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Protein Quality Control in the Endoplasmic Reticulum

Adams, Benjamin M., Oster, Michela E., Hebert, Daniel N.·2019·The Protein Journal
DOI 10.1007/s10930-019-09831-wPMC PMC6589386
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Research works printed but not linked: 152

  1. Blobel G, Sabatini DD (1971) Ribosome-membrane interaction in eukaryotic cells. Biomem 2:193–195
  2. Blobel G, Dobberstein B (1975) Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol 67:835–851 · DOI
  3. Blobel G, Dobberstein B (1975) Transfer of protein across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J Cell Biol 67:852–862 · DOI
  4. Bulleid NJ, Freedman RB (1988) Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. Nature 335:649–651 · DOI
  5. Nicchitta CV, Blobel G (1993) Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation. Cell 73:989–998 · DOI
  6. Hebert DN, Foellmer B, Helenius A (1995) Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81:425–433 · DOI · Paper page
  7. Laskey RA, Honda B, Mills AD, Finch JT (1978) Speculations on the functions of the major heat shock and glucose-regulated proteins. Nature 275:416–420 · DOI
  8. Pelham HR (1986) Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46:959–961 · DOI
  9. Cheng MY, Hartl UF, Martin J et al (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337:620–625 · DOI
  10. Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH (1989) Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature 342:884–889 · DOI
  11. Ellis JR (1996) Discovery of molecular chaperones. Cell Stress Chaperones 1:155–160 · DOI
  12. Helenius A (1989) Protein oligomerization in the endoplasmic reticulum. Annu Rev Cell Biol 5:277–307 · DOI
  13. Horwich A, Neupert W, Hartl UF (1990) Protein-catalysed protein folding. Trends Biotechnol 8:126–131 · DOI
  14. Hendershot LM (2004) The ER function BiP is a master regulator of ER function. Mt Sinai J Med 71:289–297
  15. Behnke J, Feige MJ, Hendershot LM (2015) BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions. J Mol Biol 427:1589–1608 · DOI
  16. Blond-Elguindi S, Cwirla SE, Dower WJ et al (1993) Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75:717–728 · DOI
  17. Behnke J, Mann MJ, Scruggs F-L et al (2016) Members of the Hsp70 family recognize distinct types of sequences to execute ER quality control. Mol Cell 63:739–752 · DOI
  18. Flynn GC, Pohl J, Flocco MT, Rothman JE (1991) Peptide-binding specificity of the molecular chaperone BiP. Nature 353:726–730 · DOI
  19. Schlecht R, Erbse AH, Bukau B, Mayer MP (2011) Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat Struct Mol Biol 18:345–351 · DOI
  20. Kampinga HH, Andreasson C, Barducci A et al (2018) Function, evolution, and structure of J-domain proteins. Cell Stress Chaperones 24(1):7–15 · DOI
  21. Otero JH, Lizák B, Hendershot LM (2010) Life and death of a BiP substrate. Semin Cell Dev Biol 21:472–478 · DOI
  22. Boisramé A, Kabani M, Beckerich J-M et al (1998) Interaction of Kar2p and Sls1p is required for efficient co-translational translocation of secreted proteins in the yeast Yarrowia lipolytica. J Biol Chem 273:30903–30908 · DOI
  23. Kabani M, Beckerich J-M, Brodsky JL (2002) Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol Cell Biol 22:4677–4689 · DOI
  24. Tyson JR, Stirling CJ (2000) LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. EMBO J 19:6440–6452 · DOI
  25. 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 · DOI
  26. Steel GJ, Fullerton DM, Tyson JR, Stirling CJ (2004) Coordinated activation of Hsp70 chaperones. Science 303:98–101 · DOI
  27. Chen X, Easton D, Oh H-J et al (1996) The 170 kDa glucose regulated stress protein is a large HSP70- HSP110-like protein of the endoplasmic reticulum. FEBS Lett 380:68–72 · DOI
  28. Matlack KE, Misselwitz B, Plath K, Rapoport TA (1999) BiP acts as a molecular ratchet during posttranslational transport of prepro-α factor across the ER membrane author links open overlay panel. Cell 97:553–564 · DOI
  29. Helenius A, Hammond C (1994) Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266:456–458 · DOI
  30. Hebert DN, Zhang J-X, Helenius A (1998) Protein folding and maturation in a cell-free system. Biochem Cell Biol 76:867–873 · DOI
  31. Plemper RK, Böhmler S, Bordallo J et al (1997) Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388:891–895 · DOI
  32. Skowronek MH, Hendershot LM, Haas IG (1998) The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP. Proc Natl Acad Sci USA 95:1574–1578 · DOI
  33. Brodsky JL, Werner ED, Dubas ME et al (1999) The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J Biol Chem 274:3453–3460 · DOI
  34. Farinha CM, Amaral MD (2005) Most F508del-CFTR is targeted to degradation at an early folding checkpoint and independently of calnexin. Mol Cell Biol 25:5242–5252 · DOI
  35. Sörgjerd K, Ghafouri B, Jonsson B-H et al (2006) Retention of misfolded mutant transthyretin by the chaperone BiP/GRP78 mitigates amyloidogenesis. J Mol Biol 356:469–482 · DOI
  36. Dong M, Bridges JP, Apsley K et al (2008) ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C. Mol Biol Cell 19:2620–2630 · DOI
  37. Amin-Wetzel N, Saunders RA, Kamphius MJ et al (2017) A J-protein co-chaperone recruits BiP to monomerize IRE1 and repress the unfolded protein response. Cell 171:1625–1637 · DOI
  38. Cunnea PM, Miranda-Vizuete A, Bertoli G et al (2003) ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. J Biol Chem 278:1059–1066 · DOI
  39. Ushioda R, Hoseki J, Araki K et al (2008) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321:569–572 · DOI
  40. Khodayari N, Marek G, Lu Y et al (2017) Erdj3 Has an essential role for Z variant alpha-1-antitrypsin degradation. J Cell Biochem 118:3090–3101 · DOI
  41. Tan YL, Genereux JC, Pankow S et al (2014) ERdj3 is an endoplasmic reticulum degradation factor for mutant glucocerebrosidase variants linked to Gaucher’s disease. Chem Biol 21:967–976 · DOI
  42. Rutkowski TD, Kang S-W, Goodman AG et al (2007) The role of p58IPK in protecting the stressed endoplasmic reticulum. Mol Biol Cell 18:3681–3691 · DOI
  43. Ham H, Woolery AR, Tracy C et al (2014) Unfolded protein response-regulated Drosophila Fic protein reversibly AMPylates BiP chaperone during endoplasmic reticulum homeostasis. J Biol Chem 289:36059–36069 · DOI
  44. Anwesha S, Chen AJ, Nakayasu ES et al (2015) A novel link between Fic mediated adenylation and the unfolded protein response. J Biol Chem 290:8482–8499 · DOI
  45. Preissler S, Rato C, Chen R et al (2015) AMPylation matches BiP activity to client protein load in the endoplasmic reticulum. eLife 4:e12621 · DOI
  46. Preissler S, Rohland L, Yan Y et al (2017) AMPylation targets the rate-limiting step of BiP’s ATPase cycle for its functional inactivation. eLife 6:e29428 · DOI
  47. Preissler S, Rato C, Perera L et al (2017) FICD acts bi-functionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP. Nat Struct Mol Biol 24:23–29 · DOI
  48. Christianson JC, Shaler TA, Tyler RE, Kopito RR (2009) OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol 10:272–282 · DOI · Paper page
  49. Zhong Y, Shen H, Wang Y et al (2015) Identification of ERAD components essential for dislocation of the null Hong Kong variant of α-1-antitrypsin (NHK). Biochem Biophys Res Commun 458:424–428 · DOI
  50. Di X-J, Wang Y-J, Han D-Y et al (2016) Grp94 protein delivers γ-aminobutyric acid type A (GABAA) receptors to Hrd1 protein-mediated endoplasmic reticulum-associated degradation. J Biol Chem 291:9526–9539 · DOI
  51. Dersh D, Jones SM, Eletto D et al (2014) OS-9 facilitates turnover of nonnative GRP94 marked by hyperglycosylation. Mol Biol Cell 25:2220–2234 · DOI
  52. Apweiler R, Hermjakob H, Sharon N (1999) On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim Biophys Acta 1473:4–8 · DOI
  53. Haraguchi M, Yamashiro S, Furukawa K et al (1995) The effects of the site-directed removal of N-glycosylation sites from β-1,4-N-acetylgalactosaminyltransferase on its function. Biochem J 312:273–280 · DOI
  54. Cai G, Salonikidis PS, Fei J et al (2005) The role of N-glycosylation in the stability, trafficking and GABA-uptake of GABA-transporter 1. FEBS J 272:1625–1638 · DOI
  55. Skropeta D (2009) The effect of individual N-glycans on enzyme activity. Bioorg Med Chem 17:2545–2653 · DOI
  56. Culyba EK, Price JL, Hanson SR et al (2011) Protein native-state stabilization by placing aromatic side chains in N-glycosylated reverse turns. Science 331:571–575 · DOI · Paper page
  57. Hebert DN, Lamriben L, Powers ET, Kelly JW (2014) The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis. Nat Chem Biol 10:902–910 · DOI
  58. 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 · DOI
  59. Lamriben L, Graham JB, Adams BM, Hebert DN (2016) N-glycan based ER molecular chaperone and protein quality control system: the calnexin binding cycle. Traffic 17:308–326 · DOI
  60. Shrimal S, Cherepanova NA, Gilmore R (2015) Cotranslational and posttranslocational N-glycosylation of proteins in the endoplasmic reticulum. Semin Cell Dev Biol 41:71–78 · DOI
  61. Schallus T, Jaeckh C, Fehér K et al (2008) Malectin: a novel carbohydrate-binding protein of the endoplasmic reticulum and a candidate player in the early steps of protein N-glycosylation. Mol Biol Cell 19:3404–3414 · DOI
  62. Qin S-Y, Hu D, Matsumoto K et al (2012) Malectin forms a complex with ribophorin i for enhanced association with misfolded glycoproteins. J Biol Chem 287:38080–38089 · DOI
  63. Takeda K, Qin S-Y, Matsumoto N, Yamamoto K (2014) Association of malectin with ribophorin I is crucial for attenuation of misfolded glycoprotein secretion. Biochem Biophys Res Commun 454:436–440 · DOI
  64. Galli C, Bernasconi R, Soldà T et al (2011) Malectin participates in a backup glycoprotein quality control pathway in the mammalian ER. PLoS ONE 6:e16304 · DOI
  65. Schrag JD, Bergeron JJ, Li Y et al (2001) The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol Cell 8:633–644 · DOI
  66. Gopalakrishnapai J, Gupta G, Karthikeyan T et al (2006) Isothermal titration calorimetric study defines the substrate binding residues of calreticulin. Biochem Biophys Res Commun 351:14–20 · DOI
  67. Sousa M, Parodi AJ (1995) The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J 14:4196–4203 · DOI
  68. Hebert DN, Zhang J-X, Chen W et al (1997) The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J Cell Biochem 139:613–623
  69. Vassilakos A, Michalak M, Lehrman MA, Williams DB (1998) Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 37:3480–3490 · DOI
  70. Li Z, Stafford WF, Bouvier M (2001) The metal ion binding properties of calreticulin modulate its conformational flexibility and thermal stability. Biochemistry 40:11193–11201 · DOI
  71. Kozlov G, Pocanschi CL, Rosenauer A et al (2010) Structural basis of carbohydrate recognition by calreticulin. J Biol Chem 285:38612–38620 · DOI
  72. Ellgaard L, Bettendorff P, Braun D et al (2002) NMR structures of 36 and 73-residue fragments of the calreticulin P-domain. JMB 322:773–784 · DOI
  73. Oliver JD, van der Wal FJ, Bulleid NJ, High S (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275:86–88 · DOI
  74. Kozlov G, Bastos-Aristizabal S, Määttänen P et al (2010) Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain. J Biol Chem 285:35551–35557 · DOI
  75. Kozlov G, Muñoz-Escobar J, Castro K, Gehring K (2017) Mapping the ER interactome: the P domains of calnexin and calreticulin as plurivalent adapters for foldases and chaperones. Structure 25:1415–1422 · DOI
  76. Roversi P, Marti L, Caputo AT et al (2017) Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint. Proc Natl Acad Sci USA 114:8544–8549 · DOI
  77. Satoh T, Song C, Zhu T et al (2017) Visualization of a flexible modular structure of the ER folding-sensor enzyme UGGT. Sci Rep 7:12142 · DOI
  78. Takeda Y, Seko A, Hachisu M et al (2014) Both isoforms of human UDP-glucose:glycoprotein glucosyltransferase are enzymatically active. Glycobiology 24:344–350 · DOI
  79. Ferguson AD, Labunskyy VM, Fomenko DE et al (2006) NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. J Biol Chem 281:3536–3543 · DOI
  80. Korotkov KV, Kuramaswamy E, Zhou Y et al (2001) Association between the 15-kDa selenoprotein and UDP-glucose: glycoprotein glucosyltransferase in the endoplasmic reticulum of mammalian cells. J Biol Chem 276:15330–15336 · DOI
  81. Yim SH, Everley RA, Schildberg FA et al (2018) Role of selenof as a gatekeeper of secreted disulfide-rich glycoproteins. Cell Rep 23:1387–1398 · DOI
  82. Rajagopalan S, Brenner MB (1994) Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum. J Exp Med 180:407–412 · DOI
  83. Cannon KS, Hebert DN, Helenius A (1996) Glycan dependent and independent association of vesicular stomatitis virus g protein with calnexin. J Biol Chem 271:14280–14284 · DOI
  84. Vassilakos A, Myrna C-DF, Peterson PA et al (1996) The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J 15:1495–1506 · DOI
  85. Hebert DN, Foellmer B, Helenius A (1996) Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO J 15:2961–2968 · DOI
  86. Mesaeli N, Nakamura K, Zvaritch E et al (1999) Calreticulin is essential for cardiac development. J Cell Biol 144:857–868 · DOI
  87. Molinari M, Galli C, Vanoni O et al (2005) Persistent glycoprotein misfolding activates the glucosidase II/UGT1-driven calnexin cycle to delay aggregation and loss of folding competence. Mol Cell 20:503–512 · DOI · Paper page
  88. Coe H, Jung J, Groenendyk J et al (2010) ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulum. J Biol Chem 285:6725–6738 · DOI
  89. Denzel A, Molinari M, Trigueros C et al (2002) Early postnatal death and motor disorders in mice congenitally deficient in calnexin expression. Mol Cell Biol 22:7398–7404 · DOI
  90. Wang N, Glidden EJ, Murphy SR et al (2008) The cotranslational maturation program for the type II membrane glycoprotein influenza neuraminidase. J Biol Chem 283:33826–33837 · DOI
  91. Chandrasekhar K, Ke H, Wang N et al (2016) Cellular folding pathway of a metastable serpin. Proc Natl Acad Sci USA 113:6484–6489 · DOI
  92. Wang H, Li S, Wang J et al (2018) N-glycosylation in the protease domain of trypsin-like serine proteases mediates calnexin-assisted protein folding. eLife 7:e35672 · DOI
  93. Daniels R, Kurowski B, Johnson AE, Hebert DN (2003) N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol Cell 11:79–90 · DOI
  94. Gao B, Adhikari R, Howarth M et al (2002) Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 16:99–109 · DOI
  95. Pearse BR, Gabriel L, Wang N, Hebert DN (2008) A cell-based reglucosylation assay demonstrates the role of GT1 in the quality control of a maturing glycoprotein. J Cell Biol 181:309–320 · DOI
  96. Pearse BR, Tamura T, Sunryd JC et al (2010) The role of UDP-Glc:glycoprotein glucosyltransferase 1 in the maturation of an obligate substrate prosaposin. J Cell Biol 189:829–841 · DOI
  97. Tannous A, Patel N, Tamura T, Hebert DN (2015) Reglucosylation by UDP-glucose:glycoprotein glucosyltransferase 1 delays glycoprotein secretion but not degradation. Mol Biol Cell 26:390–405 · DOI
  98. Soldà T, Galli C, Kaufman RJ, Molinari M (2007) Substrate-specific requirements for UGT1-dependent release from calnexin. Mol Cell 27:238–249 · DOI
  99. Olivari S, Molinari M (2007) Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins. FEBS Lett 581:3658–3664 · DOI
  100. Sunryd JC, Tannous A, Lamriben L, Hebert DN (2014) Chaperones of the Endoplasmic Reticulum Associated Degradation (ERAD) Pathway. In: Houry WA (ed) The molecular chaperones interaction networks in protein folding and degradation. Springer Science, New York
  101. Karaivanova VK, Luan P, Spiro RG (1998) Processing of viral envelope glycoprotein by the endomannosidase pathway: evaluation of host cell specificity. Glycobiology 8:725–730 · DOI
  102. Molinari M, Calanca V, Galli C et al (2003) Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299:1397–1400 · DOI
  103. Oda Y, Hosokawa N, Wada I, Nagata K (2003) EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299:1394–1397 · DOI
  104. Su K, Stoller T, Rocco J et al (1993) Pre-Golgi degradation of yeast prepro-alpha-factor expressed in a mammalian cell. Influence of cell type-specific oligosaccharide processing on intracellular fate. J Biol Chem 268:14301–14309 · DOI
  105. Aikawa J, Matsuo I, Ito Y (2012) In vitro mannose trimming property of human ER α-1,2 mannosidase I. Glycoconj J 29:35–45. https://doi.org/10.1007/s10719-011-9362-1 · DOI
  106. Shenkman M, Ron E, Yehuda R et al (2018) Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates. Commun Biol 1:172. https://doi.org/10.1038/s42003-018-0174-8 · DOI
  107. Słomińska-Wojewódzka M, Sandvig K (2015) The role of lectin-carbohydrate interactions in the regulation of ER-associated protein degradation. Molecules 20:9816–9846. https://doi.org/10.3390/molecules20069816 · DOI
  108. Bhamidipati A, Denic V, Quan EM, Weissman JS (2005) Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen. Mol Cell 19:741–751 · DOI
  109. Kim W, Spear ED, Ng DT (2005) Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell 19:753–764 · DOI
  110. Szathmary R, Bielmann R, Nita-Lazar M et al (2005) Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell 19:765–775 · DOI
  111. Denic V, Quan EM, Weissman JS (2006) A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126:349–359 · DOI
  112. Olivari S, Galli C, Alanen H et al (2005) A novel stress-induced EDEM variant regulating endoplasmic reticulum associated glycoprotein degradation. J Biol Chem 280:2424–2428 · DOI
  113. Hosokawa N, Tremblay LO, Sleno B et al (2010) EDEM1 accelerates the trimming of α1,2-linked mannose on the C branch of N-glycans. Glycobiology 20:567–575 · DOI
  114. Ninagawa S, Okada T, Sumitomo Y et al (2014) EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step. J Cell Biol 206:347–356 · DOI
  115. Lamriben L, Oster ME, Tamura T et al (2018) EDEM1’s mannosidase-like domain binds ERAD client proteins in a redox-sensitive manner and possesses catalytic activity. J Biol Chem 293:13932–13945 · DOI
  116. Hosokawa N, Wada I, Nagasawa K et al (2008) Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP. J Biol Chem 283:20914–20924 · DOI
  117. van der Goot AT, Pearce MM, Leto DE et al (2018) Redundant and antagonistic roles of XTP3B and OS9 in decoding glycan and non-glycan degrons in ER-associated degradation. Mol Cell 70:516–530 · DOI
  118. Calì 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 · DOI
  119. Benyair R, Ogen-Shtern N, Mazkereth N et al (2015) Mammalian ER mannosidase I resides in quality control vesicles where it encounters its glycoprotein substrates. Mol Biol Cell 26:172–184 · DOI
  120. Gauss R, Kanehara K, Carvalho P et al (2011) A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum. Mol Cell 42:782–793 · DOI · Paper page
  121. Liu C-Y, Fujimori DG, Weissman JS (2016) Htm1p–Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation. Proc Natl Acad Sci USA 113:E4015–E4024 · DOI
  122. Cormier JH, Tamura T, Sunryd JC, Hebert DN (2010) EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex. Mol Cell 34:627–633 · DOI
  123. Ushioda R, Hoseki J, Nagata K (2013) Glycosylation-independent ERAD pathway serves as a backup system under ER stress. Mol Biol Cell 24:3155–3163 · DOI
  124. Tang H-Y, Huang C-H, Zhuang Y-H et al (2014) EDEM2 and OS-9 are required for ER-associated degradation of non-glycosylated sonic hedgehog. PLoS ONE 9:e92164 · DOI
  125. Saeed M, Suzuki R, Watanabe N et al (2011) Role of the endoplasmic reticulum-associated degradation (ERAD) pathway in degradation of hepatitis C virus envelope proteins and production of virus particles. J Biol Chem 286:37264–37273 · DOI
  126. Hatahet F, Ruddock LW (2007) Substrate recognition by the protein disulfide isomerases. FEBS J 274:5223–5234 · DOI
  127. Appenzeller-Herzog C, Riemer J, Christensen B et al (2008) A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells. EMBO J 27:2977–2987 · DOI
  128. Sato Y, Kojima R, Okumura M et al (2013) Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding. Sci Rep 3:2456 · DOI
  129. Sevier CS, Kaiser CA (2008) Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim Biophys Acta 1783:549–556 · DOI
  130. Oka OB, Bulleid NJ (2013) Forming disulfides in the endoplasmic reticulum. Biochim Biophys Acta 1833:2425–2429 · DOI
  131. McLaughlin SH, Bulleid NJ (1998) Thiol-independent interaction of protein disulphide isomerase with type X collagen during intra-cellular folding and assembly. Biochem J 331:793–800 · DOI
  132. Pirneskoski A, Klappa P, Lobell M et al (2004) Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase. J Biol Chem 279:10374–10381 · DOI
  133. Denisov AY, Määttänen P, Dabrowski C et al (2009) Solution structure of the bb′ domains of human protein disulfide isomerase. FEBS J 276:1440–1449 · DOI
  134. Okumura M, Kadokura H, Inaba K (2015) Structures and functions of protein disulfide isomerase family members involved in proteostasis in the endoplasmic reticulum. Free Radic Bio Med 83:314–322 · DOI
  135. Forster ML, Sivick K, Park Y et al (2006) Protein disulfide isomerase–like proteins play opposing roles during retrotranslocation. J Cell Biol 173:853–859 · DOI
  136. Frickel E-M, Frei P, Bouvier M et al (2004) ERp57 is a multifunctional thiol-disulfide oxidoreductase. J Biol Chem 279:18277–18287 · DOI
  137. Zapun A, Darby NJ, Tessier DC et al (1998) Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J Biol Chem 273:6009–6012 · DOI
  138. Walczak CP, Tsai B (2011) A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection. J Virol 85:2386–2396 · DOI
  139. Mazzarella RA, Srinivasan M, Haugejordan SM, Green M (1990) ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J Biol Chem 265:1094–1101 · DOI
  140. Kozlov G, Määttänen P, Schrag JD et al (2009) Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72. Structure 17:651–659 · DOI
  141. Jansen G, Määttänen P, Denisov AY et al (2012) An interaction map of endoplasmic reticulum chaperones and foldases. Mol Cell Proteom 11:710–723 · DOI
  142. Menon S, Lee J, Abplanalp WA et al (2007) Oxidoreductase Interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw Rat Dwarf. J Biol Chem 282:6183–6191 · DOI
  143. Maegawa K, Watanabe S, Noi K et al (2017) The highly dynamic nature of ERdj5 is key to efficient elimination of aberrant protein oligomers through ER-associated degradation. Structure 25:846–857 · DOI
  144. Anelli T, Ceppi S, Bergamelli L et al (2007) Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis. EMBO J 26:4177–4188 · DOI
  145. Tiziana A, Alessio M, Bachi A et al (2003) Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44. EMBO J 22:5015–5022 · DOI
  146. Qiang L, Wang H, Farmer SR (2007) Adiponectin secretion is regulated by SIRT1 and the endoplasmic reticulum oxidoreductase Ero1-Lα. Mol Cell Biol 27:4698–4707 · DOI
  147. Fraldi A, Zito E, Annunziata F et al (2008) Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44. Hum Mol Genet 17:2610–2621 · DOI
  148. Mariappan M, Radhakrishnan K, Dierks T et al (2008) ERp44 mediates a thiol-independent retention of formylglycine-generating enzyme in the endoplasmic reticulum. J Biol Chem 283:6375–6383 · DOI
  149. Anelli T, Sannino S, Sitia R (2015) Proteostasis and “redoxtasis” in the secretory pathway: tales of tails from ERp44 and immunoglobulins. Free Radic Bio Med 83:323–330 · DOI
  150. Watanabe S, Harayama M, Kanemura S et al (2017) Structural basis of pH-dependent client binding by ERp44, a key regulator of protein secretion at the ER-Golgi interface. Proc Natl Acad Sci USA 114:E3224–E3232 · DOI
  151. Wang L, Wang L, Vavassori S et al (2008) Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail. EMBO Rep 9:642–647 · DOI
  152. Vavassori S, Cortini M, Masui S et al (2013) A pH-regulated quality control cycle for surveillance of secretory protein assembly. Mol Cell 50:783–792 · DOI

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Metadata

Authors
Adams, B. M., Oster, M. E., & Hebert, D. N.
Venue
The Protein Journal
Publisher
Springer Science and Business Media LLC
Published
2019-04-19
Volume
38
Issue
3
Pages
317-329
ISSN
  • 1572-3887
  • 1875-8355
DOI
10.1007/s10930-019-09831-w
PMC
PMC6589386
Cited by
142
References
8
Language
en
Licence
Funders
  • National Institute of General Medical Sciences (GM086874)
  • Foundation for the National Institutes of Health (GM008515)

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