Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1

Molecular Biology of the Cell

Volumn 22, Issue 21, 2011, Pages 3945-3954

  Ron, Efrat ^a   Shenkman, Marina ^a   Groisman, Bella ^a   Izenshtein, Yana ^a   Leitman, Julia ^a   Lederkremer, Gerardo Z ^a  

^a TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; ENDOPLASMIC RETICULUM DEGRADATION ENHANCING ALPHA MANNOSIDASE 1 LIKE PROTEIN; GLYCAN; GLYCOPROTEIN; HISTONE H2A; MANNOSIDASE; PROTEIN IRE1; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; EMBRYO; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; GENE DELETION; GENE OVEREXPRESSION; HUMAN; HUMAN CELL; KIDNEY CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN REFOLDING; PROTEIN TRANSPORT; PROTEINASE INHIBITION; UPREGULATION;

ANIMALS; ASIALOGLYCOPROTEIN RECEPTOR; BINDING SITES; ENDOPLASMIC RETICULUM; ENDORIBONUCLEASES; GENE KNOCKDOWN TECHNIQUES; HEK293 CELLS; HUMANS; LECTINS; MANNOSE; MANNOSIDASES; MEMBRANE PROTEINS; MICE; NEOPLASM PROTEINS; NIH 3T3 CELLS; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; PROTEIN-SERINE-THREONINE KINASES; PROTEOLYSIS; RNA INTERFERENCE; UNFOLDED PROTEIN RESPONSE; UP-REGULATION;

EID: 80655144729     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E10-12-0944     Document Type: Article

References (51)

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. 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. (Pubitemid 351186147)
3. Avezov E, Ron E, Izenshtein Y, Adan Y, Lederkremer GZ (2010). Pulse-chase analysis of N-linked sugar chains from glycoproteins in mammalian cells. J Vis Exp 38, 1899-1903.
4. Ayalon-Soffer M, Shenkman M, Lederkremer GZ (1999). Differential role of mannose and glucose trimming in the ER degradation of asialoglycoprotein receptor subunits. J Cell Sci 112, 3309-3318. (Pubitemid 29507211)
5. Bernasconi R, Molinari M (2011). ERAD and ERAD tuning: disposal of cargo and of ERAD regulators from the mammalian ER. Curr Opin Cell Biol 23, 176-183.
6. Bernasconi R, Pertel T, Luban J, Molinari M (2008). A dual task for the Xbp1-responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal. J Biol Chem 283, 16446-16454.
7. Brummelkamp TR, Bernards R, Agami R (2002). A system for stable expression of short interfering RNAs in mammalian cells. Science 296, 550-553. (Pubitemid 34408678)
8. 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.
9. 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. (Pubitemid 351331014)
10. 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.
11. Cormier JH, Tamura T, Sunryd JC, Hebert DN (2009). EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex. Mol Cell 34, 627-633.
12. Fang S, Ferrone M, Yang C, Jensen JP, Tiwari S, Weissman AM (2001). The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc Natl Acad Sci USA 98, 14422-14427. (Pubitemid 33121407)
13. Frenkel Z, Gregory W, Kornfeld S, Lederkremer GZ (2003). Endoplasmic reticulum-associated degradation of mammalian glycoproteins involves sugar chain trimming to Man6-5GlcNAc2. J Biol Chem 278, 34119-34124. (Pubitemid 37553252)
14. Gauss R, Kanehara K, Carvalho P, Ng DT, Aebi M (2011). A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum. Mol Cell 42, 782-793.
15. Fbs2 recognize the protein moiety and sugar chains respectively of an ER-associated degradation substrate. Isr J Chem 46, 189-196.
16. Groisman B, Shenkman M, Ron E, Lederkremer GZ (2011). Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps. J Biol Chem 286, 1292-1300.
17. Hebert DN, Bernasconi R, Molinari M (2010). ERAD substrates: which way out? Semin Cell Dev Biol 21, 526-532.
18. Hosokawa N, Kamiya Y, Kato K (2010a). The role of MRH domain-containing lectins in ERAD. Glycobiology 20, 651-660.
19. 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.
20. 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. (Pubitemid 32509958)
21. Hosokawa N, Wada I, Nagasawa K, Moriyama T, Okawa K, Nagata K (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.
22. Hosokawa N, Wada I, Natsuka Y, Nagata K (2006). EDEM accelerates ERAD by preventing aberrant dimer formation of misfolded alpha1-antitrypsin. Genes Cells 11, 465-476.
23. Hosokawa N, You Z, Tremblay LO, Nagata K, Herscovics A (2007). Stimulation of ERAD of misfolded null Hong Kong alpha1-antitrypsin by Golgi alpha1,2-mannosidases. Biochem Biophys Res Commun 362, 626-632. (Pubitemid 47368138)
24. Hosomi A, Tanabe K, Hirayama H, Kim I, Rao H, Suzuki T (2010). Identification of an Htm1 (EDEM)-dependent, Mns1-independent endoplasmic reticulum-associated degradation (ERAD) pathway in Saccharomyces cerevisiae: application of a novel assay for glycoprotein ERAD. J Biol Chem 285, 24324-24334.
25. Jakob CA, Bodmer D, Spirig U, Battig P, Marcil A, Dignard D, Bergeron JJ, Thomas DY, Aebi M (2001). Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast. EMBO Rep 2, 423-430. (Pubitemid 32509959)
26. Kamhi-Nesher S, Shenkman M, Tolchinsky S, Fromm SV, Ehrlich R, Lederkremer GZ (2001). A novel quality control compartment derived from the endoplasmic reticulum. Mol Biol Cell 12, 1711-1723. (Pubitemid 33049724)
27. Kanehara K, Kawaguchi S, Ng DT (2007). The EDEM and Yos9p families of lectin-like ERAD factors. Semin Cell Dev Biol 18, 743-750. (Pubitemid 350138449)
28. Kang SW, Rane NS, Kim SJ, Garrison JL, Taunton J, Hegde RS (2006). Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 127, 999-1013. (Pubitemid 44803063)
29. Karaveg K, Moremen KW (2005). Energetics of substrate binding and catalysis by class 1 (glycosylhydrolase family 47) α-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control. J Biol Chem 280, 29837-29848. (Pubitemid 41177061)
30. Kondratyev M, Avezov E, Shenkman M, Groisman B, Lederkremer GZ (2007). PERK-dependent compartmentalization of ERAD and unfolded protein response machineries during ER stress. Exp Cell Res 313, 3395-3407. (Pubitemid 47404548)
31. Lederkremer GZ (2009). Glycoprotein folding, quality control and ER-associated degradation. Curr Opin Struct Biol 19, 515-523.
32. Lederkremer GZ, Glickman MH (2005). A window of opportunity: timing protein degradation by trimming of sugars and ubiquitins. Trends Biochem Sci 30, 297-303. (Pubitemid 40799047)
33. 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. (Pubitemid 36254653)
34. Oda Y, Hosokawa N, Wada I, Nagata K (2003). EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299, 1394-1397. (Pubitemid 36254652)
35. Oda Y, Okada T, Yoshida H, Kaufman RJ, Nagata K, Mori K (2006). Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation. J Cell Biol 172, 383-393. (Pubitemid 43187935)
36. Olivari S, Cali T, Salo KE, Paganetti P, Ruddock LW, Molinari M (2006). EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation. Biochem Biophys Res Commun 349, 1278-1284. (Pubitemid 44416396)
37. 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. (Pubitemid 47081005)
38. Quan EM, Kamiya Y, Kamiya D, Denic V, Weibezahn J, Kato K, Weissman JS (2008). Defining the glycan destruction signal for endoplasmic reticulum-associated degradation. Mol Cell 32, 870-877.
39. Shenkman M, Ayalon M, Lederkremer GZ (1997). Endoplasmic reticulum quality control of asialoglycoprotein receptor H2a involves a determinant for retention and not retrieval. Proc Natl Acad Sci USA 94, 11363-11368. (Pubitemid 27451004)
40. Shenkman M, Ehrlich M, Lederkremer GZ (2000). Masking of an endoplasmic reticulum retention signal by its presence in the two subunits of the asialoglycoprotein receptor. J Biol Chem 275, 2845-2851. (Pubitemid 30082058)
41. Shenkman M, Tolchinsky S, Kondratyev M, Lederkremer GZ (2007a). Transient arrest in proteasomal degradation during inhibition of translation in the unfolded protein response. Biochem J 404, 509-516. (Pubitemid 46953925)
42. Shenkman M, Tolchinsky S, Lederkremer GZ (2007b). ER stress induces alternative nonproteasomal degradation of ER proteins but not of cytosolic ones. Cell Stress Chaperones 12, 373-383.
43. Termine DJ, Moremen KW, Sifers RN (2009). The mammalian UPR boosts glycoprotein ERAD by suppressing the proteolytic downregulation of ER mannosidase I. J Cell Sci 122, 976-984.
44. Tirasophon W, Lee K, Callaghan B, Welihinda A, Kaufman RJ (2000). The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response. Genes Dev 14, 2725-2736. (Pubitemid 32531199)
45. Tolchinsky S, Yuk MH, Ayalon M, Lodish HF, Lederkremer GZ (1996). Membrane-bound versus secreted forms of human asialoglycoprotein receptor subunits - role of a juxtamembrane pentapeptide. J Biol Chem 271, 14496-14503.
46. Travers KJ, Patil CK, Wodicka L, Lockhart DJ, Weissman JS, Walter P (2000). Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101, 249-258.
47. 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.
48. Wang XZ, Harding HP, Zhang Y, Jolicoeur EM, Kuroda M, Ron D (1998). Cloning of mammalian Ire1 reveals diversity in the ER stress responses. EMBO J 17, 5708-5717. (Pubitemid 28445982)
49. Hong Kong via the C-terminal MRH domain in a glycan-dependent manner. Glycobiology 20, 348-355.
50. Yoshida H, Matsui T, Hosokawa N, Kaufman RJ, Nagata K, Mori K (2003). A time-dependent phase shift in the mammalian unfolded protein response. Dev Cell 4, 265-271. (Pubitemid 36221802)
51. 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 USA 104, 4407-4412. (Pubitemid 47186239)