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Volumn 142, Issue 2, 2014, Pages 153-169

ERADication of EDEM1 occurs by selective autophagy and requires deglycosylation by cytoplasmic peptide N-glycanase

Author keywords

Alfy; Cytosolic peptide N glycanase; EDEM1; Endoplasmic reticulum; LC3; NBR1; p62 SQSTM1; Selective autophagy

Indexed keywords

AUTOPHAGY LINKED FYVE PROTEIN; ER DEGRADATION ENHANCING ALPHA MANNOSIDASE LIKE 1 PROTEIN; GLYCOPEPTIDASE; HISTONE DEACETYLASE; MANNOSIDASE; NEIGHBOR OF BRCA1 GENE 1; PROTEIN P62; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG; EDEM1 PROTEIN, HUMAN; HISTONE DEACETYLASE INHIBITOR; MEMBRANE PROTEIN; NBR1 PROTEIN, HUMAN; PROTEIN; PROTEIN SERINE THREONINE KINASE; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SMALL INTERFERING RNA; SQSTM1 PROTEIN, HUMAN; TRANSCRIPTION FACTOR; WDFY3 PROTEIN, HUMAN;

EID: 84905001446     PISSN: 09486143     EISSN: 1432119X     Source Type: Journal    
DOI: 10.1007/s00418-014-1204-3     Document Type: Article
Times cited : (19)

References (95)
  • 1
    • 84867804213 scopus 로고    scopus 로고
    • Protein folding and quality control in the ER
    • Morimoto RI, Selkoe DJ, Kelly JW (eds) Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Araki K, Nagata K (2012) Protein folding and quality control in the ER. In: Morimoto RI, Selkoe DJ, Kelly JW (eds) Protein homeostasis. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, pp 121-145
    • (2012) Protein Homeostasis , pp. 121-145
    • Araki, K.1    Nagata, K.2
  • 2
    • 10144220633 scopus 로고    scopus 로고
    • The organization of endoplasmic reticulum export complexes
    • DOI 10.1083/jcb.135.1.19
    • Bannykh SI, Rowe T, Balch WE (1996) The organization of endoplasmic reticulum export complexes. J Cell Biol 135:19-35 (Pubitemid 26337734)
    • (1996) Journal of Cell Biology , vol.135 , Issue.1 , pp. 19-35
    • Bannykh, S.I.1    Rowe, T.2    Balch, W.E.3
  • 4
    • 24944583185 scopus 로고    scopus 로고
    • Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen
    • DOI 10.1016/j.molcel.2005.07.027, PII S1097276505015248
    • 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 (Pubitemid 41316669)
    • (2005) Molecular Cell , vol.19 , Issue.6 , pp. 741-751
    • Bhamidipati, A.1    Denic, V.2    Quan, E.M.3    Weissman, J.S.4
  • 5
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • DOI 10.1083/jcb.200507002
    • Bjorkoy G, Lamark T, Brech A, Outzen H, Perander M, Overvatn A, Stenmark H, Johansen T (2005) p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 171:603-614 (Pubitemid 41668720)
    • (2005) Journal of Cell Biology , vol.171 , Issue.4 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 6
    • 1442313919 scopus 로고    scopus 로고
    • A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised
    • DOI 10.1038/sj.emboj.7600090
    • Blom D, Hirsch C, Stern P, Tortorella D, Ploegh HL (2004) A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised. EMBO J 3:650-658 (Pubitemid 38282396)
    • (2004) EMBO Journal , vol.23 , Issue.3 , pp. 650-658
    • Blom, D.1    Hirsch, C.2    Stern, P.3    Tortorella, D.4    Ploegh, H.L.5
  • 7
    • 79959481888 scopus 로고    scopus 로고
    • Protein folding and modification in the mammalian endoplasmic reticulum
    • Braakman I, Bulleid NJ (2011) Protein folding and modification in the mammalian endoplasmic reticulum. Annu Rev Biochem 80:71-99
    • (2011) Annu Rev Biochem , vol.80 , pp. 71-99
    • Braakman, I.1    Bulleid, N.J.2
  • 8
    • 8844270968 scopus 로고    scopus 로고
    • A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins
    • DOI 10.1016/j.febslet.2004.10.039, PII S0014579304012773
    • Buschhorn BA, Kostova Z, Medicherla B, Wolf DH (2004) A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins. FEBS Lett 577:422-426 (Pubitemid 39535324)
    • (2004) FEBS Letters , vol.577 , Issue.3 , pp. 422-426
    • Buschhorn, B.A.1    Kostova, Z.2    Medicherla, B.3    Wolf, D.H.4
  • 9
    • 43549087339 scopus 로고    scopus 로고
    • Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities
    • 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
    • (2008) Biochem Biophys Res Commun , vol.371 , pp. 405-410
    • Cali, T.1    Galli, C.2    Olivari, S.3    Molinari, M.4
  • 10
    • 78149482323 scopus 로고    scopus 로고
    • Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p
    • Carvalho P, Stanley AM, Rapoport TA (2010) Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p. Cell 143:579-591
    • (2010) Cell , vol.143 , pp. 579-591
    • Carvalho, P.1    Stanley, A.M.2    Rapoport, T.A.3
  • 11
    • 84904977631 scopus 로고    scopus 로고
    • Cellular strategies of protein quality control
    • Morimoto RI, Selkoe DJ, Kelly JW (eds) Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Chen B, Retzlaff M, Roos T, Frydman J (2012) Cellular strategies of protein quality control. In: Morimoto RI, Selkoe DJ, Kelly JW (eds) Protein homeostasis. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, pp 33-46
    • (2012) Protein Homeostasis , pp. 33-46
    • Chen, B.1    Retzlaff, M.2    Roos, T.3    Frydman, J.4
  • 13
    • 59849119398 scopus 로고    scopus 로고
    • Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum
    • 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
    • (2009) J Cell Biol , vol.184 , pp. 159-172
    • Clerc, S.1    Hirsch, C.2    Oggier, D.M.3    Deprez, P.4    Jakob, C.5    Sommer, T.6    Aebi, M.7
  • 14
    • 66449136067 scopus 로고    scopus 로고
    • EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex
    • 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
    • (2009) Mol Cell , vol.34 , pp. 627-633
    • Cormier, J.H.1    Tamura, T.2    Sunryd, J.C.3    Hebert, D.N.4
  • 15
    • 33746208871 scopus 로고    scopus 로고
    • A Luminal Surveillance Complex that Selects Misfolded Glycoproteins for ER-Associated Degradation
    • DOI 10.1016/j.cell.2006.05.045, PII S0092867406008610
    • Denic V, Quan EM, Weissman JS (2006) A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126:349-359 (Pubitemid 44092967)
    • (2006) Cell , vol.126 , Issue.2 , pp. 349-359
    • Denic, V.1    Quan, E.M.2    Weissman, J.S.3
  • 17
    • 23144449583 scopus 로고    scopus 로고
    • Delivery of ubiquitinated substrates to protein-unfolding machines
    • DOI 10.1038/ncb0805-742
    • Elsasser S, Finley D (2005) Delivery of ubiquitinated substrates to protein-unfolding machines. Nat Cell Biol 7:742-749 (Pubitemid 41079042)
    • (2005) Nature Cell Biology , vol.7 , Issue.8 , pp. 742-749
    • Elsasser, S.1    Finley, D.2
  • 21
    • 33746587049 scopus 로고    scopus 로고
    • A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
    • DOI 10.1038/ncb1445, PII NCB1445
    • Gauss R, Jarosch E, Sommer T, Hirsch C (2006) A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery. Nat Cell Biol 8:849-854 (Pubitemid 44151588)
    • (2006) Nature Cell Biology , vol.8 , Issue.8 , pp. 849-854
    • Gauss, R.1    Jarosch, E.2    Sommer, T.3    Hirsch, C.4
  • 22
    • 79959357020 scopus 로고    scopus 로고
    • A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum
    • Gauss R, Kanehara K, Carvalho P, Ng DTW, 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
    • (2011) Mol Cell , vol.42 , pp. 782-793
    • Gauss, R.1    Kanehara, K.2    Carvalho, P.3    Ng, D.T.W.4    Aebi, M.5
  • 23
    • 35148815642 scopus 로고    scopus 로고
    • Fluorescently labeled inhibitor for profiling cytoplasmic peptide: N-glycanase
    • DOI 10.1093/glycob/cwm079
    • Hagihara S, Miyazaki A, Matsuo I, Tatami A, Suzuki T, Ito Y (2007) Fluorescently labeled inhibitor for profiling cytoplasmic peptide: N-glycanase. Glycobiology 17:1070-1076 (Pubitemid 47543400)
    • (2007) Glycobiology , vol.17 , Issue.10 , pp. 1070-1076
    • Hagihara, S.1    Miyazaki, A.2    Matsuo, I.3    Tatami, A.4    Suzuki, T.5    Ito, Y.6
  • 24
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • DOI 10.1146/annurev.biochem.73.011303.073752
    • Helenius A, Aebi M (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73:1019-1049 (Pubitemid 39050393)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 25
    • 69249206631 scopus 로고    scopus 로고
    • A cell culture system for the induction of Mallory bodies: Mallory bodies and aggresomes represent different types of inclusion bodies
    • Hirano K, Guhl B, Roth J, Ziak M (2009) A cell culture system for the induction of Mallory bodies: Mallory bodies and aggresomes represent different types of inclusion bodies. Histochem Cell Biol 132:293-304
    • (2009) Histochem Cell Biol , vol.132 , pp. 293-304
    • Hirano, K.1    Guhl, B.2    Roth, J.3    Ziak, M.4
  • 26
    • 0037416196 scopus 로고    scopus 로고
    • A role for N-glycanase in the cytosolic turnover of glycoproteins
    • DOI 10.1093/emboj/cdg107
    • Hirsch C, Blom D, Ploegh HL (2003) A role for N-glycanase in the cytosolic turnover of glycoproteins. EMBO J 22:1036-1046 (Pubitemid 36313588)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 1036-1046
    • Hirsch, C.1    Blom, D.2    Ploegh, H.L.3
  • 28
    • 67650535999 scopus 로고    scopus 로고
    • Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans
    • Hosokawa N, Kamiya Y, Kamiya D, Kato K, Nagata K (2009) Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J Biol Chem 284:17061-17068
    • (2009) J Biol Chem , vol.284 , pp. 17061-17068
    • Hosokawa, N.1    Kamiya, Y.2    Kamiya, D.3    Kato, K.4    Nagata, K.5
  • 30
    • 68649100255 scopus 로고    scopus 로고
    • The proteostasis boundary in misfolding diseases of membrane traffic
    • Hutt DM, Powers ET, Balch WE (2009) The proteostasis boundary in misfolding diseases of membrane traffic. FEBS Lett 583:2639-2646
    • (2009) FEBS Lett , vol.583 , pp. 2639-2646
    • Hutt, D.M.1    Powers, E.T.2    Balch, W.E.3
  • 32
    • 28844475400 scopus 로고    scopus 로고
    • HDAC6 and microtubules are required for autophagic degradation of aggregated Huntingtin
    • DOI 10.1074/jbc.M508786200
    • Iwata A, Riley BE, Johnston JA, Kopito R (2005) HDAC6 and microtubules are required for autophagic degradation of aggregated huntingtin. J Biol Chem 280:40282-40292 (Pubitemid 41779165)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 40282-40292
    • Iwata, A.1    Riley, B.E.2    Johnston, J.A.3    Kopito, R.R.4
  • 33
    • 0032494135 scopus 로고    scopus 로고
    • Degradation of misfolded endoplasmic reticulum glycoproteins in saccharomyces cerevisiae is determined by a specific oligosaccharide structure
    • DOI 10.1083/jcb.142.5.1223
    • Jakob CA, Burda P, Roth J, Aebi M (1998) Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 142:1223-1233 (Pubitemid 28429104)
    • (1998) Journal of Cell Biology , vol.142 , Issue.5 , pp. 1223-1233
    • Jakob, C.A.1    Burda, P.2    Roth, J.3    Aebi, M.4
  • 35
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T, Lamark T (2011) Selective autophagy mediated by autophagic adapter proteins. Autophagy 7:279-296
    • (2011) Autophagy , vol.7 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 36
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • DOI 10.1083/jcb.143.7.1883
    • Johnston JA, Ward CL, Kopito R (1998) Aggresomes: a cellular response to misfolded proteins. J Cell Biol 143:1883-1898 (Pubitemid 29022611)
    • (1998) Journal of Cell Biology , vol.143 , Issue.7 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 37
    • 12744281810 scopus 로고    scopus 로고
    • Misfolding of glycoproteins is a prerequisite for peptide: N-glycanase mediated deglycosylation
    • Joshi S, Katiyar S, Lennarz WJ (2005) Misfolding of glycoproteins is a prerequisite for peptide: N-glycanase mediated deglycosylation. FEBS Lett 579:823-826
    • (2005) FEBS Lett , vol.579 , pp. 823-826
    • Joshi, S.1    Katiyar, S.2    Lennarz, W.J.3
  • 39
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D, Kopito R, Frydman J (2008) Misfolded proteins partition between two distinct quality control compartments. Nature 454:1088-1095
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 40
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • DOI 10.1016/S0092-8674(03)00939-5
    • Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, Yao TP (2003) The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115:727-738 (Pubitemid 38030301)
    • (2003) Cell , vol.115 , Issue.6 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.-P.6
  • 41
    • 24944552879 scopus 로고    scopus 로고
    • Yos9p detects and targets misfolded glycoproteins for ER-associated degradation
    • DOI 10.1016/j.molcel.2005.08.010, PII S1097276505015285
    • Kim W, Spear ED, Ng DT (2005) Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell 19:753-764 (Pubitemid 41316670)
    • (2005) Molecular Cell , vol.19 , Issue.6 , pp. 753-764
    • Kim, W.1    Spear, E.D.2    Ng, D.T.W.3
  • 44
    • 0029033904 scopus 로고
    • Identification and distribution of peptide: N-glycanase (PNGase) in mouse organs
    • Kitajima K, Suzuki T, Kouchi Z, Inoue S, Inoue Y (1995) Identification and distribution of peptide: N-glycanase (PNGase) in mouse organs. Arch Biochem Biophys 319:393-401
    • (1995) Arch Biochem Biophys , vol.319 , pp. 393-401
    • Kitajima, K.1    Suzuki, T.2    Kouchi, Z.3    Inoue, S.4    Inoue, Y.5
  • 49
    • 0022467150 scopus 로고
    • Immunolocalization of the oligosaccharide trimming enzyme glucosidase II
    • Lucocq JM, Brada D, Roth J (1986) Immunolocalization of the oligosaccharide trimming enzyme glucosidase II. J Cell Biol 102:2137-2146 (Pubitemid 16052153)
    • (1986) Journal of Cell Biology , vol.102 , Issue.6 , pp. 2137-2146
    • Lucocq, J.M.1    Brada, D.2    Roth, J.3
  • 50
    • 8544222633 scopus 로고    scopus 로고
    • Rad23 and Rpn10: Perennial wallflowers join the melee
    • Madura K (2004) Rad23 and Rpn10: perennial wallflowers join the melee. Trends Biochem Sci 29:637-640
    • (2004) Trends Biochem Sci , vol.29 , pp. 637-640
    • Madura, K.1
  • 52
    • 10644226176 scopus 로고    scopus 로고
    • Using a small molecule inhibitor of peptide: N-glycanaseto probe its role in glycoprotein turnover
    • DOI 10.1016/j.chembiol.2004.11.010, PII S1074552104003345
    • Misaghi S, Pacold ME, Blom D, Ploegh HL, Korbel GA (2004) Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover. Chem Biol 11:1677-1687 (Pubitemid 39651302)
    • (2004) Chemistry and Biology , vol.11 , Issue.12 , pp. 1677-1687
    • Misaghi, S.1    Pacold, M.E.2    Blom, D.3    Ploegh, H.L.4    Korbel, G.A.5
  • 54
    • 60449117244 scopus 로고    scopus 로고
    • Systematic synthesis and inhibitory activity of haloacetamidyl oligosaccharide derivatives toward cytoplasmic peptide: N-glycanase
    • Miyazaki A, Matsuo I, Hagihara S, Kakegawa A, Suzuki T, Ito Y (2009) Systematic synthesis and inhibitory activity of haloacetamidyl oligosaccharide derivatives toward cytoplasmic peptide: N-glycanase. Glycoconj J 26:133-140
    • (2009) Glycoconj J , vol.26 , pp. 133-140
    • Miyazaki, A.1    Matsuo, I.2    Hagihara, S.3    Kakegawa, A.4    Suzuki, T.5    Ito, Y.6
  • 55
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: Renovation of cells and tissues
    • Mizushima N, Komatsu M (2011) Autophagy: renovation of cells and tissues. Cell 147:728-741
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 56
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • DOI 10.1038/nature06639, PII NATURE06639
    • Mizushima N, Levine B, Cuervo AM, Klionsky DJ (2008) Autophagy fights disease through cellular self-digestion. Nature 451:1069-1075 (Pubitemid 351317450)
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 57
    • 75749122303 scopus 로고    scopus 로고
    • Methods in mammalian autophagy research
    • Mizushima N, Yoshimori T, Levine B (2010) Methods in mammalian autophagy research. Cell 140:313-326
    • (2010) Cell , vol.140 , pp. 313-326
    • Mizushima, N.1    Yoshimori, T.2    Levine, B.3
  • 60
    • 0035937853 scopus 로고    scopus 로고
    • Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins
    • Nakatsukasa K, Nishikawa S, Hosokawa N, Nagata K, Endo T (2001) Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins. J Biol Chem 276:8635-8638
    • (2001) J Biol Chem , vol.276 , pp. 8635-8638
    • Nakatsukasa, K.1    Nishikawa, S.2    Hosokawa, N.3    Nagata, K.4    Endo, T.5
  • 61
    • 13244265787 scopus 로고    scopus 로고
    • A novel stress-induced EDEM Variant regulating endoplasmic reticulum-associated glycoprotein degradation
    • DOI 10.1074/jbc.C400534200
    • 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 (Pubitemid 40189341)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.4 , pp. 2424-2428
    • Olivari, S.1    Galli, C.2    Alanen, H.3    Ruddock, L.4    Molinari, M.5
  • 62
    • 33748795800 scopus 로고    scopus 로고
    • EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation
    • DOI 10.1016/j.bbrc.2006.08.186, PII S0006291X06019887
    • 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)
    • (2006) Biochemical and Biophysical Research Communications , vol.349 , Issue.4 , pp. 1278-1284
    • Olivari, S.1    Cali, T.2    Salo, K.E.H.3    Paganetti, P.4    Ruddock, L.W.5    Molinari, M.6
  • 63
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein biosynthesis
    • Palade G (1975) Intracellular aspects of the process of protein biosynthesis. Science 189:347-358
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.1
  • 65
    • 77949324195 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of p62/SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies
    • Pankiv S, Lamark T, Bruun JA, Overvatn A, Bjorkoy G, Johansen T (2010) Nucleocytoplasmic shuttling of p62/SQSTM1 and its role in recruitment of nuclear polyubiquitinated proteins to promyelocytic leukemia bodies. J Biol Chem 285:5941-5953
    • (2010) J Biol Chem , vol.285 , pp. 5941-5953
    • Pankiv, S.1    Lamark, T.2    Bruun, J.A.3    Overvatn, A.4    Bjorkoy, G.5    Johansen, T.6
  • 66
    • 0035949651 scopus 로고    scopus 로고
    • Identification of proteins that interact with mammalian peptide: N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation
    • DOI 10.1073/pnas.201393498
    • Park H, Suzuki T, Lennarz WJ (2001) Identification of proteins that interact with mammalian peptide: N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation. Proc Natl Acad Sci USA 98:11163-11168 (Pubitemid 32928700)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.20 , pp. 11163-11168
    • Park, H.1    Suzuki, T.2    Lennarz, W.J.3
  • 67
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3'-kinases are involved in signaling pa7thways that control macroautophagy in HT-29 cells
    • DOI 10.1074/jbc.275.2.992
    • Petiot A, Ogier-Denis E, Blommaart EF, Meijer AJ, Codogno P (2000) Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem 275:992-998 (Pubitemid 30051145)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.C.3    Meijer, A.J.4    Codogno, P.5
  • 70
    • 0001688044 scopus 로고
    • The protein A-gold (pAg) technique - A qualitative and quantitative approach for antigen localization on thin sections
    • Bullock G, Petrusz P (eds) Academic Press, London
    • Roth J (1982) The protein A-gold (pAg) technique - a qualitative and quantitative approach for antigen localization on thin sections. In: Bullock G, Petrusz P (eds) Techniques in immunocytochemistry, vol 1. Academic Press, London, pp 108-133
    • (1982) Techniques in Immunocytochemistry , vol.1 , pp. 108-133
    • Roth, J.1
  • 71
    • 0024376736 scopus 로고
    • Postembedding labeling on Lowicryl K4 M tissue sections: Detection and modification of cellular components
    • Tartakoff AM (ed) Academic Press, San Diego
    • Roth J (1989) Postembedding labeling on Lowicryl K4 M tissue sections: detection and modification of cellular components. In: Tartakoff AM (ed) Methods in cell biology, vol 31. Academic Press, San Diego, pp 513-551
    • (1989) Methods in Cell Biology , vol.31 , pp. 513-551
    • Roth, J.1
  • 72
    • 0018082456 scopus 로고
    • Ultrastructural localization of intracellular antigens by the use of protein A-gold complex
    • Roth J, Bendayan M, Orci L (1978) Ultrastructural localization of intracellular antigens by the use of protein A-gold complex. J Histochem Cytochem 26:1074-1081 (Pubitemid 9076936)
    • (1978) Journal of Histochemistry and Cytochemistry , vol.26 , Issue.12 , pp. 1074-1081
    • Roth, J.1    Bendayan, M.2    Orci, L.3
  • 73
    • 0024314626 scopus 로고
    • Prevention of non-specific interactions of gold-labeled reagents on tissue sections
    • DOI 10.1007/BF00495015
    • Roth J, Taatjes DJ, Warhol MJ (1989) Prevention of non-specific interactions of gold-labeled reagents on tissue sections. Histochemistry 92:47-56 (Pubitemid 19160752)
    • (1989) Histochemistry , vol.92 , Issue.1 , pp. 47-56
    • Roth, J.1    Taatjes, D.J.2    Warhol, M.J.3
  • 75
    • 64749087257 scopus 로고    scopus 로고
    • Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase
    • Sato BK, Schulz D, Do PH, Hampton RY (2009) Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase. Mol Cell 34:212-222
    • (2009) Mol Cell , vol.34 , pp. 212-222
    • Sato, B.K.1    Schulz, D.2    Do, P.H.3    Hampton, R.Y.4
  • 77
    • 36249024826 scopus 로고    scopus 로고
    • Cytoplasmic peptide: N-glycanase and catabolic pathway for free N-glycans in the cytosol
    • Suzuki T (2007) Cytoplasmic peptide: N-glycanase and catabolic pathway for free N-glycans in the cytosol. Semin Cell Dev Biol 18:762-769
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 762-769
    • Suzuki, T.1
  • 79
    • 0035877846 scopus 로고    scopus 로고
    • Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast
    • Suzuki T, Park H, Kwofie MA, Lennarz WJ (2001) Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast. J Biol Chem 276:21601-21607
    • (2001) J Biol Chem , vol.276 , pp. 21601-21607
    • Suzuki, T.1    Park, H.2    Kwofie, M.A.3    Lennarz, W.J.4
  • 80
    • 24944478240 scopus 로고    scopus 로고
    • Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD
    • DOI 10.1016/j.molcel.2005.08.015, PII S1097276505015571
    • Szathmary R, Bielmann R, Nita-Lazar M, Burda P, Jakob CA (2005) Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol Cell 19:765-775 (Pubitemid 41316671)
    • (2005) Molecular Cell , vol.19 , Issue.6 , pp. 765-775
    • Szathmary, R.1    Bielmann, R.2    Nita-Lazar, M.3    Burda, P.4    Jakob, C.A.5
  • 82
    • 79960146847 scopus 로고    scopus 로고
    • Characterization of early EDEM1 protein maturation events and their functional implications
    • Tamura T, Cormier JH, Hebert DN (2011) Characterization of early EDEM1 protein maturation events and their functional implications. J Biol Chem 286:24906-24915
    • (2011) J Biol Chem , vol.286 , pp. 24906-24915
    • Tamura, T.1    Cormier, J.H.2    Hebert, D.N.3
  • 83
    • 0024318954 scopus 로고
    • Use of poly(vinylpyrrolidone) and poly(vinyl alcohol) for cryoultramicrotomy
    • Tokuyasu K (1989) Use of poly(vinylpyrrolidone) and poly(vinyl alcohol) for cryoultramicrotomy. Histochem J 21:163-171
    • (1989) Histochem J , vol.21 , pp. 163-171
    • Tokuyasu, K.1
  • 84
    • 0029809134 scopus 로고    scopus 로고
    • p62, a phosphotyrosine-independent ligand of the SH2 domain of p56(lck), belongs to a new class of ubiquitin-binding proteins
    • DOI 10.1074/jbc.271.34.20235
    • Vadlamudi RK, Joung I, Strominger JL, Shin J (1996) p62, a phos-photyrosine- independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins. J Biol Chem 271:20235-20237 (Pubitemid 26281785)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20235-20237
    • Vadlamudi, R.K.1    Joung, I.2    Strominger, J.L.3    Shin, J.4
  • 85
    • 79952319773 scopus 로고    scopus 로고
    • Mitochondria removal by autophagy
    • Wang K, Klionsky DJ (2011) Mitochondria removal by autophagy. Autophagy 7:297-300
    • (2011) Autophagy , vol.7 , pp. 297-300
    • Wang, K.1    Klionsky, D.J.2
  • 86
    • 79961142199 scopus 로고    scopus 로고
    • p62/SQSTM1 in autophagic clearance of a non-ubiquitylated substrate
    • Watanabe Y, Tanaka M (2011) p62/SQSTM1 in autophagic clearance of a non-ubiquitylated substrate. J Cell Sci 124:2692-2701
    • (2011) J Cell Sci , vol.124 , pp. 2692-2701
    • Watanabe, Y.1    Tanaka, M.2
  • 87
    • 20844458056 scopus 로고    scopus 로고
    • Chemistry and biology of wortmannin
    • DOI 10.1039/b504418a
    • Wipf P, Halter RJ (2005) Chemistry and biology of wortmannin. Org Biomol Chem 3:2053-2061 (Pubitemid 40859876)
    • (2005) Organic and Biomolecular Chemistry , vol.3 , Issue.11 , pp. 2053-2061
    • Wipf, P.1    Halter, R.J.2
  • 88
    • 80052716992 scopus 로고    scopus 로고
    • The ubiquitin clan: A protein family essential for life
    • Wolf DH (2011) The ubiquitin clan: a protein family essential for life. FEBS Lett 585:2769-2771
    • (2011) FEBS Lett , vol.585 , pp. 2769-2771
    • Wolf, D.H.1
  • 89
    • 84868227920 scopus 로고    scopus 로고
    • Integration of clearance mechanisms: The proteasome and autophagy
    • Morimoto RI, Selkoe DJ, Kelly JW (eds) Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Wong E, Cuervo AM (2012) Integration of clearance mechanisms: the proteasome and autophagy. In: Morimoto RI, Selkoe DJ, Kelly JW (eds) Protein homeostasis. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, pp 47-65
    • (2012) Protein Homeostasis , pp. 47-65
    • Wong, E.1    Cuervo, A.M.2
  • 90
    • 77951217000 scopus 로고    scopus 로고
    • Dual role of 3-methyladenine in modulation of autophagy via different temporal patterns of inhibition on class I and III phosphoinositide 3-kinase
    • Wu YT, Tan HL, Shui G, Bauvy C, Huang Q, Wenk MR, Ong CN, Codogno P, Shen HM (2010) Dual role of 3-methyladenine in modulation of autophagy via different temporal patterns of inhibition on class I and III phosphoinositide 3-kinase. J Biol Chem 285:10850-10861
    • (2010) J Biol Chem , vol.285 , pp. 10850-10861
    • Wu, Y.T.1    Tan, H.L.2    Shui, G.3    Bauvy, C.4    Huang, Q.5    Wenk, M.R.6    Ong, C.N.7    Codogno, P.8    Shen, H.M.9
  • 92
    • 72249117511 scopus 로고    scopus 로고
    • N-Glycosylation
    • Gabius H (ed) Wiley-VCH, Weinheim
    • Zuber C, Roth J (2009) N-Glycosylation. In: Gabius H (ed) The sugar code. Wiley-VCH, Weinheim, pp 87-110
    • (2009) The Sugar Code , pp. 87-110
    • Zuber, C.1    Roth, J.2
  • 93
    • 0033637519 scopus 로고    scopus 로고
    • Golgi apparatus immunolocalization of endomannosidase suggests post-endoplasmic reticulum glucose trimming: Implications for quality control
    • Zuber C, Spiro MJ, Guhl B, Spiro RG, Roth J (2000) Golgi apparatus immunolocalization of endomannosidase suggests post-endoplasmic reticulum glucose trimming: implications for quality control. Mol Biol Cell 11:4227-4240
    • (2000) Mol Biol Cell , vol.11 , pp. 4227-4240
    • Zuber, C.1    Spiro, M.J.2    Guhl, B.3    Spiro, R.G.4    Roth, J.5


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