Protein folding and quality control in the ER

Cold Spring Harbor Perspectives in Biology

Volumn 3, Issue 11, 2011, Pages

  Araki, Kazutaka ^a   Nagata, Kazuhiro ^a  

^a KYOTO SANGYO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CHAPERONE;

BIOLOGICAL MODEL; CALCIUM SIGNALING; CHEMISTRY; ENDOPLASMIC RETICULUM; HOMEOSTASIS; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN FOLDING; PROTEIN SYNTHESIS; PROTEIN TRANSPORT; REVIEW;

CALCIUM; CALCIUM SIGNALING; ENDOPLASMIC RETICULUM; HOMEOSTASIS; MODELS, BIOLOGICAL; MOLECULAR CHAPERONES; OXIDATION-REDUCTION; PROTEIN BIOSYNTHESIS; PROTEIN FOLDING; PROTEIN TRANSPORT;

EID: 84857612880     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a007526     Document Type: Article

References (245)

1. Aebi M, Bernasconi R, Clerc S, Molinari M. 2010. N-glycan structures: Recognition and processing in the ER. Trends Biochem Sci 35: 74-82.
2. Anelli T, Sitia R. 2008. Protein quality control in the early secretory pathway. EMBO J 27: 315-327.
3. Appenzeller-Herzog C. 2011. Glutathione-and non-glutathione-based oxidant control in the endoplasmic reticulum. J Cell Sci 124: 847-855.
4. Appenzeller-Herzog C, Ellgaard L. 2008. The human PDI family: Versatility packed into a single fold. Biochim Biophys Acta 1783: 535-548.
5. Appenzeller-Herzog C, Riemer J, Zito E, Chin KT, Ron D, Spiess M, Ellgaard L. 2010. Disulphide production by Ero1α-PDI relay is rapid and effectively regulated. EMBO J 29: 3318-3329.
6. Avezov E, Frenkel Z, Ehrlich M, Herscovics A, Lederkremer GZ. 2008. Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation. Mol Biol Cell 19: 216-225.
7. Bagola K, Mehnert M, Jarosch E, Sommer T. 2011. Protein dislocation from the ER. Biochim Biophys Acta 1808: 925-936.
8. Ballar P, Zhong Y, Nagahama M, Tagaya M, Shen Y, Fang S. 2007. Identification of SVIP as an endogenous inhibitor of endoplasmic reticulum-associated degradation. J Biol Chem 282: 33908-33914.
9. Bays NW, Gardner RG, Seelig LP, Joazeiro CA, Hampton RY. 2001a. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nature Cell Biol 3: 24-29.
10. Bays NW, Wilhovsky SK, Goradia A, Hodgkiss-Harlow K, Hampton RY. 2001b. HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins. Mol Biol Cell 12: 4114-4128.
11. Behrends C, Langer CA, Boteva R, Bottcher UM, Stemp MJ, Schaffar G, Rao BV, Giese A, Kretzschmar H, Siegers K, et al. 2006. Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol Cell 23: 887-897.
12. Bernasconi R, Molinari M. 2011. ERAD and ERAD tuning: Disposal of cargo and of ERADregulators fromthe mammalian ER. Curr Opin Cell Biol 23: 176-183.
13. Bernasconi R, Galli C, Calanca V, Nakajima T, Molinari M. 2010. Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-L S substrates. J Cell Biol 188: 223-235.
14. Blasiole DA, Davis RA, Attie AD. 2007. The physiological and molecular regulation of lipoprotein assembly and secretion. Mol Biosyst 3: 608-619.
15. Bordallo J, Plemper RK, Finger A, Wolf DH. 1998. Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol Biol Cell 9: 209-222.
16. Borgese N, Fasana E. 2011. Targeting pathways of C-tailanchored proteins. Biochim Biophys Acta 1808: 937-946.
17. Braakman I, Hoover-Litty H, Wagner KR, Helenius A. 1991. Folding of influenza hemagglutinin in the endoplasmic reticulum. J Cell Biol 114: 401-411.
18. Braun S, Matuschewski K, Rape M, Thoms S, Jentsch S. 2002. Role of the ubiquitin-selective CDC48(UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J 21: 615-621.
19. Brodsky JL. 2007. The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation). Biochem J 404: 353-363.
20. Brodsky JL. 2010. The special delivery of a tail-anchored protein: Why it pays to use a dedicated courier. Mol Cell 40: 5-7.
21. Burr ML, Cano F, Svobodova S, Boyle LH, Boname JM, Lehner PJ. 2011. HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation. Proc Natl Acad Sci 108: 2034-2039.
22. Bygrave FL, Benedetti A. 1996. What is the concentration of calcium ions in the endoplasmic reticulum? Cell Calcium 19: 547-551.
23. Cabral WA, Chang W, Barnes AM, Weis M, Scott MA, Leikin S, Makareeva E, Kuznetsova NV, Rosenbaum KN, Tifft CJ, et al. 2007. Prolyl 3-hydroxylase 1 deficiency causes a recessive metabolic bone disorder resembling lethal/severe osteogenesis imperfecta. Nat Genet 39: 359-365.
24. Cali T, Galli C, Olivari S, Molinari M. 2008. Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities. Biochem Biophys Res Commun 371: 405-410.
25. Carvalho P, Goder V, Rapoport TA. 2006. Distinct ubiquitinligase complexes define convergent pathways for the degradation of ER proteins. Cell 126: 361-373.
26. Carvalho P, Stanley AM, Rapoport TA. 2010. Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p. Cell 143: 579-591.
27. Chapman DC, Williams DB. 2010. ER quality control in the biogenesis of MHCclass I molecules. Semin Cell Dev Biol 21: 512-519.
28. Chapman E, Fry AN, Kang M. 2010. The complexities of p97 function in health and disease. Mol Biosyst 7: 700-710.
29. Chen X, Karnovsky A, Sans MD, Andrews PC, Williams JA. 2010. Molecular characterization of the endoplasmic reticulum: Insights from proteomic studies. Proteomics 10: 4040-4052.
30. Choi JW, Sutor SL, Lindquist L, Evans GL, Madden BJ, Bergen HR III, Hefferan TE, Yaszemski MJ, Bram RJ. 2009. Severe osteogenesis imperfecta in cyclophilin B-deficient mice. PLoS Genet 5: e1000750.
31. Christianson JC, Shaler TA, Tyler RE, Kopito RR. 2008. OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol 10: 272-282.
32. Chung KT, Shen Y, Hendershot LM. 2002. BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP. J Biol Chem 277: 47557-47563.
33. Churchman LS, Weissman JS. 2011. Nascent transcript sequencing visualizes transcription at nucleotide resolution. Nature 469: 368-373.
34. Claessen JH, Mueller B, Spooner E, Pivorunas VL, Ploegh HL. 2010. The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum. J Biol Chem 285: 20732-20739.
35. Clerc S, Hirsch C, Oggier DM, Deprez P, Jakob C, Sommer T, Aebi M. 2009. Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J Cell Biol 184: 159-172.
36. Coe H, Michalak M. 2009. Calcium binding chaperones of the endoplasmic reticulum. Gen Physiol Biophys 28: F96-F103.
37. Coe H, Jung J, Groenendyk J, Prins D, Michalak M. 2010. ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum. J Biol Chem 285: 6725-6738.
38. Coppari S, Altieri F, Ferraro A, Chichiarelli S, Eufemi M, Turano C. 2002. Nuclear localization and DNA interaction of protein disulfide isomerase ERp57 in mammalian cells. J Cell Biochem 85: 325-333.
39. Cortini M, Sitia R. 2010. ERp44 and ERGIC-53 synergize in coupling efficiency and fidelity of IgM polymerization and secretion. Traffic 11: 651-659.
40. Csala M, Margittai E, Banhegyi G. 2010. Redox control of endoplasmic reticulum function. Antioxid Redox Sign 13: 77-108.
41. D'Alessio C, Caramelo JJ, Parodi AJ. 2010. UDP-GlC: Glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control. Semin Cell Dev Biol 21: 491-499.
42. Dancourt J, Barlowe C. 2010. Protein sorting receptors in the early secretory pathway. Annu Rev Biochem 79: 777-802.
43. Denic V, Quan EM, Weissman JS. 2006. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126: 349-359.
44. Deveraux Q, Ustrell V, Pickart C, Rechsteiner M. 1994. A 26 S protease subunit that binds ubiquitin conjugates. J Biol Chem 269: 7059-7061.
45. Dias-Gunasekara S, Gubbens J, van Lith M, Dunne C, Williams JA, Kataky R, Scoones D, Lapthorn A, Bulleid NJ, Benham AM. 2005. Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1β. J Biol Chem 280: 33066-33075.
46. Ding WX, Yin XM. 2008. Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome. Autophagy 4: 141-150.
47. Dong M, Bridges JP, Apsley K, Xu Y, Weaver TE. 2008. ERdj4 and ERdj5 are required for endoplasmic reticulumassociated protein degradation of misfolded surfactant protein C. Mol Biol Cell 19: 2620-2630.
48. Douglas PM, Dillin A. 2010. Protein homeostasis and aging in neurodegeneration. J Cell Biol 190: 719-729.
49. Dudek J, Benedix J, Cappel S, Greiner M, Jalal C, Muller L, Zimmermann R. 2009. Functions and pathologies of BiP and its interaction partners. Cell Mol Life Sci 66: 1556-1569.
50. Eletto D, Dersh D, Argon Y. 2010. GRP94 in ER quality control and stress responses. Semin Cell Dev Biol 21: 479-485.
51. Ellgaard L, Helenius A. 2003. Quality control in the endoplasmic reticulum. Nature Rev Mol Cell Biol 4: 181-191.
52. Ellgaard L, Ruddock LW. 2005. The human protein disulphide isomerase family: Substrate interactions and functional properties. EMBO Rep 6: 28-32.
53. Enyedi B, Varnai P, Geiszt M. 2010. Redox state of the endoplasmic reticulum is controlled by Ero1L-α and intraluminal calcium. Antioxid Redox Sign 13: 721-729.
54. Ernst R, Mueller B, Ploegh HL, Schlieker C. 2009. The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Mol Cell 36: 28-38.
55. Feige MJ, Hendershot LM. 2010. Disulfide bonds in ER protein folding and homeostasis. Curr Opin Cell Biol 23: 167-175.
56. Feng W, Liu G, Allen PD, Pessah IN. 2000. Transmembrane redox sensor of ryanodine receptor complex. J Biol Chem 275: 35902-35907.
57. Finley D. 2009. Recognition and processing of ubiquitinprotein conjugates by the proteasome. Annu Rev Biochem 78: 477-513.
58. Finn RD, Mistry J, Tate J, Coggill P, Heger A, Pollington JE, Gavin OL, Gunasekaran P, Ceric G, Forslund K, et al. 2010. The Pfam protein families database. Nucleic Acids Res 38: D211-D222.
59. Frand AR, Kaiser CA. 1998. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1: 161-170.
60. Fu L, Sztul E. 2009. ER-associated complexes (ERACs) containing aggregated cystic fibrosis transmembrane conductance regulator (CFTR) are degraded by autophagy. Eur J Cell Biol 88: 215-226.
61. Fujita E, Kouroku Y, Isoai A, Kumagai H, Misutani A, Matsuda C, Hayashi YK, Momoi T. 2007. Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: Ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II). Hum Mol Genet 16: 618-629.
62. Gale M Jr, Blakely CM, Hopkins DA, Melville MW, Wambach M, Romano PR, Katze MG. 1998. Regulation of interferon-induced protein kinase PKR: Modulation of P58IPK inhibitory function by a novel protein, P52rI PK. Mol Cell Biol 18: 859-871.
63. Garbi N, Tanaka S, Momburg F, Hammerling GJ. 2006. Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57. Nat Immunol 7: 93-102.
64. Gilady SY, Bui M, Lynes EM, Benson MD, Watts R, Vance JE, Simmen T. 2010. Ero1α requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM). Cell Stress Chaperon 15: 619-629.
65. Goeckeler JL, Brodsky JL. 2010. Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation. Diabetes Obes Metab 12: 32-38.
66. Gorlach A, Klappa P, Kietzmann T. 2006. The endoplasmic reticulum: Folding, calcium homeostasis, signaling, and redox control. Antioxid Redox Sign 8: 1391-1418.
67. Gorres KL, Raines RT. 2010. Prolyl 4-hydroxylase. Crit Rev Biochem Mol Biol 45: 106-124.
68. Grinna LS, Robbins PW. 1979. Glycoprotein biosynthesis. Rat liver microsomal glucosidases which process oligosaccharides. J Biol Chem 254: 8814-8818.
69. Grove DE, Fan CY, Ren HY, Cyr DM. 2010. The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRdF508. Mol Biol Cell 22: 301-314.
70. Hagiwara M, Maegawa K, Suzuki M, Ushioda R, Araki K, Matsumoto Y, Hoseki J, Nagata K, Inaba K. 2011. Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5. Mol Cell 41: 432-444.
71. Hatahet F, Ruddock LW, Ahn K, Benham A, Craik D, Ellgaard L, Ferrari D, Ventura S. 2009. Protein disulfide isomerase:Acritical evaluation of its function in disulfide bond formation. Antioxid Redox Sign 11: 2807-2850.
72. 2+ signaling and cell survival. Cell 131: 596-610.
73. Hayashi T, Rizzuto R, Hajnoczky G, Su TP. 2009. MAM: More than just a housekeeper. Trends Cell Biol 19: 81-88.
74. Hayashi-Nishino M, Fujita N, Noda T, Yamaguchi A, Yoshimori T, Yamamoto A. 2009. A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation. Nat Cell Biol 11: 1433-1437.
75. Hebert DN, Molinari M. 2007. In and out of the ER: Protein folding, quality control, degradation, and related human diseases. Physiol Rev 87: 1377-1408.
76. Hebert DN, Garman SC, Molinari M. 2005. The glycan code of the endoplasmic reticulum: Asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol 15: 364-370.
77. Hegde RS, Kang SW. 2008. The concept of translocational regulation. J Cell Biol 182: 225-232.
78. Hegde RS, Ploegh HL. 2010. Quality and quantity control at the endoplasmic reticulum. Curr Opin Cell Biol 22: 437-446.
79. Helenius A. 1994. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol Biol Cell 5: 253-265.
80. Hendershot LM. 2004. The ER function BiP is a master regulator of ER function. Mt Sinai J Med 71: 289-297.
81. Hidvegi T, Ewing M, Hale P, Dippold C, Beckett C, Kemp C, Maurice N, Mukherjee A, Goldbach C, Watkins S, et al. 2010. An autophagy-enhancing drug promotes degradation of mutant α1-antitrypsin Z and reduces hepatic fibrosis. Science 329: 229-232.
82. Higo T, Hattori M, Nakamura T, Natsume T, Michikawa T, Mikoshiba K. 2005. Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-triphosphate receptor type 1 by ERp44. Cell 120: 85-98.
83. Hirao K, Natsuka Y, Tamura T, Wada I, Morito D, Natsuka S, Romero P, Sleno B, Tremblay LO, Herscovics A, et al. 2006. EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming. J Biol Chem 281: 9650-9658.
84. Hirsch C, Gauss R, Horn SC, Neuber O, Sommer T. 2009. The ubiquitylation machinery of the endoplasmic reticulum. Nature 458: 453-460.
85. Hoffstrom BG, Kaplan A, Letso R, Schmid RS, Turmel GJ, Lo DC, Stockwell BR. 2010. Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins. Nat Chem Biol 6: 900-906.
86. Hoseki J, Ushioda R, Nagata K. 2010. Mechanism and components of endoplasmic reticulum-associated degradation. J Biochem 147: 19-25.
87. Hosoda A, Tokuda M, Akai R, Kohno K, Iwawaki T. 2010. Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein quality control in the salivary gland. Biochem J 425: 117-125.
88. Hosokawa N, Wada I, Hasegawa K, Yorihuzi T, Tremblay LO, Herscovics A, Nagata K. 2001. A novel ER α-mannosidase-like protein accelerates ER-associated degradation. EMBO Rep 2: 415-422.
89. Hosokawa N, Wada I, Natsuka Y, Nagata K. 2006. EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded α1-antitrypsin. Genes Cells 11:465-476.
90. Hosokawa N, You Z, Tremblay LO, Nagata K, Herscovics A. 2007. Stimulation of ERAD of misfolded null HongKong α1-antitrypsin by Golgi α1,2-mannosidases. Biochem Biophys Res Commun 362: 626-632.
91. Hosokawa N, Wada I, Nagasawa K, Moriyama T, Okawa K, Nagata K. 2008. Human XTP3-B forms an endoplasmic reticulumquality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP. J Biol Chem 283: 20914-20924.
92. Hosokawa N, Kamiya Y, Kato K. 2010a. The role of MRH domain-containing lectins in ERAD. Glycobiology 20: 651-660.
93. Hosokawa N, Tremblay LO, Sleno B, Kamiya Y, Wada I, Nagata K, Kato K, Herscovics A. 2010b. EDEM1 accelerates the trimming of α1,2-linked mannose on the C branch of N-glycans. Glycobiology 20: 567-575.
94. Husnjak K, Elsasser S, Zhang N, Chen X, Randles L, Shi Y, Hofmann K, Walters KJ, Finley D, Dikic I. 2008. Proteasome subunit Rpn13 is a novel ubiquitin receptor. Nature 453: 481-488.
95. Hutt D, Balch WE. 2010. Cell biology. The proteome in balance. Science 329: 766-767.
96. Hutt DM, Powers ET, Balch WE. 2009. The proteostasis boundary in misfolding diseases of membrane traffic. FEBS Lett 583: 2639-2646.
97. Hwang C, Sinskey AJ, Lodish HF. 1992. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257: 1496-1502.
98. Inaba K, Masui S, Iida H, Vavassori S, Sitia R, Suzuki M. 2010. Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI. EMBO J 29: 3330-3343.
99. Ishida Y, Yamamoto A, Kitamura A, Lamande SR, Yoshimori T, Bateman JF, Kubota H, Nagata K. 2009. Autophagic elimination of misfolded procollagen aggregates in the endoplasmic reticulum as a means of cell protection. Mol Biol Cell 20: 2744-2754.
100. Ishikawa Y, Wirz J, Vranka JA, Nagata K, Bachinger HP. 2009. Biochemical characterization of the prolyl 3-hydroxylase 1. cartilage-associated protein. cyclophilin B complex. J Biol Chem 284: 17641-17647.
101. Ishikura S, Weissman AM, Bonifacino JS. 2010. Serine residues in the cytosolic tail of the T-cell antigen receptor α-chain mediate ubiquitination and endoplasmic reticulum-associated degradation of the unassembled protein. J Biol Chem 285: 23916-23924.
102. Iuchi Y, Okada F, Tsunoda S, Kibe N, Shirasawa N, Ikawa M, Okabe M, Ikeda Y, Fujii J. 2009. Peroxiredoxin 4 knockout results in elevated spermatogenic cell death via oxidative stress. Biochem J 419: 149-158.
103. Jarosch E. 2002. Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4: 134-139.
104. Jessop CE, Watkins RH, Simmons JJ, Tasab M, Bulleid NJ. 2009. Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins. J Cell Sci 122: 4287-4295.
105. Jin Y, Awad W, Petrova K, Hendershot LM. 2008. Regulated release of ERdj3 from unfolded proteins by BiP. EMBO J 27: 2873-2882.
106. Jo Y, Debose-Boyd RA. 2010. Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase. Crit Rev Biochem Mol Biol 45: 185-198.
107. John LM, Lechleiter JD, Camacho P. 1998. Differential modulation of SERCA2 isoforms by calreticulin. J Cell Biol 142: 963-973.
108. Johnson AE, Van Waes MA. 1999. The translocon: A dynamic gateway at the ER membrane. Annu Rev Cell Dev Biol 15: 799-842.
109. Kamiya Y, Kamiya D, Yamamoto K, Nyfeler B, Hauri HP, Kato K. 2008. Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36. J Biol Chem 283: 1857-1861.
110. Kampinga HH, Craig EA. 2010. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 11: 579-592.
111. Kanehara K, Kawaguchi S, Ng DT. 2007. The EDEM and Yos9p families of lectin-like ERAD factors. Semin Cell Dev Biol 18: 743-750.
112. Karala AR, Lappi AK, Saaranen MJ, Ruddock LW. 2009. Efficient peroxide-mediated oxidative refolding of a protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum. Antioxid Redox Sign 11: 963-970.
113. Kawaguchi S, Ng DT. 2007. SnapShot: ER-associated protein degradation pathways. Cell 129: 1230.
114. Kim I, Rodriguez-Enriquez S, Lemasters JJ. 2007. Selective degradation of mitochondria by mitophagy. Arch Biochem Biophys 462: 245-253.
115. Kimura T, Horibe T, Sakamoto C, Shitara Y, Fujiwara F, Komiya T, Yamamoto A, Hayano T, Takahashi N, Kikuchi M. 2008. Evidence for mitochondrial localization of P5, a member of the protein disulphide isomerase family. J Biochem 144: 187-196.
116. Kitamura A, Kubota H, Pack CG, Matsumoto G, Hirayama S, Takahashi Y, Kimura H, Kinjo M, Morimoto RI, Nagata K. 2006. Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state. Nat Cell Biol 8: 1163-1170.
117. Kjeldsen T, Ludvigsen S, Diers I, Balschmidt P, Sorensen AR, Kaarsholm NC. 2002. Engineering-enhanced protein secretory expression in yeast with application to insulin. J Biol Chem 277: 18245-18248.
118. Knop M, Finger A, Braun T, Hellmuth K, Wolf DH. 1996. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J 15: 753-763.
119. Kopito RR. 1999. Biosynthesis and degradation of CFTR. Physiol Rev 79 (Suppl): S167-S173.
120. Korotkov KV, Kumaraswamy E, Zhou Y, Hatfield DL, Gladyshev VN. 2001. Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells. J Biol Chem 276: 15330-15536.
121. Kouroku Y, Fujita E, Tanida I, Ueno T, Isoai A, Kumagai H, Ogawa S, Kaufman RJ, Kominami E, Momoi T. 2007. ER stress (PERK/eIF2α phosphorylation) mediates the polyglutamine-induced LC3 conversion, an essential step for autophagy formation. Cell Death Differ 14: 230-239.
122. Kowalski JM, Parekh RN, Mao J, Wittrup KD. 1998. Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control. J Biol Chem 273: 19453-19458.
123. Kroeger H, Miranda E, MacLeod I, Perez J, Crowther DC, Marciniak SJ, Lomas DA. 2009. Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins. J Biol Chem 284: 22793-22802.
124. Lam YA, Lawson TG, Velayutham M, Zweier JL, Pickart CM. 2002. A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 416: 763-767.
125. Lawrence JM, Samways MJ, Henwood J, Kelly J. 2011. Effect of an invasive ant and its chemical control on a threatened endemic Seychelles millipede. Ecotoxicology doi: 101007/s10646-011-0614-4.
126. Le Fourn V, Gaplovska-Kysela K, Guhl B, Santimaria R, Zuber C, Roth J. 2009. Basal autophagy is involved in the degradation of the ERAD component EDEM1. Cell Mol Life Sci 66: 1434-1445.
127. Lebiedzinska M, Szabadkai G, Jones AW, Duszynski J, Wieckowski MR. 2009. Interactions between the endoplasmic reticulum, mitochondria, plasma membrane and other subcellular organelles. Int J Biochem Cell Biol 41: 1805-1816.
128. Lederkremer GZ. 2009. Glycoprotein folding, quality control and ER-associated degradation. Curr Opin Struct Biol 19: 515-523.
129. Lee SO, Cho K, Cho S, Kim I, Oh C, Ahn K. 2010. Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation. EMBO J 29: 363-375.
130. Letunic I, Doerks T, Bork P. 2009. SMART 6: Recent updates and new developments. Nucleic Acids Res 37: D229-D232.
131. 2+-dependent redox modulation of SERCA 2b by ERp57. J Cell Biol 164: 35-46.
132. Li G, Mongillo M, Chin KT, Harding H, Ron D, Marks AR, Tabas I. 2009. Role of ERO1-α-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol 186: 783-792.
133. Liang J, Yin C, Doong H, Fang S, Peterhoff C, Nixon RA, Monteiro MJ. 2006. Characterization of erasin (UBXD2): A new ER protein that promotes ER-associated protein degradation. J Cell Sci 119: 4011-4024.
134. Lilley BN, Ploegh HL. 2004. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429: 834-840.
135. Lim PJ, Danner R, Liang J, Doong H, Harman C, Srinivasan D, Rothenberg C, Wang H, Ye Y, Fang S, et al. 2009. Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD. J Cell Biol 187: 201-217.
136. 2+ influx. Curr Biol 15: 1235-1241.
137. Loureiro J, Lilley BN, Spooner E, Noriega V, Tortorella D, Ploegh HL. 2006. Signal peptide peptidase is required for dislocation from the endoplasmic reticulum. Nature 441: 894-897.
138. Manjithaya R, Nazarko TY, Farre JC, Subramani S. 2010. Molecular mechanism and physiological role of pexophagy. FEBS Lett 584: 1367-1373.
139. Margittai E, Banhegyi G. 2010. Oxidative folding in the endoplasmic reticulum: Towards a multiple oxidant hypothesis? FEBS Lett 584: 2995-2998.
140. Mariappan M, Li X, Stefanovic S, Sharma A, Mateja A, Keenan RJ, Hegde RS. 2010. A ribosome-associating factor chaperones tail-anchored membrane proteins. Nature 466: 1120-1124.
141. Mast SW, Diekman K, Karaveg K, Davis A, Sifers RN, Moremen KW. 2005. Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins. Glycobiology 15: 421-436.
142. Mateja A, Szlachcic A, Downing ME, Dobosz M, Mariappan M, Hegde RS, Keenan RJ. 2009. The structural basis of tail-anchored membrane protein recognition by Get3. Nature 461: 361-366.
143. McLaughlin M, Vandenbroeck K. 2010. The endoplasmic reticulum protein folding factory and its chaperones: New targets for drug discovery? Br J Pharmacol 162: 328-345.
144. Meunier L, Usherwood YK, Tae Chung K, Hendershot LM. 2002. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13: 4456-4469.
145. Michalak M, Groenendyk J, Szabo E, Gold LI, Opas M. 2009. Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem J 417: 651-666.
146. Molinari M. 2007. N-glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol 3: 313-320.
147. Molinari M, Calanca V, Galli C, Lucca P, Paganetti P. 2003. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299: 1397-1400.
148. Morello R, Rauch F. 2010. Role of cartilage-associated protein in skeletal development. Curr Osteoporos Rep 8: 77-83.
149. Morello R, Bertin TK, Chen Y, Hicks J, Tonachini L, Monticone M, Castagnola P, Rauch F, Glorieux FH, Vranka J, et al. 2006. CRTAP is required for prolyl 3-hydroxylation and mutations cause recessive osteogenesis imperfecta. Cell 127: 291-304.
150. Morito D, Hirao K, Oda Y, Hosokawa N, Tokunaga F, Cyr DM, Tanaka K, Iwai K, Nagata K. 2008. Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRD508. Mol Biol Cell 19: 1328-1336.
151. Mu TW, Ong DS, Wang YJ, Balch WE, Yates JR III, Segatori L, Kelly JW. 2008. Chemical and biological approaches synergize to ameliorate protein-folding diseases. Cell 134: 769-781.
152. Mueller B, Klemm EJ, Spooner E, Claessen JH, Ploegh HL. 2008. SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins. Proc Natl Acad Sci 105: 12325-12330.
153. Myhill N, Lynes EM, Nanji JA, Blagoveshchenskaya AD, Fei H, Carmine Simmen K, Cooper TJ, Thomas G, Simmen T. 2008. The subcellular distribution of calnexin is mediated by PACS-2. Mol Biol Cell 19: 2777-2788.
154. Nagai N, Hosokawa M, Itohara S, Adachi E, Matsushita T, Hosokawa N, Nagata K. 2000. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. J Cell Biol 150: 1499-1506.
155. Nagasawa K, Higashi T, Hosokawa N, Kaufman RJ, Nagata K. 2007. Simultaneous induction of the four subunits of the TRAP complex by ER stress accelerates ER degradation. EMBO Rep 8: 483-489.
156. Nagata K. 2003. HSP47 as a collagen-specific molecular chaperone: Function and expression in normal mouse development. Semin Cell Dev Biol 14: 275-282.
157. Naidoo N. 2009. ER and aging-Protein folding and the ER stress response. Ageing Res Rev 8: 150-159.
158. Neutzner A, Neutzner M, Benischke AS, Ryu SW, Frank S, Youle RJ, Karbowski M. 2011. A systematic search for ER membrane-associated RING finger proteins identifies Nixin/ZNRF4 as a regulator of calnexin stability and ER homeostasis. J Biol Chem 286: 8633-8643.
159. Ng W, Sergeyenko T, Zeng N, Brown JD, Romisch K. 2007. Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum. J Cell Sci 120: 682-691.
160. Oda Y, Hosokawa N, Wada I, Nagata K. 2003. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299: 1394-1397.
161. Ogata M, Hino S, Saito A, Morikawa K, Kondo S, Kanemoto S, Murakami T, Taniguchi M, Tanii I, Yoshinaga K, et al. 2006. Autophagy is activated for cell survival after endoplasmic reticulum stress. Mol Cell Biol 26: 9220-9231.
162. Okuda-Shimizu Y, Hendershot LM. 2007. Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp. Mol Cell 28: 544-554.
163. Olivari S, Galli C, Alanen H, Ruddock L, Molinari M. 2005. A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation. J Biol Chem 280: 2424-2428.
164. Olivari S, Cali T, Salo KEH, Paganetti P, Ruddock LW, Molinari M. 2006. EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of foldingdefective polypeptides and by inhibiting their covalent aggregation. Biochem Biophys Res Commun 349: 1278-1284.
165. Oliver JD, Roderick HL, Llewellyn DH, High S. 1999. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol Biol Cell 10: 2573-2582.
166. Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, Tartaglia GG, Vendruscolo M, Hayer-Hartl M, Hartl FU, Vabulas RM. 2011. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144: 67-78.
167. 2+ increases enhance mutant glucocerebrosidase proteostasis. Nat Chem Biol 6: 424-432.
168. Orlando RA. 2004. The low-density lipoprotein receptorrelated protein associates with calnexin, calreticulin, and protein disulfide isomerase in receptor-associatedprotein-deficient fibroblasts. Exp Cell Res 294: 244-253.
169. Otero JH, Lizak B, Hendershot LM. 2010. Life and death of a BiP substrate. Semin Cell Dev Biol 21: 472-478.
170. Ozcan U, Yilmaz E, Ozcan L, Furuhashi M, Vaillancourt E, Smith RO, Gorgun CZ, Hotamisligil GS. 2006. Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 313: 1137-1140.
171. Paetzel M, Karla A, Strynadka NC, Dalbey RE. 2002. Signal peptidases. Chem Rev 102: 4549-4580.
172. Pani B, Singh BB. 2009. Lipid rafts/caveolae as microdomains of calcium signaling. Cell Calcium 45: 625-633.
173. Park B, Lee S, Kim E, Cho K, Riddell SR, Cho S, Ahn K. 2006. Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 127: 369-382.
174. Park CY, Shcheglovitov A, Dolmetsch R. 2010. The CRAC channel activator STIM1 binds and inhibits L-type voltage-gated calcium channels. Science 330: 101-105.
175. Petrova K, Oyadomari S, Hendershot LM, Ron D. 2008. Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3. EMBO J 27: 2862-2872.
176. Pilon M, Schekman R, Romisch K. 1997. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J 16: 4540-4548.
177. Pollard MG, Travers KJ, Weissman JS. 1998. Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1: 171-182.
178. Powers ET, Morimoto RI, Dillin A, Kelly JW, Balch WE. 2009. Biological and chemical approaches to diseases of proteostasis deficiency. Annu Rev Biochem 78: 959-991.
179. Raasi S, Wolf DH. 2007. Ubiquitin receptors and ERAD: A network of pathways to the proteasome. Semin Cell Dev Biol 18: 780-791.
180. Rabinovich E, Kerem A, Froehlich KU, Diamant N, Bar-Nun S. 2002. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 22: 626-634.
181. Rabu C, Schmid V, Schwappach B, High S. 2009. Biogenesis of tail-anchored proteins: The beginning for the end? J Cell Sci 122: 3605-3612.
182. Reggiori F, Monastyrska I, Verheije MH, Cali T, Ulasli M, Bianchi S, Bernasconi R, de Haan CA, Molinari M. 2010. Coronaviruses hijack the LC3-I-positive EDEMosomes, ER-derived vesicles exporting short-lived ERAD regulators, for replication. Cell Host Microbe 7: 500-508.
183. Riemer J, Appenzeller-Herzog C, Johansson L, Bodenmiller B, Hartmann-Petersen R, Ellgaard L. 2009. A luminal flavoprotein in endoplasmic reticulum-associated degradation. Proc Natl Acad Sci 106: 14831-14836.
184. 2+: Molecular determinants and functional consequences. Physiol Rev 86: 369-408.
185. 2+ transfer from the ER to mitochondria: When, how and why. Biochim Biophys Acta
186. Ruiz-Canada C, Kelleher DJ, Gilmore R. 2009. Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell 136: 272-283.
187. Rumpf S, Jentsch S. 2006. Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone. Mol Cell 21: 261-269.
188. Rutkevich LA, Williams DB. 2010. Participation of lectin chaperones and thiol oxidoreductases in protein folding within the endoplasmic reticulum. Curr Opin Cell Biol 23: 157-166.
189. Rutkevich LA, Cohen-Doyle MF, Brockmeier U, Williams DB. 2010. Functional relationship between protein disulfide isomerase family members during the oxidative folding of human secretory proteins. Mol Biol Cell 21: 3093-3105.
190. Rutkowski DT, Kang SW, Goodman AG, Garrison JL, Taunton J, Katze MG, Kaufman RJ, Hegde RS. 2007. The role of p58IPK in protecting the stressed endoplasmic reticulum. Mol Biol Cell 18: 3681-3691.
191. Sanders CR, Myers JK. 2004. Disease-related misassembly of membrane proteins. Annu Rev Biophys Biomol Struct 33: 25-51.
192. Saraogi I, Shan SO. 2011. Molecular mechanism of co-translational protein targeting by the signal recognition particle. Traffic 12: 535-542.
193. Sato Y, Murase K, Kato J, Kobune M, Sato T, Kawano Y, Takimoto R, Takada K, Miyanishi K, Matsunaga T, et al. 2008. Resolution of liver cirrhosis using vitamin A-coupled liposomes to deliver si RNA against a collagen-specific chaperone. Nat Biotechnol 26: 431-442.
194. Satoh T, Chen Y, Hu D, Hanashima S, Yamamoto K, Yamaguchi Y. 2010. Structural basis for oligosaccharide recognition of misfolded glycoproteins by OS-9 in ER-associated degradation. Mol Cell 40: 905-916.
195. Schafer A, Wolf DH. 2009. Sec61p is part of the endoplasmic reticulum-associated degradation machinery. EMBO J 28: 2874-2884.
196. Schuberth C, Buchberger A. 2008. UBX domain proteins: Major regulators of the AAA ATPase Cdc48/p97. Cell Mol Life Sci 65: 2360-2371.
197. Sekijima Y, Wiseman RL, Matteson J, Hammarstrom P, Miller SR, Sawkar AR, Balch WE, Kelly JW. 2005. The biological and chemical basis for tissue-selective amyloid disease. Cell 121: 73-85.
198. Shen Y, Hendershot LM. 2005. ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates. Mol Biol Cell 16: 40-50.
199. Shibatani T, David LL, McCormack AL, Frueh K, Skach WR. 2005. Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry 44: 5982-5992.
200. Shimizu Y, Okuda-Shimizu Y, Hendershot LM. 2010. Ubiquitylation of an ERAD substrate occurs on multiple types of amino acids. Mol Cell 40: 917-926.
201. Simmen T, Lynes EM, Gesson K, Thomas G. 2010. Oxidative protein folding in the endoplasmic reticulum: Tight links to the mitochondria-associated membrane (MAM). Biochim Biophys Acta 1798: 1465-1473.
202. Solda T, Galli C, Kaufman RJ, Molinari M. 2007. Substratespecific requirements for UGT1-dependent release from calnexin. Mol Cell 27: 238-249.
203. Stevens FJ, Argon Y. 1999. Protein folding in the ER. Semin Cell Dev Biol 10: 443-454.
204. Swanson R, Locher M, Hochstrasser M. 2001. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matα2 repressor degradation. Genes Dev 15: 2660-2674.
205. Tam S, Geller R, Spiess C, Frydman J. 2006. The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8: 1155-1162.
206. Tanabe K, Lennarz WJ, Suzuki T. 2006. A cytoplasmic peptide: N-glycanase. Meth Enzymol 415: 46-55.
207. Tavender TJ, Bulleid NJ. 2010a. Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum. Antioxid Redox Sign 13: 1177-1187.
208. 2 produced during disulphide formation. J Cell Sci 123: 2672-2679.
209. Tavender TJ, Springate JJ, Bulleid NJ. 2010. Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. EMBO J 29: 4185-4197.
210. Taxis C, Hitt R, Park SH, Deak PM, Kostova Z, Wolf DH. 2003. Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J Biol Chem 278: 35903-35913.
211. Tien AC, Rajan A, Schulze KL, Ryoo HD, Acar M, Steller H, Bellen HJ. 2008. Ero1L, a thiol oxidase, is required for Notch signaling through cysteine bridge formation of the Lin12-Notch repeats in Drosophila melanogaster. J Cell Biol 182: 1113-1125.
212. Timmins JM, Ozcan L, Seimon TA, Li G, Malagelada C, Backs J, Backs T, Bassel-Duby R, Olson EN, Anderson ME, et al. 2009. Calcium/calmodulin-dependent protein kinase II links ER stress with Fas and mitochondrial apoptosis pathways. J Clin Invest 119: 2925-2941.
213. Todde V, Veenhuis M, van der Klei IJ. 2009. Autophagy: Principles and significance in health and disease. Biochim Biophys Acta 1792: 3-13.
214. Tsai YC, Weissman AM. 2010. The unfolded protein response, degradation from endoplasmic reticulum and cancer. Genes Cancer 1: 764-778.
215. Ushioda R, Nagata K. 2011. The endoplasmic reticulumassociated degradation and disulfide reductase ERdj5. Meth Enzymol 490: 235-258.
216. Ushioda R, Hoseki J, Araki K, Jansen G, Thomas DY, Nagata K. 2008. ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321: 569-572.
217. Vashist S, Ng DT. 2004. Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J Cell Biol 165: 41-52.
218. Voeltz GK, Rolls MM, Rapoport TA. 2002. Structural organization of the endoplasmic reticulum. EMBO Rep 3: 944-950.
219. Wahlman J. 2007. Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system. Cell 129: 943-955.
220. Wang B, Heath-Engel H, Zhang D, Nguyen N, Thomas DY, Hanrahan JW, Shore GC. 2008. BAP31 interacts with Sec61 translocons and promotes retrotranslocation of CFTRdF508 via the derlin-1 complex. Cell 133: 1080-1092.
221. Wang X, Herr RA, Rabelink M, Hoeben RC, Wiertz EJ, Hansen TH. 2009. Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates. J Cell Biol 187:655-668.
222. Wang F, Brown EC, Mak G, Zhuang J, Denic V. 2010a. A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol Cell 40: 159-171.
223. Wang Y, Deng X, Mancarella S, Hendron E, Eguchi S, Soboloff J, Tang XD, Gill DL. 2010b. The calcium store sensor, STIM1, reciprocally controls Orai and CaV1.2 channels. Science 330: 105-109.
224. Wang L, Zhu L, Wang CC. 2011. The endoplasmic reticulum sulfhydryl oxidase Ero1β drives efficient oxidative protein folding with loose regulation. Biochem J 434: 113-121.
225. Wiertz EJ. 1996. The human cytomegalovirus us11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84: 769-779.
226. Wiertz EJ, Tortorella D, Bogyo M, Yu J, Mothes W, Jones TR, Rapoport TA, Ploegh HL. 1996. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384: 432-438.
227. Willer M, Forte GMA, Stirling CJ. 2008. 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 283: 33883-33888.
228. Williams DB. 2006. Beyond lectins: The calnexin/calreticulin chaperone system of the endoplasmic reticulum. J Cell Sci 119: 615-623.
229. Wiseman RL, Powers ET, Buxbaum JN, Kelly JW, Balch WE. 2007. An adaptable standard for protein export from the endoplasmic reticulum. Cell 131: 809-821.
230. Wong E, Cuervo AM. 2010. Integration of clearance mechanisms: The proteasome and autophagy. Cold Spring Harb Perspect Biol 2: a006734.
231. Yamamoto YH, Kimura T, Momohara S, Takeuchi M, Tani T, Kimata Y, Kadokura H, Kohno K. 2010. A novel ER Jprotein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR. Cell Struct Funct 35: 107-116.
232. Yan W, Frank CL, Korth MJ, Sopher BL, Novoa I, Ron D, Katze MG. 2002. Control of PERK eIF2α kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc Natl Acad Sci 99: 15920-15925.
233. Ye Y, Shibata Y, Yun C, Ron D, Rapoport TA. 2004. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429: 841-847.
234. Yla-Anttila P, Vihinen H, Jokitalo E, Eskelinen EL. 2009. 3D tomography reveals connections between the phagophore and endoplasmic reticulum. Autophagy 5: 1180-1185.
235. Yorimitsu T, Klionsky DJ. 2007a. Eating the endoplasmic reticulum: Quality control by autophagy. Trends Cell Biol 17: 279-285.
236. Yorimitsu T, Klionsky DJ. 2007b. Endoplasmic reticulum stress: A new pathway to induce autophagy. Autophagy 3: 160-162.
237. Yoshida Y, Tanaka K. 2010. Lectin-like ERAD players in ER and cytosol. Biochim Biophys Acta 1800: 172-180.
238. Younger JM, Chen L, Ren HY, Rosser MF, Turnbull EL, Fan CY, Patterson C, Cyr DM. 2006. Sequential qualitycontrol checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 126: 571-582.
239. 2+ release mechanism. J Biol Chem 272: 7069-7077.
240. Zahedi RP, Volzing C, Schmitt A, Frien M, Jung M, Dudek J, Wortelkamp S, Sickmann A, Zimmermann R. 2009. Analysis of the membrane proteome of canine pancreatic rough microsomes identifies a novel Hsp40, termed ERj7. Proteomics 9: 3463-3473.
241. Zavacki AM, Arrojo EDR, Freitas BC, Chung M, Harney JW, Egri P, Wittmann G, Fekete C, Gereben B, Bianco AC. 2009. The E3 ubiquitin ligase TEB4 mediates degradation of type 2 iodothyronine deiodinase. Mol Cell Biol 29: 5339-5347.
242. Zimmermann R, Eyrisch S, Ahmad M, Helms V. 2010. Protein translocation across the ER membrane. Biochim Biophys Acta 1808: 912-924.
243. Zito E, Chin KT, Blais J, Harding HP, Ron D. 2010a. ERO1-β, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis. J Cell Biol 188: 821-832.
244. Zito E, Melo EP, Yang Y, Wahlander A, Neubert TA, Ron D. 2010b. Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin. Mol Cell 40: 787-797.
245. Zuber C, Cormier JH, Guhl B, Santimaria R, Hebert DN, Roth J. 2007. EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites. Proc Natl Acad Sci 104: 4407-4412.