Ubiquitylation In The Erad Pathway

Subcellular Biochemistry

Volumn 54, Issue , 2010, Pages 136-148

  Eisele, Frederik ^a   Schâfer, Antje ^a   Wolf, Dieter H ^b  

^a Universitât Stuttgart ^*

^b UNIVERSITY OF STUTTGART   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CELL CYCLE PROTEIN; PROTEASOME; SACCHAROMYCES CEREVISIAE PROTEIN;

ANIMAL; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; HUMAN; METABOLISM; UBIQUITINATION;

ADENOSINE TRIPHOSPHATASES; ANIMALS; CELL CYCLE PROTEINS; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM-ASSOCIATED DEGRADATION; HUMANS; PROTEASOME ENDOPEPTIDASE COMPLEX; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITINATION;

EID: 84855201218     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-6676-6_11     Document Type: Article

References (109)

1. Sommer T, Wolf DH. Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J 1997; 11(14):1227-1233.
2. Plemper RK, WolfDH. Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem Sci 1999; 24(7):266-270.
3. Brodsky JL, McCracken AA. ER protein quality control and proteasome-mediated protein degradation. Semin Cell Dev Biol 1999; 10(5):507-513.
4. Kostova Z, WolfDH. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J 2003; 22(10):2309-2317.
5. Hirsch C, Jarosch E, Sommer T et al. Endoplasmic reticulum-associated protein degradation—one model fits all? Biochim Biophys Acta 2004; 1695(1-3):215-223.
6. Meusser B, Hirsch C, Jarosch E et al. ERAD: the long road to destruction. Nat Cell Biol 2005; 7(8):766-772.
7. Vembar SS, Brodsky JL. One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 2008; 9(12):944-957.
8. Ellgaard L, Molinari M, Helenius A. Setting the standards: quality control in the secretory pathway. Science 1999; 286(5446):1882-1888.
9. Helenius A, Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 2004; 73:1019-1049.
10. Jakob CA, Burda P, Roth J et al. Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 1998; 142(5):1223-1233.
11. Knop M, Hauser N, Wolf DH. N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 1996; 12(12):1229-1238.
12. Clerc S, Hirsch C, Oggier DM et al. Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J Cell Biol 2009; 184(1):159-172.
13. Quan EM, Kamiya Y, Kamiya D et al. Defining the glycan destruction signal for endoplasmic reticulum-associated degradation. Mol Cell 2008; 32(6):870-877.
14. Aebi M, Bernasconi R, Clerc S et al. N-glycan structures: recognition and processing in the ER. Trends Biochem Sci 2010; 35(2):74-82.
15. Gillece P, Luz JM, Lennarz WJ et al. Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J Cell Biol 1999; 147(7):1443-1456.
16. Sakoh-Nakatogawa M, Nishikawa S, Endo T. Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradation. J Biol Chem 2009; 284(18):11815-11825.
17. Ushioda R, Hoseki J, Araki K et al. ERdj5 is required as a disulfide reductase for degradation of misfolded proteins inthe ER. Science 2008; 321(5888):569-572.
18. Denic V, Quan EM, Weissman JS. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 2006; 126(2):349-359.
19. Buschhorn BA, Kostova Z, Medicherla B et al. A genome-wide screen identifies Yos9p as essential for ER-associated degradation ofglycoproteins. FEBS Lett 2004; 577(3):422-426.
20. Gauss R, Jarosch E, Sommer T et al. A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery. Nat Cell Biol 2006; 8(8):849-854.
21. Hosokawa N, Kamiya Y, Kamiya D et al. Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J Biol Chem 2009; 284(25):17061-17068.
22. Bernasconi R, Pertel T, Luban J et al. A dual task for theXbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal. J Biol Chem 2008; 283(24):16446-16454.
23. Christianson JC, Shaler TA, Tyler RE et al. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol 2008; 10(3):272-282.
24. Mueller B, Klemm EJ, Spooner E et al. SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins. Proc Natl Acad Sci USA 2008; 105(34):12325-12330.
25. Mueller B, Lilley BN, PloeghHL. SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER. J Cell Biol 2006; 175(2):261-270.
26. Kostova Z, Wolf DH. Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation. J Cell Sci 2005; 118(Pt 7):1485-1492.
27. Spear ED, Ng DT. Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation. J Cell Biol 2005; 169(1):73-82.
28. Xie W, Kanehara K, Sayeed A et al. Intrinsic conformational determinants signal proteinmisfolding to the Hrd1/ Htm1 endoplasmic reticulum-associated degradation system. Mol Biol Cell 2009; 20(14):3317-3329.
29. Hiller MM, Finger A, Schweiger M et al. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasomepathway. Science 1996; 273(5282):1725-1728.
30. 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 1993; 218(2):565-574.
31. Plemper RK, Deak PM, Otto RT et al. Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. FEBS Lett 1999; 443(3):241-245.
32. Friedlander R, Jarosch E, Urban J et al. A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat Cell Biol 2000; 2(7):379-384.
33. Biederer T, Volkwein C, Sommer T. Role of Cue1p in ubiquitination and degradation at the ER surface. Science 1997; 278(5344):1806-1809.
34. Bordallo J, Plemper RK, Finger A et al. Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol Biol Cell 1998; 9(1):209-222.
35. Deak PM, WolfDH. Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J Biol Chem 2001; 276(14):10663-10669.
36. Bays NW, Gardner RG, Seelig LP et al. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol 2001; 3(1):24-29.
37. Bordallo J, WolfDH. A RING-H2 finger motif is essential for the function ofDer3/Hrd1 in endoplasmic reticulum associated protein degradation in the yeast Saccharomyces cerevisiae. FEBS Lett 1999; 448(2-3):244-248.
38. 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(12):2029-2044.
39. Plemper RK, Egner R, Kuchler K et al. 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(49):32848-32856.
40. Carvalho P, Goder V, Rapoport TA. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation ofER proteins. Cell 2006; 126(2):361-373.
41. Plemper RK, Bordallo J, Deak PM et al. Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation. J Cell Sci 1999; 112(Pt22):4123-4134.
42. Gardner RG, Swarbrick GM, Bays NW et al. Endoplasmic reticulum degradation requires lumen to cytosol signaling. Transmembrane control ofHrd1p by Hrd3p. J Cell Biol 2000; 151(1):69-82.
43. Hitt R, WolfDH. Der1p, a protein required for degradation of malfolded soluble proteins of the endoplasmic reticulum: topology and Der1-like proteins. FEMS Yeast Res 2004; 4(7):721-729.
44. Knop M, Finger A, Braun T et al. Der1, a novel protein specifically required for endoplasmic reticulum degradationinyeast. EMBO J 1996; 15(4):753-763.
45. Horn SC, Hanna J, Hirsch C et al. Usa1 Functions as a Scaffold of the HRD-Ubiquitin Ligase. Mol Cell 2009; 36(5):782-793.
46. Kim I, Li Y, Muniz P et al. Usa1 protein facilitates substrate ubiquitylation through two separate domains. PLoS One 2009; 4(10):e7604.
47. Younger JM, Chen L, Ren HY et al. Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 2006; 126(3):571-582.
48. Ye Y, Shibata Y, Yun C et al. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 2004; 429(6994):841-847.
49. Lilley BN, Ploegh HL. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 2004; 429(6994):834-840.
50. Oda Y, Okada T, Yoshida H et al. Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation. J Cell Biol 2006; 172(3):383-393.
51. Schâfer A, Wolf DH. Sec61p is part of the endoplasmic reticulum-associated degradation machinery. EMBO J 2009; 28(19):2874-2884.
52. Plemper RK, Bohmler S, Bordallo J et al. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 1997; 388(6645):891-895.
53. Willer M, Forte GM, Stirling CJ. Sec61p is required for ERAD-L: genetic dissection of the translocation and ERAD-L functions of Sec61P using novel derivatives of CPY. J Biol Chem 2008; 283(49):33883-33888.
54. Shearer AG, Hampton RY. Lipid-mediated, reversible misfolding of a sterol-sensing domain protein. EMBO J 2005; 24(1):149-159.
55. Sato BK, Schulz D, Do PH et al. Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Mol Cell 2009; 34(2):212-222.
56. 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(6864):652-656.
57. Jarosch E, Taxis C, Volkwein C et al. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 2002; 4(2):134-139.
58. Bays NW, Wilhovsky SK, Goradia A et al. HRD4/NPL4 is required for the proteasomal processing of ubiquitinatedERproteins. MolBiolCell 2001; 12(12):4114-4128.
59. Rabinovich E, Kerem A, Frohlich KU et al. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 2002; 22(2):626-634.
60. Braun S, Matuschewski K, Rape M et al. Role of the ubiquitin-selective CDC48(UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J 2002; 21(4):615-621.
61. Neuber O, Jarosch E, Volkwein C et al. Ubx2 links the Cdc48 complex to ER-associated protein degradation. Nat Cell Biol 2005; 7(10):993-998.
62. Schuberth C, Richly H, Rumpf S et al. Shp1 andUbx2 are adaptors ofCdc48 involved in ubiquitin-dependent protein degradation. EMBO Rep 2004; 5(8):818-824.
63. Alberts SM, Sonntag C, Schafer A et al. Ubx4 modulates cdc48 activity and influences degradation of misfolded proteins ofthe endoplasmic reticulum. J Biol Chem 2009; 284(24):16082-16089.
64. Medicherla B, Kostova Z, Schaefer A et al. A genomic screen identifies Dsk2p and Rad23p as essential components ofER-associated degradation. EMBO Rep 2004; 5(7):692-697.
65. Richly H, Rape M, Braun S et al. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 2005; 120(1):73-84.
66. Crosas B, Hanna J, Kirkpatrick DS et al. Ubiquitin chains are remodeled at the proteasome by opposing ubiquitin ligase and deubiquitinating activities. Cell 2006; 127(7):1401-1413.
67. Kohlmann S, Schafer A, Wolf DH. Ubiquitin ligase Hul5 isrequiredfor fragment-specific substrate degradation in endoplasmic reticulum-associated degradation. J Biol Chem 2008; 283(24):16374-16383.
68. Huyer G, Piluek WF, Fansler Z et al. Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation ofamiútispanningmembrane protein anda soluble luminal protein. J Biol Chem 2004; 279(37):38369-38378.
69. Vashist S, Ng DT. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J Cell Biol 2004; 165(1):41-52.
70. 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(20):2660-2674.
71. Kreft SG, Wang L, Hochstrasser M. Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI). J Biol Chem 2006;281(8):4646-4653.
72. Gnann A, Riordan JR, Wolf DH. Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast. Mol Biol Cell 2004; 15(9):4125-4135.
73. Ravid T, Kreft SG, Hochstrasser M. Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. EMBO J 2006; 25(3):533-543.
74. Metzger MB, Maurer MJ, Dancy BM et al. Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery. J Biol Chem 2008; 283(47):32302-32316.
75. Nadav E, Shmueli A, Barr H et al. A novel mammalian endoplasmic reticulum ubiquitin ligase homologous to the yeast Hrd1. Biochem Biophys Res Commun 2003; 303(1):91-97.
76. Kikkert M, Doolman R, Dai M et al. Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum. J Biol Chem 2004; 279(5):3525-3534.
77. Cattaneo M, Otsu M, Fagioli C et al. SEL1L and HRD1 are involved in the degradation of unassembled secretory Ig-mu chains. J Cell Physiol 2008; 215(3):794-802.
78. Okuda-Shimizu Y, Hendershot LM. Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp. Mol Cell 2007; 28(4):544-554.
79. Arteaga MF, Wang L, Ravid T et al. An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery. Proc Natl Acad Sci USA 2006; 103(30):11178-11183.
80. Yamasaki S, YagishitaN, Sasaki T et al. Cytoplasmic destruction ofp53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'. EMBO J 2007; 26(1):113-122.
81. Fang S, Ferrone M, Yang C et al. The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc Natl Acad Sci USA 2001; 98(25):14422-14427.
82. Chen B, Mariano J, Tsai YC et al. The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger and an E2-binding site. Proc Natl Acad Sci USA 2006; 103(2):341-346.
83. Song BL, Sever N, DeBose-Boyd RA. Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase. Mol Cell 2005; 19(6):829-840.
84. Shmueli A, Tsai YC, Yang M et al. Targeting of gp78 for ubiquitin-mediated proteasomal degradation by Hrd1: cross-talk between E3s in the endoplasmic reticulum. Biochem Biophys Res Commun 2009; 390(3):758-762.
85. Ballar P, Ors AU, Yang H et al. Differential regulation of CFTRDeltaF508 degradation by ubiquitin ligases gp78 and Hrd1. Int J Biochem Cell Biol 2009; 42(1):167-173.
86. Hassink G, Kikkert M, van Voorden S et al. TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulum. Biochem J 2005; 388(Pt 2):647-655.
87. Zavacki AM, Arrojo EDR, Freitas BC et al. The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase. Mol Cell Biol 2009; 29(19):5339-5347.
88. Dentice M, Bandyopadhyay A, Gereben B et al. The Hedgehog-inducible ubiquitin ligase subunit WSB-1 modulates thyroid hormone activation and PTHrP secretion in the developing growth plate. Nat Cell Biol 2005; 7(7):698-705.
89. Gemmill RM, West JD, Boldog F et al. The hereditary renal cell carcinoma 3; 8 translocation fuses FHIT to a patched-related gene, TRC8. Proc Natl Acad Sci USA 1998; 95(16):9572-9577.
90. Irisawa M, Inoue J, Ozawa N et al. The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8 hampers ER to Golgi transport of sterol regulatory element-binding protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces SREBP-2 cleavage. J Biol Chem 2009; 284(42):28995-29004.
91. Stagg HR, Thomas M, van denBoomen D et al. The TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ER. J Cell Biol 2009; 186(5):685-692.
92. Wiertz EJ, 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(6608):432-438.
93. Lerner M, Corcoran M, Cepeda D et al. The RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERAD. Mol Biol Cell 2007; 18(5):1670-1682.
94. Morito D, Hirao K, Oda Y et al. Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508. Mol Biol Cell 2008; 19(4):1328-1336.
95. Imai Y, Soda M, Inoue H et al. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate ofParkin. Cell 2001; 105(7):891-902.
96. Omura T, Kaneko M, Okuma Y et al. A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate ofParkin. J Neurochem 2006; 99(6):1456-1469.
97. Fewell SW, Travers KJ, Weissman JS et al. The action of molecular chaperones in the early secretory pathway. Annu Rev Genet 2001; 35:149-191.
98. Taxis C, Hitt R, Park SH et al. Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement ofERAD. J Biol Chem 2003; 278(38):35903-35913.
99. Nishikawa SI, Fewell SW, Kato Y et al. Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 2001; 153(5):1061-1070.
100. Ruddock LW, Molinari M. N-glycan processing in ER quality control. J Cell Sci 2006; 119(Pt 21):4373-4380.
101. Wang X, Ye Y, Lencer W et al. The viral E3 ubiquitin ligase mK3 uses the Derlin/p97 endoplasmic reticulum-associated degradation pathway to mediate down-regulation of major histocompatibility complex class I proteins. J Biol Chem 2006; 281(13):8636-8644.
102. Oh RS, Bai X, Rommens JM. Humanhomologs ofUbc6p ubiquitin-conjugating enzyme and phosphorylation ofHsUbc6e in response to endoplasmic reticulum stress. J Biol Chem 2006; 281(30):21480-21490.
103. Tiwari S, Weissman AM. Endoplasmic reticulum (ER)-associated degradation of T-cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s). J Biol Chem 2001; 276(19):16193-16200.
104. Schuberth C, Buchberger A. UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97. Cell Mol Life Sci 2008; 65(15):2360-2371.
105. Kothe M, Ye Y, Wagner JS et al. Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate. J Biol Chem 2005; 280(30):28127-28132.
106. Ye Y, Meyer HH, Rapoport TA. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of non-ubiquitinated polypeptide segments and polyubiquitin chains. J CellBiol 2003; 162(1):71-84.
107. Meyer HH, Wang Y, Warren G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J 2002; 21(21):5645-5652.
108. Kleijnen MF, Alarcon RM, Howley PM. The ubiquitin-associated domain of hPLIC-2 interacts with the proteasome. Mol Biol Cell 2003; 14(9):3868-3875.
109. Chen L, Madura K. Evidence for distinct functions for human DNA repair factors hHR23A andhHR23B. FEBS Lett 2006; 580(14):3401-3408.