion of apolipoprotein B-containing lipoproteins from Hep G2 cells by inhibiting early intracellular degradation of apolipoprotein B. J. Biol. Chem. 266 (1991) 5080-5086
37. Dixon J.L., and Ginsberg H.N. Regulation of hepatic secretion of apolipoprotein B-containing lipoproteins: information obtained from cultured liver cells. J. Lipid Res. 34 (1993) 167-179
38. Doyle C., Sambrook J., and Gething M.J. Analysis of progressive deletions of the transmembrane and cytoplasmic domains of influenza hemagglutinin. J. Cell Biol. 103 (1986) 1193-1204
39. Driscoll J., and Goldberg A.L. The Proteasome (multicatalytic protease) is a component of the 1500-kDa proteolytic complex which degrades ubiquitin-conjugated proteins. Proc. Natl. Acad. Sci. USA 265 (1990) 4789-4792
40. Du E.Z., Jurth J., Wang S.-L., Humiston P., and Davis R.A. Proteolysis-coupled secretion of the N terminus of apolipoprotein B; characterization of a transient, translocation arrested intermediate. J. Biol. Chem. 269 (1994) 24169-24176
41. Du E.Z., Wang S.L., Kayden H.J., Sokol R., Curtiss L.K., and Davis R.A. Translocation of apolipoprotein B across the endoplasmic reticulum is blocked in abetalipoproteinemia J. Lipid Res. 37 (1996) 1309-1315
42. Dulis B.H., Kloppel T.M., Grey H.M., and Kubo R.T. Regulation of catabolism of IgM heavy chains in a B lymphoma cell line. J. Biol. Chem. 257 (1982) 4369-4374
43. Dunten R.L., and Cohen R.E. Recognition of modified forms of ribonuclease A by the ubiquitin system. J. Biol. Chem. 264 (1989) 16739-16747
44. Economou A., and Wickner W. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell 78 (1994) 835-843
45. Edwards P.A., and Gould R.G. Turnover rate of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase as determined by use of cycloheximide. J. Biol. Chem. 247 (1972) 1520-1524
46. Elias S., Bercovich B., Kahana C., Coffino P., Fischer M., Hilt W., Wolf D.H., and Ciechanover A. Degradation of orthine decarboxylase by the mammalian and yeast 26s proteasome complexes requires all the components of the protease. Eur. J. Biochem. 229 (1995) 276-283
47. Eliasson E., Mkrtchian S., and Ingelman S.M. Hormone- and substrate-regulated intracellular degradation of cytochrome P450 (2E1) involving MgATP-activated rapid proteolysis in the endoplasmic reticulum membranes. J. Biol. Chem. 267 (1992) 15765-15769
48. Erickson R.H., Suzuki Y., Sedlmayer A., and Kim Y.S. Biosynthesis and degradation of altered immature forms of intestinal dipeptidyl peptidase IV in a rat strain lacking the enzyme. J. Biol. Chem. 267 (1992) 21623-21629
49. Esser V., and Russell D.W. 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 (1988) 13276-13281
50. Etlinger J.D., and Goldberg A.L. Proc. Natl. Acad. Sci. USA 74 (1977) 54-58
51. Fagerhol M.K., and Cox D.W. The Pi polymorphism: genetic., biochemical and clinical aspects of human alpha 1-antitrypsin. Adv. Hum. Genet. 11 (1981) 1-62
52. Faust J.R., Luskey K.L., Chin D.J., Goldstein J.L., and Brown M.S. Regulation of synthesis and degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase by low density lipoprotein and 25-hydroxycholesterol in UT-1 cells. Proc. Natl. Acad. Sci. USA 79 (1982) 5205-5209
53. Fenteany G., Standaert R.F., Lane W.S., Choi S., Corey E.J., and Schreiber S.L. Inhibition of proteasome activities and subunit-specific amino-terminal threronine modification by lactacystin. Science 286 (1995) 726-731
54. Finger A., Knopp M., and Wolf D.H. Analysis of two mutated vacuolar proteins reveals a degradation pathway in the ER or an ER-related compartment of yeast. Eur. J. Biochem. 218 (1993) 565-574
55. Fra A.M., Fagioli C., Finazzi D., Sitia R., and Alberini C.M. Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation. EMBO J. 12 (1993) 4755-4761
56. Fukuda R., Umebayashi J., Horiuchi H., Ohta A., and Takagi M. Degradation of Rhizopus niveus aspartic proteinase-I with mutated prosequences occurs in the endoplasmic reticulum of Saccharomyces cerevisiae. J. Biol. Chem. 271 (1996) 14252-14255
57. Furukawa S., Sakata N., Ginsberg H.N., and Dixon J.L. Studies of the sites of intracellular degradation of apolipoprotein B in Hep G2 cells. J. Biol. Chem. 267 (1992) 22630-22638
58. Gardner A.M., Aviel S., and Argon Y. Rapid degradation of an unassembled immunoglobulin light chain is mediated by a serine protease and occurs in a pre-Golgi compartment. J. Biol. Chem. 268 (1993) 25940-25947
59. Gething M.-J., and Sambrook J. Protein folding in the cell. Nature 355 (1992) 33-45
60. Gottesman S., and Maurizi M.R. Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol. Rev. 56 (1992) 593-621
61. Habener J.F., Kemper B., and Potts Jr. J.T. Calcium-dependent intracellular degradation of parathyroid hormone: a possible mechanism for the regulation of hormone stores. Endocrinology 97 (1975) 431-441
62. Halaban R., Cheng E., Zhang Y., Moellmann G., Hanlon D., Michalak M., Setaluri V., and Hebert D.N. 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. Halban P.A., and Wollheim C.B. Intracellular degradation of insulin stores by rat pancreatic islets in vitro. J. Biol. Chem. 255 (1980) 6003-6006
64. Hammond C., and Helenius A. Folding of VSV G protein: sequential interaction with BiP and Calnexin. Science 266 (1994) 456-458
65. Hammond C., Braakman I., and Helenius A. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. USA. 91 (1994) 913-917
66. Hampton R.Y., and Bhakta H. Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase. Proc. Natl. Acad. Sci. USA 94 (1997) 12944-12948
67. Hampton R.Y., and Rine J. Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast. J. Cell Biol. 125 (1994) 299-312
68. Hampton R.Y., Dimster-Denk D., and Rine J. The biology of HMG-CoA reductase; the pros of contra-regulation. Trends Biochem. Sci. 21 (1996) 140-145
69. Hampton R.Y., Gardener R., and Rine J. The 26s proteasome and novel proteins for the degradation of HMG-CoA reductase, an integral ER membrane protein. Mol. Biol. Cell 7 (1996) 2029-2044
70. Hannum C., Marrack P., Kubo R., and Kappler J. Thymocytes with the predicted properties of pre-T cells. J. Exp. Med. 166 (1987) 874-889
71. Haiti F.U. Molecular chaperones in cellular protein folding. Nature 381 (1996) 571-580
72. Hebert D.N., Foelimer G., and Helenius A. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the ER. Cell 81 (1995) 425-433
73. Heinemeyer W., Kleinschmidt J., Saidowsky A., Saidowsky J., Escher C., and Wolf D.H. Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. EMBO J. 10 (1991) 555-562
74. Heinemeyer W., Gruhler A., Mohrle V., Mahe Y., and Wolfe D.H. PRE2, highly homologous to the human major histocompatability complex-linked RING 10 gene, codes for a yeast proteasome subunit necessary for chrymotryptic activity and degradation of ubiquitinated proteins. J. Biol. Chem. 268 (1993) 5115-5120
75. Hendil K.B. Degradation of abnormal proteins in HeLa Cells. J. Cell Physiol. 87 (1975) 289-296
76. Hershko A., and Rose I.A. Ubiquitin-alldehyde: a general inhibitor of ubiquitin-recycling processes. Proc. Natl. Acad. Sci. USA 84 (1984) 1829-1833
77. Hiller M.M., Finger A., Schweiger M., and Wolf D.H. ER-degradation of a misfolded luminal protein occurs via the cytosolic ubiquitin-proteasome pathway. Science 273 (1996) 1725-1728
78. Hilt W., and Wolf D.H. Proteasomes: destruction as a program. Trends Biochem. Sci. 21 (1996) 96-102
79. Hochstrasser M. Ubiquitin, proteasomes and the regulation of intracellular degradation. Curr. Opin. Cell Biol. 7 (1995) 215-223
80. Hoe M.H., and Hunt R.C. Loss of one asparagine-linked oligosaccharide from human transferrin receptors results in specific cleavage and association with the endoplasmic reticulum. J. Biol. Chem. 267 (1992) 4916-4923
81. Ingram M.F., and Shelness G.S. Apolipoprotein B-100 destined for lipoprotein assembly and intracellular degradation undergoes efficient translocation across the endoplasmic reticulum membrane. J Lipid Res. 37 (1996) 2202-2214
82. Inoue S., and Simoni R.D. 3-Hydroxy-3-methylglutaryl-coenzyme A reductase and T cell receptor alpha subunit are differentially degraded in the endoplasmic reticulum. J. Biol. Chem. 267 (1992) 9080-9086
83. Jensen T.J., Loo M.A., Pind S., Williams D.B., Goldberg A.L., and Riordan J.R. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83 (1995) 129-135
84. Jentsch S. The ubiquitin conjugation system. Annu. Rev. Genet. 26 (1992) 177-205
85. Jubete Y., Maurizi M.R., and Gottesman S. Role of the heat shock protein DnaJ in the Lon-dependent degradation of naturally unstable proteins. J. Biol. Chem. 271 (1996) 30798-30803
86. Kandror O., Busconi L., Sherman M., and Goldberg A.L. Rapid degradation of an abnormal protein in E.coli involves the chaperones GroEL and GroES. J. Biol. Chem. 269 (1994) 23575-23582
87. Kelleher D.J., Kreibich G., and Gilmore R. Oligosaccharyl-transferase activity is associated with a protein complex composed of ribophorins I and II and a 48 Kd protein. Cell 69 (1992) 55-65
88. Kim P.S., and Arvan P. Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J. Cell Biol. 128 (1995) 29-35
89. Klausner R.D., Lippincott-Schwartz J., and Bonifacino J.S. The T cell antigen receptor: Insights into organelle biology. Annu. Rev. Cell Biol. 6 (1990) 403-431
90. Klausner R.D., and Sitia R. Protein degradation in the endoplasmic reticulum. Cell 62 (1990) 611-614
91. Knittler M.R., Dirks S., and Haas I.G. Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Immunology 92 (1995) 1764-1768
92. Knop M., Finger A., Braun T., Hellmuth K., and Wolf D.H. Deri, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J. 15 (1996) 753-763
93. Kuchler K., Sterne R.E., and Thorner J. Saccharomyces cerevisiae STE6 gene product: a novel pathway for protein export in eukaryotic cells. EMBO J. 8 (1989) 3973-3984
94. Kulka R.G., Raboy B., Schuster R., Parag H.A., Diamond G., Ciechanover A., and Marcus M. A Chinese hamster cell cycle mutant arrested at G2 phase has a temperature-sensitive ubiquitin-activating enzyme. J. Biol. Chem. 263 (1988) 15726-15731
95. Kurosaki T., Gander I., and Ravetch J.V. A subunit common to an IgG Fc receptor and the T-cell receptor mediates assembly through different interactions. Proc. Natl. Acad. Sci. USA 88 (1991) 3837-3841
96. Lassoued K., Illges H., Benlagha K., and Cooper M.D. Fate of surrogate light chains in B lineage cells. J. Exp. Med. 183 (1996) 421-429
97. Lau M.M., and Neufeld E.F. 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
98. Le A., Graham K.S., and Sifers R.N. Intracellular degradation of the transport-impaired human PiZ alpha 1-antitrypsin variant. Biochemical mapping of the degradative event among compartments of the secretory pathway. J. Biol. Chem. 265 (1990) 14001-14007
99. Le A., Ferrell G.A., Dishon D.S., Le Q.Q., and Sifers R.N. Soluble aggregates of the human PiZ alpha 1-antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis. J. Biol. Chem. 267 (1992) 1072-1080
100. Lee D.H., Sherman M.Y., and Goldberg A.L. Involvement of the molecular chaperone Ydjl in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae. Mol. Cell. Biol. 16 (1996) 4773-4781
101. Lederkremer G.Z., and Lodish H.F. An alternatively spliced mini exon alters the subcellular fate of the human asialoglycoprotein receptor H2 subunit. Endoplasmic reticulum retention and degradation or cell surface expression. J. Biol. Chem. 266 (1991) 1237-1244
102. Leiper J.M., Harrison G.B., Harrrison J.D., Bayliss J., Scott R., and Pease R.J. Systematic expression of the complete coding sequence of apoB-100 does not reveal transmembrane determinants. J. Lipid Res. 37 (1996) 2215-2231
103. Leonard D.A., and Chen H.W. ATP-dependent degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in permeabilized cells. J. Biol. Chem. 262 (1987) 7914-7919
104. Lippincott-Schwartz S.J., Bonifacino J.S., Yuan L.C., and Klausner R.D. Degradation from the endoplasmic reticulum: disposing of newly synthesized proteins. Cell 54 (1988) 209-220
105. Loayza, D., Tan, A., & Michaelis, S. Yeast ste6 mutants unable to exit from the ER may define two distinct steps in ER quality control. (Submitted).
106. Lobell R.B., Arm J.P., Raizman M.B., Austen K.F., and Katz H.R. Intracellular degradation of Fc gamma RIII in mouse bone marrow culture-derived progenitor mast cells prevents its surface expression and associated function. J. Biol. Chem. 268 (1993) 1207-1212
107. Lukacs G.L., Mohamed A., Kartner N., Chang X.-B., Riordan J.R., and Grinstein S. Conformational maturation of CFTR but not its mutant counterpart (D508) occurs in the endoplasmic reticulum and requires ATP. EMBO J. 13 (1994) 6076-6086
108. McCracken A.A. Trafficking of secreted proteins. In: Hannover J., and Steer C. (Eds). Intracellular Trafficking of Proteins (1992), Cambridge University Press, Cambridge. England 504-548
109. McCracken A.A., and Brodsky J.L. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell Biol. 132 (1996) 291-298
110. McCracken A.A., Karpichev I.V., Ernaga J.E., Wemer E.D., Dillin A.G., and Courchesne W.E. Yeast mutants deficient in ER-associated degradation of the Z variant of a-1-protease inhibitor. Genetics 144 (1996) 1355-1362
111. McCracken A.A., and Kruse K.B. Selective protein degradation in the yeast exocytic pathway. Mol. Biol. Cell. 4 (1993) 729-736
112. McCracken A.A., Kruse K.B., Valentine J., Roberts C., Yohannes T.Z., and Brown J.L. Construction and expression of alpha-1-proteinase inhibitor mutants and the effects of these mutations on secretion of the variant inhibitors. J. Biol. Chem. 226 (1991) 7578-7582
113. McGee T.P., Cheng H.H., Humagai H., Omura S., and Simoni R.D. Degradation of HMG-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. J. Biol. Chem. 271 (1996) 25630-25638
114. Meigs T.E., and Simoni R.D. Regulated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in permeabilized cells. J. Biol. Chem. 267 (1992) 13547-13552
115. Moore S.E.H., Bauvy C., and Codogno P. Endoplasmic reticulum-to-cytosol transport of free polymannose oligosaccharides in permeabilized HepG2 cells. EMBO J. 14 (1995) 6034-6042
116. Mullins C., Lu Y., Campbell A., Fang H., and Green N. A mutation affecting signal peptidase inhibits degradation of an abnormal membrane protein in Saccharomyces cerevisiae. J. Biol. Chem. 270 (1995) 17139-17147
117. Murakami Y., Matsufuji S., Kameji T., Hayashi S., Igarashi K., Tamura T., Tanaka K., and Ichihara A. Outline decarboxylase is degraded by the 26s proteasome without ubiquitination. Nature 360 (1992) 597-599
118. Nicchitta C.V., and Blobel G. Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation. Cell 73 (1993) 989-998
119. Oda K., Wada I., Takame N., Fujiwara T., Misumi Y., and Ikehara Y. Bip/GRP78 but not calnexin associates with a precursor of glycosylphosphatidylinositol-anchored protein. Biochem. J. 316 (1996) 623-630
120. Oda K., Ikehara Y., and Omura S. Lactacystin, an inhibitor of the proteasome, blocks the degradation of a mutant precursor of glycosylphosphatidylinositol-linked protein in a pre-Golgi compartment. Biochem. Biophys. Res. Commu. 219 (1996) 800-805
121. Ogata M., Chaudhary V.K., Pastan I., and FitzGerald D.J. Processing of Pseudomonas exotoxin by a cellular protease results in the generation of a 37,000-Da toxin fragment that is translocated to the Cytosol. J. Biol. Chem. 265 (1990) 20678-20685
122. Oliver J.D., van der Wai F.J., Bulleid N.J., and High S. Interaction of the thiol-dependent reductase Erp57 with nascent glycoproteins. Science 275 (1997) 86-88
123. Olofsson L.O., Bjursell B., Boström K., Carlsson P., Elovson J., Procter A.A., Reuben M.A., and Bondjers G. Apoliporpotein B: structure, biosynthesis and role in the lipoprotein assembly process. Atherosclerosis 68 (1987) 1-17
124. Omura F., Otsu M., Yoshimori T., Tashiro Y., and Kikuchi M. Non-lysosomal degradation of misfolded human lysozyme with and without an asparagine-linked glycosylation site. Eur. J. Biochem. 210 (1992) 591-599
125. Orci L., Brown M.S., Goldstein J.L., Garcia-Segura L.M., and Anderson R.G.W. Increase in membrane cholesterol: a possible trigger for degradation of HMG CoA reductase and crystalloid endoplasmic reticulum in UT-1 cells. Cell 36 (1984) 835-845
126. Otsu M., Urade R., Kito M., Omura F., and 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
127. Ou W.-J., Cameron P.H., Thomas D.Y., and Bergeron J.J.M. Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature 364 (1993) 771-776
128. Parlati F., Dominguez M., Bergeron J.J.M., and Thomas D.Y. Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J. Biol. Chem. 270 (1995) 214-253
129. Parlati, F., Sifers, R., Bergeron, J.J.M., & Thomas, D.Y. Rescue of the secretion defective phenotype of mutnat al-antitrypsin by C-terminal deletion of calnexin in Schizosaccharomyces pombe. (Submitted).
130. Pelham H.R.B., Roberts M.L., and Lord J.M. Toxin entry: how reversible is the secretory pathway?. Trends Cell Biol. 2 (1992) 183-185
131. Pilon M., Schekman R., and Romisch K. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 16 (1997) 4540-4548
132. Pind S., Riordan J.R., and Williams D.B. Participation of the ER chaperone calnexin (p88 IP90) in the biogenesis of the CFTR. J. Biol. Chem. 269 (1994) 12784-12788
133. Plemper R.K., Bohmler S., Bordallo J., Sommer T., and Wolf D.H. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388 (1997) 891-895
134. Prouty W.F. Orthine decarboxylase inactivation in Hela Cells. J. Cell. Physiol. 89 (1976) 65-76
135. Qu D., Techman J.H., Omura S., and Perlmutter D.H. Degradation of a mutant secretory protein, al-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem. 271 (1996) 22791-22795
136. Rabinovich E., Bar-Nun S., Amitay R., Shachar I., Gur B., Taya M., and Haimovich J. Different assembly species of IgM are directed to distinct degradation sites along the secretory pathway. J. Biol. Chem. 268 (1993) 24145-24148
137. Rabinovitz M., and Fisher J.M. Characteristics on the inhibition of hemoglobin synthesis in rabbit reticulocytes by threo-a-amino-b-chlorobutyric acid. Biochem. Biophys. Acta 91 (1964) 313-322
138. Rajagopalan S., Xu Y., and Brenner M.B. Retention of unassembled components of integral membrane proteins by Calnexin. Science 263 (1994) 387-390
139. Raposo G., van Santen H.M., Leijendekker R., Geuze H.J., and Ploegh H.L. Misfolded Major Histocompatibility complex class I molecules accumulate in an expanded ER-Golgi intermediate compartment. J. Cell Biol. 131 (1995) 1403-1419
140. Razooki-Hasan H., White D.A., and Mayer R.J. Extensive destruction of newly synthesized casein in mammary explants in organ culture. Biochem. J. 202 (1982) 133-138
141. Riederer M.A., and Hinnen A. Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding. J. Bact. 173 (1991) 3539-3546
142. Riordan J.R., Rommens J.M., Kerem B.-S., Alon N., Rozmahel R., Grzelczak Z., Zielenski J., Lok S., Plavsi C.N., Chou J.-L., Drumm M.L., Iannuzzi M.C., Collins F.S., and Tsui L.-C. Identification of the Cystic Fibrosis gene: Cloning and characterisation of complementary DNA. Science 245 (1989) 1066-1073
143. Rivett A.J., Palmer A., and Knecht E. Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells. J. Histochem. Cytochem. 40 (1992) 1165-1172
144. Rivett A.J. Proteasomes: multicatalytic proteinase complexes. Biochem. J. 291 (1993) 1-10
145. Romisch K., and Schekman R. Distinct processes mediate glycoprotein and glycopeptide export from the endoplasmic reticulum in S. cerevisiae. Proc. Natl. Acad. Sci. USA 89 (1992) 7227-7231
146. Rothblatt J., Novick P., and Stevens T.H. Guidebook to the Secretory Pathway, Sambrook & Tooze (1994), Oxford University Press, New York
147. Rotundo R.L. Biogenesis of acetylcholinesterase molecular forms in muscle. Evidence for a rapidly turning over, catalytically inactive precursor pool. J. Biol. Chem. 263 (1988) 19398-19406
148. Rotundo R.L., Thomas K., Porter J.K., Benson R.J., Fernandez V.C., and Fine R.E. Intracellular transport, sorting, and turnover of acetylcholinesterase. Evidence for an endoglycosidase H-sensitive form in Golgi apparatus, sarcoplasmic reticulum, and clathrin-coated vesicles and its rapid degradation by a non-lysosomal mechanism. J. Biol. Chem. 264 (1989) 3146-3152
149. Roy S., Yu S., Banerjee D., Overton O., Mukhopadhyay G., Oddoux C., Grieninger G., and Redman C. Assembly and secretion of fibrinogen. Degradation of individual chains. J. Biol. Chem. 267 (1992) 23151-23158
150. Sakata M., Wu X., Dixon J.L., and Ginsberg H.N. Proteolysis and lipid-facilitated translocation are distinct but competitive processes diat regulate secretion of apolipoprotein B in Hep G2 cells. J. Biol. Chem. 268 (1993) 22967-22970
151. Sanchez Y., and Lindquist S.L. HSP104 required for induced thermotolerance. Science 248 (1990) 1112-1115
152. Sato R., Imanaka T., Takatsuki A., and Takano T. Degradation of newly synthesized apolipoprotein B-100 in a pre-Golgi compartment. J. Biol. Chem. 265 (1990) 11880-11884
153. Sawa T., Imamura T., Haruta T., Sasaoka T., Iskiki M., Takata Y., Morika H., Ishihara H., Usui I., and Kobayashi M. 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 (1996) 449-453
154. Schatz B., and Dobberstein B. Common principles of protein translocation across membranes. Science 271 (1996) 1519-1526
155. Schimke R.T. Regulation of protein degradation in mammalian tissues. In: Munro H.N. (Ed). Mammalian Protein Metabolism 4 (1970), New York Academic 177-228
156. Schmitz A., Maintz M., Kehle T., and Herzog V. In vivo iodination of a misfolded proinsulin reveals co-localized signals for BiP binding and for degradation in the ER. EMBO J. 14 (1995) 1091-1098
157. Schubert U., Bour S., Ferrer-Montiel A.V., Montal M., Maldarelli R., and Strebel K. The two biological activities of human immunodeficiency virus type 1 Vpu protein involve two separable structural domains. J. Virol. 70 (1996) 809-819
158. Seufert W., and Jentsch S. In vivo function of the proteasome in the ubiquitin pathway. EMBO J. 11 (1992) 3077-3080
159. Shachar I., Rabinovich E., Kerem A., and Bar-Nun S. Thiol-reducing agents and calcium perturbants alter intracellular sorting of immunoglobulin M. J. Biol. Chem. 269 (1994) 27344-27350
160. Sharp D., Blinderman L., Combs K.A., Kienzle B., Ricci B., Wager-Smith K., Gill C.M., Truck C.W., Bouma M.E., Rader D.J., Aggerbeck L.P., Gregg R.E., Gordon D.A., and Wetterau J.R. Cloning and gene defects in microsomal triglyceride transfer protein associated with abetalipoproteinaemia. Nature 365 (1993) 65-69
161. Shelness G. Microsomal signal peptidase complex. In: Rothblatt J., Novick P., and Stevens T.H. (Eds). Guidebook to the Secretory Pathway (1994), Sambrook & Tooze Publication; Oxford University Press, New York
162. Shenai R., and Wallis M. Biosynthesis and degradation of prolactin in the rat anterior pituitary gland. Biochem. J. 182 (1979) 735-743
163. Sherman M.Y., and Goldberg A.L. Involvement of the chaperonin DnaK in the rapid degradation of a mutant protein in E. coli. EMBO J. 11 (1993) 71-77
164. Shia M.A., and Lodish H.F. The two subunits of the human asialoglycoprotein receptor have different fates when expressed alone in fibroblasts. Proc. Natl. Acad. Sci. USA 86 (1989) 152-158
165. Sidman C. B lymphocyte differentiation and the control of IgM mu chain expression. Cell 23 (1981) 379-389
166. Simon S.M., Peskin C.S., and Oster G.F. What drives the translocation of proteins? Proc. Natl. Acad. Sci. USA 89 (1992) 3770-3774
167. Simpson J.C., Dascher C., Roberts L.M., Lord J.M., and Balch W.E. Ricin cytotoxicity is sensitive to recycling between the endoplasmic reticulum and the Golgi complex. J. Biol. Chem. 270 (1995) 20078-20083
168. Sitia R., Neuberger M.S., and Milstein C. Regulation of membrane IgM expression in secretory B cells: translational and post-translational events. EMBO J. 6 (1987) 3969-3977
169. Skowronek M.H., Hendershot L.M., and Haas I.G. The variable domain of nonassembled IG light chains determines both their half-life and binding to the chaperone BiP. Proc. Natl. Acad. Sci. USA 95 (1998) 1574-1578
170. Sommer T., and Jentsch S. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 365 (1993) 176-179
171. Stafford F.J., and Bonifacino J.S. A permeabilized cell system identifies the endoplasmic recticulum as a site of protein degradation. J. Bid. Chem. 115 (1991) 1225-1236
172. Stoller T.J., and Shields D. The propeptide of preprosomatostatin mediates intracellular transport and secretion of a-globin from mammalian cells. J. Cell Biol. 108 (1989) 1647-1655
173. Strebel K., Klimkait T., and Martin M.A. A novel gene of HIV-1, vpu, and its 16 kD product. Science 241 (1988) 1221-1223
174. Su K., Stoller T., Rocco J., Zemsky J., and Green R. Pre-Golgi degradation of yeast prepro-alpha-factor expressed in a mammalian cell. J. Biol. Chem. 268 (1993) 14301-14309
175. Taya M., Rabinovich E., and Haimovich J. Characterization of IgM molecules in light-chain deficient variants of a B-cell tumor. Immunol. Lett. 33 (1991) 173-177
176. Thrift R.N., Drisko J., Dueland S., Trawick J.D., and Davis R.A. Translation of apoliprotein B across the endoplasmic reticulum is blocked in a nonheptic cell line. Proc. Natl. Acad. Sci. USA 89 (1992) 9161-9165
177. Tosetti F., Ferrari N., Pfeffer U., Brigati C., and Vidali G. Regulation of plasma retinol binding protein secretion in human HepG2 cells. Exp. Cell Res. 200 (1992) 467-472
178. Tsao Y.S., Ivessa N.E., Adesnik M., Sabatini D.D., and Kreibich G. Carboxy terminally truncated forms of ribophorin I are degraded in pre-Golgi compartments by a calcium-dependent process. J. Cell Biol. 116 (1992) 57-67
179. Tsuji E., Misumi Y., Fujiwara T., Takami N., Ogata S., and Ikehara Y. An active-site mutation (Gly633->Arg) of dipeptidyl peptidase IV causes its retention and rapid degradation in the endoplasmic reticulum. Biochemistry 31 (1992) 11921-11927
180. Urade R., Nasu M., Moriyama T., Wada K., and Kito M. Protein degradation by the phosphoinositide-specific phopholipase C-a family from rat-liver endoplasmic reticulum. J. Biol. Chem. 267 (1992) 15192-15198
181. Vertel B.M., Walthers L.M., Grier B., Maine N., and Goetinck P.F. Nonomelic chondrocytes synthesize, but fail to translocate, a truncated aggrecan precursor. Nanomelic chondrocytes, but fail to translocate, a truncated aggrecan precursor. J. Cell Sci. 104 (1993) 939-948
182. Vertel B.M., Grier B.L., Li H., and Schwartz N.B. The chondrocystrophy, nanomelia: biosynthesis and processing of the defective aggrecan precursor. Biochem. J. 301 (1994) 211-216
183. Wagner I., Heike A., van Dyke L., Langer T., and Neupert W. Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13 (1994) 5135-5145
184. Wales R., Roberts L.M., and Lord J.M. Addition of an endoplasmic reticulum retrieval sequence to Ricin A chain significantly increases its cytotoxicity to mammalian cells. J. Biol. Chem. 268 (1993) 23986-23990
185. Wang C.-N., Hobman T.C., and Brindley D.N. Degradation of apolipoprotein B in cultured rat hepatocytes occurs in a post-endoplasmic reticulum compartment. J. Biol. Chem. 270 (1995) 24624-24631
186. Ward C.L., Omura S., and Kopito R.R. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83 (1995) 121-127
187. Ware F.E., Vassilakos A., Peterson P.A., Jackson M.R., Lehrman M.A., and Williams D.B. The molecular chaperone Calnexin binds GlcMan9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem. 270 (1995) 4697-4704
188. Werner E.D., Brodsky J.L., and McCracken A.A. Proteasome-dependentER-associated protein degradation: an unconventional route to a familiar fate. Proc. Natl. Acad. Sci. USA 93 (1996) 13797-13801
189. Wickner S., Gottesman S., Skowyra D., Hoskins J., McKenney K., and Mauruizi M.R. A molecular chaperone, ClpA, functions like DnaK and Dna. J. Proc. Natl. Acad. Sci. USA 91 (1994) 12218-12222
190. Wiertz E.J.H., Jones T.R., Sun L., Bogyo M., Geuze H.J., and Pleogh H.L. The human cytomegalovirus US11 gene product dislocates MHC Class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84 (1996) 769-779
191. Wiertz E.J.H., Tortorella D., Sun L., Bogyo Yu.J., Mothes W., Jones T.R.M., Rapoport T.A., and Pleogh H.L. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384 (1996) 432-438
192. Wikström L., and Lodish H.F. Non-lysosomal, pre-Golgi degradation of unassembled asialoglycoprotein receptor subunits: a TLCK- and TPCK-sensitive cleavage within the ER. J. Cell Biol. 113 (1991) 997-1007
193. Wikström L., and Lodish H.F. Endoplasmic reticulum degradation of a subunit of the asialoglycoprotein receptor in vitro. Vesicular transport from endoplasmic reticulum is unnecessary. J. Biol. Chem. 267 (1992) 5-8
194. Wikström L., and Lodish H.F. Unfolded H2b asialoglycoprotein receptor subunit polypeptides are selectively degraded within the endoplasmic reticulum. J. Biol. Chem. 268 (1993) 14412-14416
195. Wileman T., Carson G.R., Shih F.F., Concino M.F., and 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
196. Wileman T., Pettey C., and Terhorst C. Recognition for degradation in the endoplasmic reticulum and lysosomes prevents the transport of single TCR beta and CD3 delta subunits of the T-cell antigen receptor to the surface of cells. Int. Immunol. 2 (1990) 743-754
197. Wileman T., Kane L.P., and Terhorst C. Degradation of T-cell receptor chains in the endoplasmic reticulum is inhibited by inhibitors of cysteine proteases. Cell Regul. 2 (1991) 753-765
198. Wileman T., Kane L.P., Young J., Carson G.R., and Terhorst C. Associations between subunit ectodomains promote T cell antigen receptor assembly and protect against degradation in the ER. J. Cell Biol. 122 (1993) 67-78
199. Willey R.L., Maldarelli F., Martin M.A., and Strebel K. Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4. J. Virol. 66 (1992) 7193-7200
200. Winitz D., Shachar I., Elkabetz Y., Amitay R., Samuelov M., and Bar-Nun S. Degradation of distinct assembly forms of immunoglobulin M occurs in multiple sites in permeabilized B cells. J. Biol. Chem. 271 (1996) 27645-27651
201. Wu Y., Whitman I., Molmenti E., Moore K., Hippenmeyer P., and Perlmutter D.H. A lag in intracellular degradation of mutant alpha 1 -antitrypsin correlates with the liver disease phenotype inhomozygous PiZZ alpha 1-antitrypsin deficiency. Proc. Natl. Acad. Sci. USA 91 (1994) 9014-9018
202. Yang B., Hoe M.H., Black P., and Hunt R.C. Role of oligosaccharides in the processing and function of human transferrin receptors. Effect of the loss of the three N-glycosyl oligosaccharides individually or together. J. Biol. Chem. 268 (1993) 7435-7441
203. Yao Z., Tran K., and McLeod R.S. Intracellular degradation of newly synthesized apolipoprotein B. J. Lipid Res. 38 (1997) 1937-1953
204. Young J., Kane L.P., Exley M., and Wileman T. Regulation of selective protein degradation in the endoplasmic reticulum by redox potential. J. Biol. Chem. 268 (1993) 19810-19818
205. Yu H., Kaung G., Kobayashi S., and Kopito R.R. Cytosolic degradation of T-cell receptor a chains by the proteasome. J. Biol. Chem. 272 (1997) 20800-20804
206. Yuk H.H., and Lodish H.F. Enhanced folding and processing of a disulfide mutant of the human asialoglycoprotein receptor H2b subunit. J. Biol. Chem. 270 (1995) 20169-20176
207. Zhang Q., Tector M., and Salter R.D. Calnexin recognises carbohydrate and protein determinants of class I major histocompatability complex molecules. J. Biol. Chem. 270 (1995) 3944-3948
208. Zhou M., Wu X., Huang L.-S., and Ginsberg H.N. Apolipoprotein B100, an inefficiently translocated secretory protein, is bound to the cytosolic chaperone, heat shock protein 70. J. Biol. Chem. 270 (1995) 25220-25224