Protein dislocation from the endoplasmic reticulum - Pulling out the suspect

Traffic

Volumn 3, Issue 8, 2002, Pages 530-536

  Jarosch, Ernst ^a   Geiss Friedlander, Ruth ^a   Meusser, Birgit ^a   Walter, Jan ^a   Sommer, Thomas ^a  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

Author keywords

Cdc48 complex; Endoplasmic reticulum (ER); Endoplasmic reticulum associated protein degradation (ERAD); Proteasome; Proteolysis; Sec61 complex; Ubiquitin

Indexed keywords

PROTEASOME; UBIQUITIN;

CELL COMPARTMENTALIZATION; CELL MEMBRANE; COMPLEX FORMATION; CYTOPLASM; CYTOSOL; ENDOPLASMIC RETICULUM; MOLECULE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN TRANSPORT; REGULATORY MECHANISM; REVIEW;

ANIMALS; CELL CYCLE PROTEINS; ENDOPLASMIC RETICULUM; HUMANS; INTRACELLULAR MEMBRANES; MEMBRANE PROTEINS; PROTEIN TRANSPORT; UBIQUITIN;

EID: 0036704679     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-0854.2002.30803.x     Document Type: Review

References (73)

1. Fewell SW, Travers KJ, Weissman JS, Brodsky JL. The action of molecular chaperones in the early secretory pathway. Annu Rev Genet 2001;35:149-191.
2. Brodsky JL, McCracken AA. ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together. Trends Cell Biol 1997;7:151-156.
3. Hampton RY, Gardner RG, Rine J. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol Cell 1996;7:2029-2044.
4. Walter J, Urban J, Volkwein C, Sommer T. Sec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p. EMBO J 2001;20:3124-3131.
5. Braun S, Matuschewski K, Rape M, Thoms S, Jentsch S. Role of the ubiquitin-selective CDC48 (UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J 2002;21:615-621.
6. Tortorella D, Gewurz BE, Furman MH, Schust DJ, Ploegh HL. Viral subversion of the immune system. Annu Rev Immunol 2000;18:861-926.
7. Plemper RK, Wolf DH. Retrograde protein translocation. ERADication of secretory proteins in health and disease. Trends Biochem Sci 1999;24:266-270.
8. Bonifacino JS, Weissman AM. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Ann Rev Cell Dev Biol 1998:14:19-57.
9. Wiertz EJ, Tortorella D, Bogyo MYuJ, Mothes W, Jones TR, Rapoport TA, Ploegh HL. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 1996;384:432-438.
10. 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 1997;388:891-895.
11. 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 1997;16:4540-4548.
12. Nishikawa S, Fewell SW, Kato Y, Brodsky JL, Endo T. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 2001;153:1061-1069.
13. Gillece P, Luz JM, Lennarz WJ, de La Cruz FJ, Romisch K. Export of a cystein-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J Cell Biol 1999;147:1443-1456.
14. 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;269:12784-12788.
15. Loo MA, Jensen TJ, Cui L, Hou Y, Chang XB, Riordan JR. Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J 1998;17:6879-6887.
16. Meacham GC, Lu Z, King S, Sorscher E, Tousson A, Cyr DM. The Hdj2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J 1999;18:1492-1505.
17. Ellgaard L, Helenius A. ER quality control: Towards an understanding at the molecular level. Curr Opin Cell Biol 2001;13:431-437.
18. Jakob CA, Burda P, Roth J, Aebi M. Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 1998;142:1223-1233.
19. Knop M, Finger A, Braun T, Hellmuth K, Wolf DH. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J 1996;15:753-763.
20. Misselwitz B, Staeck O, Rapoport TA. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol Cell 1998;2:593-603.
21. Gardner RG, Shearer AG, Hampton RY. In vivo action of the HRD ubiquitin ligase complex: Mechanisms of endoplasmic reticulum quality control and sterol regulation. Mol Cell Biol 2001;21:4276-4291.
22. 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 1998;273:32848-32856.
23. Wilkinson BM, Tyson JR, Stirling CJ. Ssh1p determines the translocation and dislocation capacities of the yeast endoplasmic reticulum. Dev Cell 2001;1:401-409.
24. Finke K, Plath K, Panzner S, Prehn S, Rapoport TA, Hartmann E, Sommer T. A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J 1996;15:1482-1494.
25. Plath K, Mothes W, Wilkinson BM, Stirling CJ, Rapoport TA. Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 1998;94:795-807.
26. Sommer T, Jentsch S. A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature 1993;365:176-179.
27. Hochstrasser M. Evolution and function of ubiquitin-like protein-conjugation systems. Nat Cell Biol 2000;2:E153-E157.
28. Pickart CM. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001;70:503-533.
29. 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 1996;15:2069-2076.
30. Hiller MM, Finger A, Schweiger M, Wolf DH. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 1996;273:1725-1728.
31. Biederer T, Volkwein C, Sommer T. Role of Cue1p in ubiquitination and degradation at the ER surface. Science 1997;278:1806-1809.
32. Friedlander R, Jarosch E, Urban J, Volkwein C, Sommer T. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2000;2:379-384.
33. Bays NW, Gardner RG, Seelig LP, Joazeiro CA, Hampton RY. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol 2001;3:24-29.
34. Joazeiro CAP, Weissman AM. RING finger proteins. mediators of ubiquitin ligase activity. Cell 2000;102:549-552.
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 1998;9:209-222.
36. Gardner RG, Swarbrick GM, Bays NW, Cronin SR, Wilhovsky S, Seelig L, Kim C, Hampton RY. Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control of Hrd1p by Hrd3p. J Cell Biol 2000;151:69-82.
37. Plemper RK, Bordallo J, Deak PM, Taxis C, Hitt R, Wolf DH. Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retrotranslocation complex mediating protein transport for ER degradation. J Cell Sci 1999:112:4123-4134.
38. Swanson R, Locher M, Hochstrasser M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev 2001;15:2660-2674.
39. Fang S, Ferrone M, Yang C, Jensen JP, Tiwari S, Weissman AM. The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc Natl Aced Sci USA 2001;98:14422-14427.
40. Yu H, Kopito RR. The role of multiubiquitination in dislocation and degradation of the α subunit of the T cell antigen receptor. J Biol Chem 1999;274:36852-36858.
41. Rapoport TA, Jungnickel B, Kutay U. Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu Rev Biochem 1996:65:271-303.
42. Jarosch E, Taxis C, Volkwein C, Bordello J, Finley D, Wolf DH, Sommer T. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 2002;4:134-139.
43. Kikkert M, Hassink G, Barel M, Hirsch C, van der Wal FJ, Wiertz E. Ubiquitination is essential for human cytomegalovirus US11-mediated dislocation of MHC class I molecules from the endoplasmic reticulum to the cytosol. Biochem J 2001:358:369-377.
44. Shamu CE, Flierman D, Ploegh HL, Rapoport TA, Chau V. Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol Biol Cell 2001;12:2546-2555.
45. de Virgilio M, Weninger H, Ivessa NE. Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J Biol Chem 1998;273:9734-9743.
46. Lam YA, Lawson TG, Velayutharn M, Zweier JL, Pickart CM. A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 2002;416:763-767.
47. Mayer TU, Braun T, Jentsch S. Role of the proteasome in membrane extraction of a short-lived ER-transmembrane protein. EMBO J 1998;17:3251-3257.
48. Chillaron J, Haas IG. Dissociation from BiP and retrotranslocation of unassembled immunoglobulin light chains are tightly coupled to proteasome activity. Mol Biol Cell 2000;11:217-226.
49. Dai RM, Li CC. Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat Cell Biol 2001;3:740-744.
50. Rape M, Hoppe T, Gorr I, Kalocay M, Richly H, Jentsch S. Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48 (UFD1/NPL4), a ubiquitin-selective chaperone. Cell 2001;107:667-677.
51. Zhang X, Shaw A, Bates PA, Newman RH, Gowen B, Orlova E, Gorman MA, Kondo H, Dokurno P, Lally J, Leonard G, Meyer H, van Heel M, Freemont PS. Structure of the AAA ATPase p97. Mol Cell 2000;6:1473-1484.
52. Rouiller I, Butel VM, Latterich M, Milligan RA, Wilson-Kubalek EM. A major conformational change in p97 AAA ATPase upon ATP binding. Mol Cell 2000;6:1485-1490.
53. Frohlich KU, Fries HW, Rudiger M, Erdmann R, Botstein D, Mecke D. Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression. J Cell Biol 1991;114:443-453.
54. Latterich M, Frohlich KU, Schekman R. Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes. Cell 1995;82:885-893.
55. Dai RM, Chen E, Longo DL, Gorbea CM, Li CC. Involvement of valosin-containing protein, an ATPase co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha. J Biol Chem 1998;273:3562-3573.
56. Roy L, Bergeron JJ, Lavoie C, Hendriks R, Gushue J, Fazel A, Pelletier A, Morre DJ, Subramaniam VN, Hong W, Paiement J. Role of p97 and syntaxin 5 in the assembly of transitional endoplasmic reticulum. Mol Biol Cell 2000;11:2529-2542.
57. Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G. A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97 to ubiquitin and nuclear transport pathways. EMBO J 2000;19:2181-2192.
58. Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear-assembly. Nat Cell Biol 2001;3:1086-1091.
59. Johnson ES, Ma PC, Ota IM, Varshavsky A. A proteolytic pathway that recognizes ubiquitin as a degradation signal. J Biol Chem;1995:270:17442-17456.
60. Verma R, Chen S, Feldman R, Schieltz D, Yates J, Dohmen J, Deshaies RJ. Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes. Mol Biol Cell 2000;11:3425-3439.
61. Hitchcock AL, Krebber H, Frietze S, Lin A, Latterich M, Silver PA. The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol Biol Cell 2001;12:3226-3241.
62. Ye Y, Meyer HH, Rapoport TA. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 2001;414:652-656.
63. Bays NW, Wilhovsky SK, Goradia A, Hodgkiss-Harlow, K, Hampton RY. HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol Biol Cell 2001;12:4114-4128.
64. Rabinovich E, Kerem A, Frohlich KU, Diamant N, Bar-Nun S. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 2002;22:626-634.
65. Langer T. AAA proteases: cellular machines for degrading membrane proteins. Trends Biochem Sci 2000;25:247-251.
66. Ward CL, Omura S, Kopito RR. Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 1995;83:121-127.
67. Qu D, Teckman JH, Omura S, Perlmutter DH. Degradation of a mutant secretory protein, α1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J Biol Chem 1996;271:22791-22795.
68. Imai Y, Soda M, Inoue H, Hattori N, Mizuno Y, Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 2001;105:891-902.
69. Boname JM, Stevenson PG. MHC class I ubiquitination by a viral PHD/LAP finger protein. Immunity 2001;15:627-636.
70. Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 2001;3:100-105.
71. Margottin F, Bour SP, Durand H, Selig L, Benichou S, Richard V, Thomas D, Strebel K, Benarous R. A novel human WD protein, h-β TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif. Mol Cell 1998;1:565-574.
72. Schmitz A, Herrgen H, Winkler A, Herzog V. Cholera toxin is exported from microsomes by the Sec61 complex. J Cell Biol 2000;148:1203-1212.
73. Tsai B, Rodighiero C, Lencer WI, Rapoport TA. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. 2001:104:937-948.