The glycan code of the endoplasmic reticulum: Asparagine-linked carbohydrates as protein maturation and quality-control tags

Trends in Cell Biology

Volumn 15, Issue 7, 2005, Pages 364-370

  Hebert, Daniel N ^a   Garman, Scott C ^a   Molinari, Maurizio ^b  

^a UNIVERSITY OF MASSACHUSETTS   (United States)

^b INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARAGINE LINKED OLIGOSACCHARIDE; CARBOHYDRATE; CARBOHYDRATE BINDING PROTEIN; CHAPERONE; GLUCOSE; GLYCAN; GLYCOPROTEIN; GLYCOSIDASE; MANNOSE; OXIDOREDUCTASE; PROTEASOME; RECEPTOR; TRANSFERASE;

CARBOHYDRATE ANALYSIS; CELL FUNCTION; CHEMICAL MODIFICATION; CHEMICAL STRUCTURE; CYTOSOL; ENDOPLASMIC RETICULUM; ENZYME SPECIFICITY; GLYCOSYLATION; HYDROPHILICITY; INTRACELLULAR TRANSPORT; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROCESSING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROCESSING; PROTEIN QUALITY; PROTEIN STRUCTURE; PROTEIN TARGETING; PROTEIN TRANSPORT; QUALITY CONTROL; REVIEW; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE; SECRETION;

ANIMALS; ASPARAGINE; ENDOPLASMIC RETICULUM; GLYCOPROTEINS; GLYCOSYLATION; HUMANS; MEMBRANE PROTEINS; MOLECULAR CHAPERONES; POLYSACCHARIDES; PROTEIN FOLDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN TRANSPORT;

EID: 21744447192     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2005.05.007     Document Type: Review

References (72)

1. R. Apweiler On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database Biochim. Biophys. Acta 1473 1999 4 8
2. A.J. Petrescu Statistical analysis of the protein environment of N-glycosylation sites: implications for occupancy, structure, and folding Glycobiology 14 2004 103 114
3. J.B. Lowe, and J.D. Marth A genetic approach to mammalian glycan function Annu. Rev. Biochem. 72 2003 643 691
4. A. Helenius, and M. Aebi Roles of N-linked glycans in the endoplasmic reticulum Annu. Rev. Biochem. 73 2004 1019 1049
5. R. Knauer, and L. Lehle The oligosaccharyltransferase complex from yeast Biochim. Biophys. Acta 1426 1999 259 273
6. I. Nilsson Photocross-linking of nascent chains to the STT3 subunit of the oligosaccharyltransferase complex J. Cell Biol. 161 2003 715 725
7. D.J. Kelleher Oligosaccharyltransferase isoforms that contain different catalytic STT3 subunits have distinct enzymatic properties Mol. Cell 12 2003 101 111
8. I. Nilsson, and G. von Heijne Determination of the distance between oligosaccharyltransferase active site and the endoplasmic reticulum membrane J. Biol. Chem. 268 1993 5798 5801
9. M. Kowarik Protein folding during cotranslational translocation in the endoplasmic reticulum Mol. Cell 10 2002 769 778
10. S. Allen Intracellular folding of tissue-type plasminogen activator: Effects of disulfide bond formation and N-linked glycosylation and secretion J. Biol. Chem. 270 1995 4797 4804
11. T.C. Huffaker, and P.W. Robbins Yeast mutants deficient in protein glycosylation Proc. Natl. Acad. Sci. U. S. A. 80 1983 7466 7470
12. A. Yan, and W.J. Lennarz Unraveling the mechanism of protein N-glycosylation J. Biol. Chem. 280 2005 3121 3124
13. C. Hammond Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum Proc. Natl. Acad. Sci. U. S. A. 91 1994 913 917
14. J.D. Schrag The structure of calnexin, an ER chaperone involved in quality control of protein folding Mol. Cell 8 2001 633 644
15. M. Kapoor Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone J. Biol. Chem. 278 2003 6194 6200
16. I. Wada Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms J. Biol. Chem. 270 1995 20298 20304
17. D.N. Hebert The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin J. Cell Biol. 139 1997 613 623
18. L. Ellgaard NMR structure of the calreticulin P-domain Proc. Natl. Acad. Sci. U. S. A. 98 2001 3133 3138
19. W. Chen Cotranslational folding and calnexin binding of influenza hemagglutinin in the endoplasmic reticulum Proc. Natl. Acad. Sci. U. S. A. 92 1995 6229 6233
20. M. Molinari, and A. Helenius Chaperone selection during glycoprotein translocation into the endoplasmic reticulum Science 288 2000 331 333
21. R. Daniels N-linked glycans direct the cotranslational maturation of influenza hemagglutinin Mol. Cell 11 2003 79 90
22. D.J. Schnell, and D.N. Hebert Protein modulators: multi-functional mediators of protein translocation across membranes Cell 112 2003 491 505
23. D.N. Hebert Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes EMBO J. 15 1996 2961 2968
24. A. Vassilakos The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules EMBO J. 15 1996 1495 1506
25. S. Rajagopalan Retention of unassembled components of integral membrane proteins by calnexin Science 263 1994 387 390
26. D.N. Hebert Glucose trimming and reglucosylation determines glycoprotein association with calnexin Cell 81 1995 425 433
27. J.D. Oliver Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins Science 275 1997 86 88
28. E.M. Frickel TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain Proc. Natl. Acad. Sci. U. S. A. 99 2002 1954 1959
29. S. Pollock Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system EMBO J. 23 2004 1020 1029
30. E.S. Trombetta, and A.J. Parodi Quality control and protein folding in the secretory pathway Annu. Rev. Cell Dev. Biol. 19 2003 649 676
31. M. Guerin, and A.J. Parodi The UDP-glucose:Glycoprotein glucosyltransferase is organized in at least two tightly bound domains from yeast to mammals J. Biol. Chem. 278 2003 20540 20546
32. M. Sousa, and A.J. Parodi The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc: glycoprotein glucosyltransferase EMBO J. 14 1995 4196 4203
33. S.C. Taylor Glycopeptide specificity of the secretory protein folding sensor UDP-glucose glycoprotein:glucosyltransferse EMBO Rep. 4 2003 405 411
34. J.J. Caramelo The endoplasmic reticulum glucosyltransferase recognizes nearly native glycoprotein folding intermediates J. Biol. Chem. 279 2004 46280 46285
35. C. Ritter, and A. Helenius Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase Nat. Struct. Biol. 7 2000 278 280
36. S.C. Taylor The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation Nat. Struct. Mol. Biol. 11 2004 128 134
37. H.P. Hauri Lectins and traffic in the secretory pathway FEBS Lett. 476 2000 32 37
38. F. Vollenweider Mistargeting of the lectin ERGIC-53 to the endoplasmic reticulum of HeLa cells impairs the secretion of a lysosomal enzyme J. Cell Biol. 142 1998 377 389
39. W.C. Nichols Mutations in the ER-Golgi intermediate compartment protein ERGIC-53 cause combined deficiency of coagulation factors V and VIII Cell 93 1998 61 70
40. C. Appenzeller The lectin ERGIC-53 is a cargo transport receptor for glycoproteins Nat. Cell Biol. 1 1999 330 334
41. C. Appenzeller-Herzog pH-induced conversion of the transport lectin ERGIC-53 triggers glycoprotein release J. Biol. Chem. 279 2004 12943 12950
42. A.A. McCracken, and J.L. Brodsky Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD) BioEssays 25 2003 868 877
43. M. Ermonval N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation Glycobiology 11 2001 565 576
44. N. Hosokawa Enhancement of endoplasmic reticulum (ER) degradation of misfolded null Hong Kong alpha1-antitrypsin by human ER mannosidase I J. Biol. Chem. 278 2003 26287 26294
45. Z. Frenkel Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2 J. Biol. Chem. 278 2003 34119 34124
46. K. Su Pre-Golgi degradation of yeast prepro-α-factor in a mammalian cell J. Biol. Chem. 268 1993 14301 14309
47. C.A. Jakob Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure J. Cell Biol. 142 1998 1223 1233
48. R.G. Spiro Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi J. Biol. Chem. 271 1996 11588 11594
49. L. Ellgaard Setting the standards: quality control in the secretory pathway Science 286 1999 1882 1888
50. Y. Liu Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome J. Biol. Chem. 274 1999 5861 5867
51. M. Molinari Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER J. Cell Biol. 158 2002 247 257
52. C.M. Cabral Dissecting glycoprotein quality control in the secretory pathway Trends Biochem. Sci. 26 2001 619 624
53. N. Hosokawa A novel ER α-mannosidase-like protein accelerates ER-associated degradation EMBO Rep. 2 2001 415 422
54. S.W. Mast Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins Glycobiology 15 2005 421 436
55. S. Olivari A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation J. Biol. Chem. 280 2005 2424 2428
56. K. Nakatsukasa Mnl1p, an alpha-mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins J. Biol. Chem. 276 2001 8635 8638
57. K. Karaveg Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control J. Biol. Chem. 280 2005 16197 16207
58. C.A. Jakob Lectins of the ER quality control machinery Results Probl. Cell Differ. 33 2001 1 17
59. H. Yoshida A time-dependent phase shift in the mammalian unfolded protein response Dev. Cell 4 2003 265 271
60. K.K. Eriksson EDEM contributes to maintenance of protein folding efficiency and secretory capacity J. Biol. Chem. 279 2004 44600 44605
61. M. Molinari Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle Science 299 2003 1397 1400
62. Y. Oda EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin Science 299 2003 1394 1397
63. C.A. Jakob Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast EMBO Rep. 2 2001 423 430
64. A. Hershko Basic Medical Research Award. The ubiquitin system Nat. Med. 6 2000 1073 1081
65. Y. Yoshida E3 ubiquitin ligase that recognizes sugar chains Nature 418 2002 438 442
66. Y. Yoshida Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates EMBO Rep. 6 2005 239 244
67. T. Suzuki PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase J. Cell Biol. 149 2000 1039 1051
68. C. Hirsch A role for N-glycanase in the cytosolic turnover of glycoproteins EMBO J. 22 2003 1036 1046
69. S. Misaghi Using a small molecule inhibitor of Peptide: N-glycanase to probe its role in glycoprotein turnover Chem. Biol. 11 2004 1677 1687
70. Y. Li, and P. Camacho Ca2+-dependent redox modulation of SERCA 2b by ERp57 J. Cell Biol. 164 2004 35 46
71. P.M. Rudd Glycosylation and the immune system Science 291 2001 2370 2376
72. M. Aebi, and T. Hennet Congenital disorders of glycosylation: genetic model systems lead the way Trends Cell Biol. 11 2001 136 141