메뉴 건너뛰기




Volumn 20, Issue 6, 2010, Pages 651-660

The role of MRH domain-containing lectins in ERAD

Author keywords

ERAD (ER associated protein degradation); Lectin; MRH domain; OS 9; XTP3 B

Indexed keywords

ERLECTIN; FUNGAL PROTEIN; GLUCOSIDASE; GLYCOPEPTIDASE; LECTIN; PROTEIN HRD1P; PROTEIN HRD3P; PROTEIN OS 9; PROTEIN XTP3 B; PROTEIN YOS9P; SOMATOMEDIN B; SOMATOMEDIN B RECEPTOR; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 77952849160     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwq013     Document Type: Review
Times cited : (66)

References (87)
  • 1
    • 58149336774 scopus 로고    scopus 로고
    • Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins
    • Alcock F, Swanton E. 2009. Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins. J Mol Biol. 385:1032-1042.
    • (2009) J Mol Biol , vol.385 , pp. 1032-1042
    • Alcock, F.1    Swanton, E.2
  • 2
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • Anelli T, Sitia R. 2008. Protein quality control in the early secretory pathway. Embo J. 27:315-327.
    • (2008) Embo J , vol.27 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 3
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
    • Appenzeller-Herzog C, Hauri HP. 2006. The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J Cell Sci. 119:2173-2183.
    • (2006) J Cell Sci , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 4
    • 38749122389 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation
    • 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.
    • (2008) Mol Biol Cell , vol.19 , pp. 216-225
    • Avezov, E.1    Frenkel, Z.2    Ehrlich, M.3    Herscovics, A.4    Lederkremer, G.Z.5
  • 5
    • 13944276440 scopus 로고    scopus 로고
    • OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha
    • Baek JH, Mahon PC, Oh J, Kelly B, Krishnamachary B, Pearson M, Chan DA, Giaccia AJ, Semenza GL. 2005. OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha. Mol Cell. 17:503-512.
    • (2005) Mol Cell , vol.17 , pp. 503-512
    • Baek, J.H.1    Mahon, P.C.2    Oh, J.3    Kelly, B.4    Krishnamachary, B.5    Pearson, M.6    Chan, D.A.7    Giaccia, A.J.8    Semenza, G.L.9
  • 6
    • 0029958044 scopus 로고    scopus 로고
    • Bovine UDP-N-acetyl-glucosamine:lysosomal-enzyme N-acetylglucosamine-1-phosphotransferase I. Purification and subunit structure
    • Bao M, Booth JL, Elmendorf BJ, Canfield WM. 1996. Bovine UDP-N-acetylglucosamine:lysosomal-enzyme N-acetyl-glucosamine-1-phosphotransferase. I. Purification and subunit structure. J Biol Chem. 271:31437-31445.
    • (1996) J Biol Chem , vol.271 , pp. 31437-31445
    • Bao, M.1    Booth, J.L.2    Elmendorf, B.J.3    Canfield, W.M.4
  • 7
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays NW, Gardner RG, Seelig LP, Joazeiro CA, Hampton RY. 2001. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol. 3:24-29.
    • (2001) Nat Cell Biol , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joazeiro, C.A.4    Hampton, R.Y.5
  • 8
    • 47749109897 scopus 로고    scopus 로고
    • 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
    • Bernasconi R, Pertel T, Luban J, Molinari M. 2008. A dual task for the Xbp1responsive OS-9 variants in the mammalian endoplasmic reticulum: inhibiting secretion of misfolded protein conformers and enhancing their disposal. J Biol Chem. 283:16446-16454.
    • (2008) J Biol Chem , vol.283 , pp. 16446-16454
    • Bernasconi, R.1    Pertel, T.2    Luban, J.3    Molinari, M.4
  • 9
    • 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
    • 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.
    • (2005) Mol Cell , vol.19 , pp. 741-751
    • Bhamidipati, A.1    Denic, V.2    Quan, E.M.3    Weissman, J.S.4
  • 10
    • 0032441479 scopus 로고    scopus 로고
    • Ubiquitin and the control of protein fate in the secretory and endocytic pathways
    • Bonifacino JS, Weissman AM. 1998. Ubiquitin and the control of protein fate in the secretory and endocytic pathways. Annu Rev Cell Dev Biol. 14:19-57.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 19-57
    • Bonifacino, J.S.1    Weissman, A.M.2
  • 11
    • 0033046227 scopus 로고    scopus 로고
    • Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases
    • Burda P, Jakob CA, Beinhauer J, Hegemann JH, Aebi M. 1999. Ordered assembly of the asymmetrically branched lipid-linked oligosaccharide in the endoplasmic reticulum is ensured by the substrate specificity of the individual glycosyltransferases. Glycobiology. 9:617-625.
    • (1999) Glycobiology , vol.9 , pp. 617-625
    • Burda, P.1    Jakob, C.A.2    Beinhauer, J.3    Hegemann, J.H.4    Aebi, M.5
  • 12
    • 8844270968 scopus 로고    scopus 로고
    • A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins
    • 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.
    • (2004) FEBS Lett , vol.577 , pp. 422-426
    • Buschhorn, B.A.1    Kostova, Z.2    Medicherla, B.3    Wolf, D.H.4
  • 13
    • 0035478934 scopus 로고    scopus 로고
    • Dissecting glycoprotein quality control in the secretory pathway
    • Cabral CM, Liu Y, Sifers RN. 2001. Dissecting glycoprotein quality control in the secretory pathway. Trends Biochem Sci. 26:619-624.
    • (2001) Trends Biochem Sci , vol.26 , pp. 619-624
    • Cabral, C.M.1    Liu, Y.2    Sifers, R.N.3
  • 14
    • 44849102178 scopus 로고    scopus 로고
    • Getting in and out from calnexin/calreticulin cycles
    • Caramelo JJ, Parodi AJ. 2008. Getting in and out from calnexin/calreticulin cycles. J Biol Chem. 283:10221-10225.
    • (2008) J Biol Chem , vol.283 , pp. 10221-10225
    • Caramelo, J.J.1    Parodi, A.J.2
  • 15
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
    • Carvalho P, Goder V, Rapoport TA. 2006. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell. 126: 361-373.
    • (2006) Cell , vol.126 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 16
    • 0042068176 scopus 로고    scopus 로고
    • Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p)
    • Chantret I, Frenoy JP, Moore SE. 2003. Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p). Biochem J. 373:901-908.
    • (2003) Biochem J , vol.373 , pp. 901-908
    • Chantret, I.1    Frenoy, J.P.2    Moore, S.E.3
  • 17
    • 40549122304 scopus 로고    scopus 로고
    • Free oligosaccharide regulation during mammalian protein N-glycosylation
    • Chantret I, Moore SE. 2008. Free oligosaccharide regulation during mammalian protein N-glycosylation. Glycobiology. 18:210-224.
    • (2008) Glycobiology , vol.18 , pp. 210-224
    • Chantret, I.1    Moore, S.E.2
  • 18
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson JC, Shaler TA, Tyler RE, Kopito RR. 2008. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol. 10:272-282.
    • (2008) Nat Cell Biol , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 19
    • 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
  • 20
    • 33744965386 scopus 로고    scopus 로고
    • The MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognition
    • Cruciat CM, Hassler C, Niehrs C. 2006. The MRH protein Erlectin is a member of the endoplasmic reticulum synexpression group and functions in N-glycan recognition. J Biol Chem. 281:12986-12993.
    • (2006) J Biol Chem , vol.281 , pp. 12986-12993
    • Cruciat, C.M.1    Hassler, C.2    Niehrs, C.3
  • 21
    • 0024364949 scopus 로고
    • Mannose 6-phosphate receptors and lysosomal enzyme targeting
    • Dahms NM, Lobel P, Kornfeld S. 1989. Mannose 6-phosphate receptors and lysosomal enzyme targeting. J Biol Chem. 264:12115-12118.
    • (1989) J Biol Chem , vol.264 , pp. 12115-12118
    • Dahms, N.M.1    Lobel, P.2    Kornfeld, S.3
  • 22
    • 58149107948 scopus 로고    scopus 로고
    • Strategies for carbohydrate recognition by the mannose 6-phosphate receptors
    • Dahms NM, Olson LJ, Kim JJ. 2008. Strategies for carbohydrate recognition by the mannose 6-phosphate receptors. Glycobiology. 18:664-678.
    • (2008) Glycobiology , vol.18 , pp. 664-678
    • Dahms, N.M.1    Olson, L.J.2    Kim, J.J.3
  • 23
    • 0035815754 scopus 로고    scopus 로고
    • Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation
    • Deak PM, Wolf DH. 2001. Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J Biol Chem. 276:10663-10669.
    • (2001) J Biol Chem , vol.276 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 24
    • 33746208871 scopus 로고    scopus 로고
    • A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation
    • Denic V, Quan EM, Weissman JS. 2006. A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell. 126:349-359.
    • (2006) Cell , vol.126 , pp. 349-359
    • Denic, V.1    Quan, E.M.2    Weissman, J.S.3
  • 25
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L, Helenius A. 2003. Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol. 4:181-191.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 26
    • 0027137885 scopus 로고
    • Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast
    • Finger A, Knop M, Wolf DH. 1993. Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Eur J Biochem. 218:565-574.
    • (1993) Eur J Biochem , vol.218 , pp. 565-574
    • Finger, A.1    Knop, M.2    Wolf, D.H.3
  • 27
    • 0037144427 scopus 로고    scopus 로고
    • YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins
    • Friedmann E, Salzberg Y, Weinberger A, Shaltiel S, Gerst JE. 2002. YOS9, the putative yeast homolog of a gene amplified in osteosarcomas, is involved in the endoplasmic reticulum (ER)-Golgi transport of GPI-anchored proteins. J Biol Chem. 277:35274-35281.
    • (2002) J Biol Chem , vol.277 , pp. 35274-35281
    • Friedmann, E.1    Salzberg, Y.2    Weinberger, A.3    Shaltiel, S.4    Gerst, J.E.5
  • 29
    • 33746587049 scopus 로고    scopus 로고
    • A complex of Yos9p and the HRD ligase integrates endoplasmic reticulum quality control into the degradation machinery
    • 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.
    • (2006) Nat Cell Biol , vol.8 , pp. 849-854
    • Gauss, R.1    Jarosch, E.2    Sommer, T.3    Hirsch, C.4
  • 30
    • 0037336348 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors: new twists in the tale
    • Ghosh P, Dahms NM, Kornfeld S. 2003. Mannose 6-phosphate receptors: new twists in the tale. Nat Rev Mol Cell Biol. 4:202-212.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 202-212
    • Ghosh, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 31
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C, Braakman I, Helenius A. 1994. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc Natl Acad Sci U S A. 91:913-917.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 32
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius A, Aebi M. 2001. Intracellular functions of N-linked glycans. Science. 291:2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 33
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A, Aebi M. 2004. Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem. 73:1019-1049.
    • (2004) Annu Rev Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 34
    • 0036019901 scopus 로고    scopus 로고
    • The specificity of the yeast and human class I ER alpha 1 2-mannosidases involved in ER quality control is not as strict previously reported
    • Herscovics A, Romero PA, Tremblay LO. 2002. The specificity of the yeast and human class I ER alpha 1, 2-mannosidases involved in ER quality control is not as strict previously reported. Glycobiology. 12:14G-15G.
    • (2002) Glycobiology , vol.12
    • Herscovics, A.1    Romero, P.A.2    Tremblay, L.O.3
  • 36
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • Hirsch C, Gauss R, Horn SC, Neuber O, Sommer T. 2009. The ubiquitylation machinery of the endoplasmic reticulum. Nature. 458:453-460.
    • (2009) Nature , vol.458 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4    Sommer, T.5
  • 37
    • 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
  • 39
    • 0037829617 scopus 로고    scopus 로고
    • Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I
    • Hosokawa N, Tremblay LO, You Z, Herscovics A, Wada I, Nagata K. 2003. Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I. J Biol Chem. 278:26287-26294.
    • (2003) J Biol Chem , vol.278 , pp. 26287-26294
    • Hosokawa, N.1    Tremblay, L.O.2    You, Z.3    Herscovics, A.4    Wada, I.5    Nagata, K.6
  • 40
    • 51049121849 scopus 로고    scopus 로고
    • Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP
    • 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.
    • (2008) J Biol Chem , vol.283 , pp. 20914-20924
    • Hosokawa, N.1    Wada, I.2    Nagasawa, K.3    Moriyama, T.4    Okawa, K.5    Nagata, K.6
  • 42
    • 25844454688 scopus 로고    scopus 로고
    • Structural approaches to the study of oligosaccharides in glycoprotein quality control
    • Ito Y, Hagihara S, Matsuo I, Totani K. 2005. Structural approaches to the study of oligosaccharides in glycoprotein quality control. Curr Opin Struct Biol. 15:481-489.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 481-489
    • Ito, Y.1    Hagihara, S.2    Matsuo, I.3    Totani, K.4
  • 43
    • 0032494135 scopus 로고    scopus 로고
    • Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
    • 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.
    • (1998) J Cell Biol , vol.142 , pp. 1223-1233
    • Jakob, C.A.1    Burda, P.2    Roth, J.3    Aebi, M.4
  • 44
    • 77749326886 scopus 로고    scopus 로고
    • Sophisticated modes of sugar recognition by intracellular lectins involved in quality control of glycoporteins
    • Powell G and McCabe O, editors. New York: Nova Science Publishers, Inc
    • Kamiya Y, Kamiya D, Urade R, Suzuki T, Kato K. 2009. Sophisticated modes of sugar recognition by intracellular lectins involved in quality control of glycoporteins. In: Powell G and McCabe O, editors. Glycobiology Research Trends. New York: Nova Science Publishers, Inc. p. 27-40.
    • (2009) Glycobiology Research Trends , pp. 27-40
    • Kamiya, Y.1    Kamiya, D.2    Urade, R.3    Suzuki, T.4    Kato, K.5
  • 45
    • 38349136210 scopus 로고    scopus 로고
    • Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36
    • 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.
    • (2008) J Biol Chem , vol.283 , pp. 1857-1861
    • Kamiya, Y.1    Kamiya, D.2    Yamamoto, K.3    Nyfeler, B.4    Hauri, H.P.5    Kato, K.6
  • 47
    • 36249014338 scopus 로고    scopus 로고
    • The EDEM and Yos9p families of lectin-like ERAD factors
    • Kanehara K, Kawaguchi S, Ng DT. 2007. The EDEM and Yos9p families of lectin-like ERAD factors. Semin Cell Dev Biol. 18:743-750.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 743-750
    • Kanehara, K.1    Kawaguchi, S.2    Ng, D.T.3
  • 48
    • 0022467156 scopus 로고
    • Frontal affinity chromatoraphy: theory for its application to studies on specofoc interactions of biomolecules
    • Kasai K, Oda Y, Nishikawa M, Ishii S. 1986. Frontal affinity chromatoraphy: theory for its application to studies on specofoc interactions of biomolecules. J Chromatogr. 376:33-47.
    • (1986) J Chromatogr , vol.376 , pp. 33-47
    • Kasai, K.1    Oda, Y.2    Nishikawa, M.3    Ishii, S.4
  • 49
    • 35048842895 scopus 로고    scopus 로고
    • Structural views of glycoprotein-fate determination in cells
    • Kato K, Kamiya Y. 2007. Structural views of glycoprotein-fate determination in cells. Glycobiology. 17:1031-1044.
    • (2007) Glycobiology , vol.17 , pp. 1031-1044
    • Kato, K.1    Kamiya, Y.2
  • 50
    • 70349882101 scopus 로고    scopus 로고
    • Carbohydrate recognition by the mannose-6-phosphate receptors
    • Kim JJ, Olson LJ, Dahms NM. 2009. Carbohydrate recognition by the mannose-6-phosphate receptors. Curr Opin Struct Biol. 19:534-542.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 534-542
    • Kim, J.J.1    Olson, L.J.2    Dahms, N.M.3
  • 51
    • 24944552879 scopus 로고    scopus 로고
    • Yos9p detects and targets misfolded glycoproteins for ER-associated degradation
    • Kim W, Spear ED, Ng DT. 2005. Yos9p detects and targets misfolded glycoproteins for ER-associated degradation. Mol Cell. 19:753-764.
    • (2005) Mol Cell , vol.19 , pp. 753-764
    • Kim, W.1    Spear, E.D.2    Ng, D.T.3
  • 53
    • 0031970586 scopus 로고    scopus 로고
    • Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines
    • Kimura Y, Nakazawa M, Yamada M. 1998. Cloning and characterization of three isoforms of OS-9 cDNA and expression of the OS-9 gene in various human tumor cell lines. J Biochem (Tokyo). 123:876-882.
    • (1998) J Biochem (Tokyo) , vol.123 , pp. 876-882
    • Kimura, Y.1    Nakazawa, M.2    Yamada, M.3
  • 54
    • 0029817714 scopus 로고    scopus 로고
    • N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast
    • Knop M, Hauser N, Wolf DH. 1996. N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast. 12:1229-1238.
    • (1996) Yeast , vol.12 , pp. 1229-1238
    • Knop, M.1    Hauser, N.2    Wolf, D.H.3
  • 55
    • 20444429745 scopus 로고    scopus 로고
    • A window of opportunity: timing protein degradation by trimming of sugars and ubiquitins
    • Lederkremer GZ, Glickman MH. 2005. A window of opportunity: timing protein degradation by trimming of sugars and ubiquitins. Trends Biochem Sci. 30:297-303.
    • (2005) Trends Biochem Sci , vol.30 , pp. 297-303
    • Lederkremer, G.Z.1    Glickman, M.H.2
  • 56
    • 34848903008 scopus 로고    scopus 로고
    • Murine UDPGlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase lacking the gamma-subunit retains substantial activity toward acid hydrolases
    • Lee WS, Payne BJ, Gelfman CM, Vogel P, Kornfeld S. 2007. Murine UDPGlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase lacking the gammasubunit retains substantial activity toward acid hydrolases. J Biol Chem. 282:27198-27203.
    • (2007) J Biol Chem , vol.282 , pp. 27198-27203
    • Lee, W.S.1    Payne, B.J.2    Gelfman, C.M.3    Vogel, P.4    Kornfeld, S.5
  • 57
    • 0037072881 scopus 로고    scopus 로고
    • A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta
    • Litovchick L, Friedmann E, Shaltiel S. 2002. A selective interaction between OS-9 and the carboxyl-terminal tail of meprin beta. J Biol Chem.277: 34413-34423.
    • (2002) J Biol Chem , vol.277 , pp. 34413-34423
    • Litovchick, L.1    Friedmann, E.2    Shaltiel, S.3
  • 58
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • Malhotra JD, Kaufman RJ. 2007. The endoplasmic reticulum and the unfolded protein response. Semin Cell Dev Biol. 18:716-731.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 59
    • 20444393746 scopus 로고    scopus 로고
    • Human EDEM2, a novel homolog of family 47 glycosidases, is involved in ER-associated degradation of glycoproteins
    • 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.
    • (2005) Glycobiology , vol.15 , pp. 421-436
    • Mast, S.W.1    Diekman, K.2    Karaveg, K.3    Davis, A.4    Sifers, R.N.5    Moremen, K.W.6
  • 60
    • 34248997838 scopus 로고    scopus 로고
    • N-glycan structure dictates extension of protein folding or onset of disposal
    • Molinari M. 2007. N-glycan structure dictates extension of protein folding or onset of disposal. Nat Chem Biol. 3:313-320.
    • (2007) Nat Chem Biol , vol.3 , pp. 313-320
    • Molinari, M.1
  • 61
    • 50449107542 scopus 로고    scopus 로고
    • SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins
    • 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 USA. 105:12325-12330.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 12325-12330
    • Mueller, B.1    Klemm, E.J.2    Spooner, E.3    Claessen, J.H.4    Ploegh, H.L.5
  • 62
    • 33750359201 scopus 로고    scopus 로고
    • SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER
    • Mueller B, Lilley BN, Ploegh HL. 2006. SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER. J Cell Biol. 175:261-270.
    • (2006) J Cell Biol , vol.175 , pp. 261-270
    • Mueller, B.1    Lilley, B.N.2    Ploegh, H.L.3
  • 63
    • 0035838410 scopus 로고    scopus 로고
    • The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins
    • Munro S. 2001. The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins. Curr Biol. 11:R499-501.
    • (2001) Curr Biol , vol.11
    • Munro, S.1
  • 64
    • 0032587825 scopus 로고    scopus 로고
    • Ca2(+)-dependent interaction of N-copine, a member of the two C2 domain protein family, with OS-9, the product of a gene frequently amplified in osteosarcoma
    • Nakayama T, Yaoi T, Kuwajima G, Yoshie O, Sakata T. 1999. Ca2(+)-dependent interaction of N-copine, a member of the two C2 domain protein family, with OS-9, the product of a gene frequently amplified in osteosarcoma. FEBS Lett. 453:77-80.
    • (1999) FEBS Lett , vol.453 , pp. 77-80
    • Nakayama, T.1    Yaoi, T.2    Kuwajima, G.3    Yoshie, O.4    Sakata, T.5
  • 65
    • 33748795800 scopus 로고    scopus 로고
    • EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation
    • 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.
    • (2006) Biochem Biophys Res Commun , vol.349 , pp. 1278-1284
    • Olivari, S.1    Cali, T.2    Salo, K.E.3    Paganetti, P.4    Ruddock, L.W.5    Molinari, M.6
  • 66
    • 34447512641 scopus 로고    scopus 로고
    • Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins
    • 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.
    • (2007) FEBS Lett , vol.581 , pp. 3658-3664
    • Olivari, S.1    Molinari, M.2
  • 67
    • 0025225456 scopus 로고
    • The retention signal for soluble proteins of the endoplasmic reticulum
    • Pelham HR. 1990. The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem Sci. 15:483-486.
    • (1990) Trends Biochem Sci , vol.15 , pp. 483-486
    • Pelham, H.R.1
  • 68
    • 0033492290 scopus 로고    scopus 로고
    • Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation
    • Plemper RK, Bordallo J, Deak PM, Taxis C, Hitt R, Wolf DH. 1999. Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation. J Cell Sci. 112(Pt 22): 4123-4134.
    • (1999) J Cell Sci , vol.112 , Issue.PT 22 , pp. 4123-4134
    • Plemper, R.K.1    Bordallo, J.2    Deak, P.M.3    Taxis, C.4    Hitt, R.5    Wolf, D.H.6
  • 69
  • 70
    • 36249022073 scopus 로고    scopus 로고
    • Ubiquitin receptors and ERAD: a network of pathways to the proteasome
    • Raasi S, Wolf DH. 2007. Ubiquitin receptors and ERAD: a network of pathways to the proteasome. Semin Cell Dev Biol. 18:780-791.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 780-791
    • Raasi, S.1    Wolf, D.H.2
  • 71
    • 0032524316 scopus 로고    scopus 로고
    • Molecular basis of lysosomal enzyme recognition: three-dimensional structure of the cation-dependent mannose 6-phosphate receptor
    • Roberts DL, Weix DJ, Dahms NM, Kim JJ. 1998. Molecular basis of lysosomal enzyme recognition: three-dimensional structure of the cation-dependent mannose 6-phosphate receptor. Cell. 93:639-648.
    • (1998) Cell , vol.93 , pp. 639-648
    • Roberts, D.L.1    Weix, D.J.2    Dahms, N.M.3    Kim, J.J.4
  • 72
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, Walter P. 2007. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol. 8:519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 73
    • 0024709671 scopus 로고
    • Isolation of cDNAs encoding a substrate for protein kinase C: nucleotide sequence and chromosomal mapping of the gene for a human 80K protein
    • Sakai K, Hirai M, Minoshima S, Kudoh J, Fukuyama R, Shimizu N. 1989. Isolation of cDNAs encoding a substrate for protein kinase C: nucleotide sequence and chromosomal mapping of the gene for a human 80K protein. Genomics. 5:309-315.
    • (1989) Genomics , vol.5 , pp. 309-315
    • Sakai, K.1    Hirai, M.2    Minoshima, S.3    Kudoh, J.4    Fukuyama, R.5    Shimizu, N.6
  • 76
    • 15844379850 scopus 로고    scopus 로고
    • Complete sequence analysis of a gene (OS-9) ubiquitously expressed in human tissues and amplified in sarcomas
    • Su YA, Hutter CM, Trent JM, Meltzer PS. 1996. Complete sequence analysis of a gene (OS-9) ubiquitously expressed in human tissues and amplified in sarcomas. Mol Carcinog. 15:270-275.
    • (1996) Mol Carcinog , vol.15 , pp. 270-275
    • Su, Y.A.1    Hutter, C.M.2    Trent, J.M.3    Meltzer, P.S.4
  • 77
    • 0028577893 scopus 로고
    • Direct isolation of genes encoded within a homogeneously staining region by chromosome microdissection
    • Su YA, Trent JM, Guan XY, Meltzer PS. 1994. Direct isolation of genes encoded within a homogeneously staining region by chromosome microdissection. Proc Natl Acad Sci U S A. 91:9121-9125.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9121-9125
    • Su, Y.A.1    Trent, J.M.2    Guan, X.Y.3    Meltzer, P.S.4
  • 78
    • 84863711034 scopus 로고    scopus 로고
    • Free N-linked oligosaccharide chains: formation and degradation
    • Suzuki T, Funakoshi Y. 2006. Free N-linked oligosaccharide chains: formation and degradation. Glycoconj J. 23:291-302.
    • (2006) Glycoconj J , vol.23 , pp. 291-302
    • Suzuki, T.1    Funakoshi, Y.2
  • 79
    • 24944478240 scopus 로고    scopus 로고
    • Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD
    • 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.
    • (2005) Mol Cell , vol.19 , pp. 765-775
    • Szathmary, R.1    Bielmann, R.2    Nita-Lazar, M.3    Burda, P.4    Jakob, C.A.5
  • 80
    • 0344393021 scopus 로고    scopus 로고
    • Quality control and protein folding in the secretory pathway
    • Trombetta ES, Parodi AJ. 2003. Quality control and protein folding in the secretory pathway. Annu Rev Cell Dev Biol. 19:649-676.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 649-676
    • Trombetta, E.S.1    Parodi, A.J.2
  • 81
    • 0029910144 scopus 로고    scopus 로고
    • Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit
    • Trombetta ES, Simons JF, Helenius A. 1996. Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J Biol Chem. 271:27509-27516.
    • (1996) J Biol Chem , vol.271 , pp. 27509-27516
    • Trombetta, E.S.1    Simons, J.F.2    Helenius, A.3
  • 82
    • 23744457478 scopus 로고    scopus 로고
    • Versatility of the endoplasmic reticulum protein folding factory
    • van Anken E, Braakman I. 2005. Versatility of the endoplasmic reticulum protein folding factory. Crit Rev Biochem Mol Biol. 40:191-228.
    • (2005) Crit Rev Biochem Mol Biol , vol.40 , pp. 191-228
    • van Anken, E.1    Braakman, I.2
  • 83
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulumassociated degradation
    • Vembar SS, Brodsky JL. 2008. One step at a time: endoplasmic reticulumassociated degradation. Nat Rev Mol Cell Biol. 9:944-957.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 84
    • 37549002929 scopus 로고    scopus 로고
    • OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum
    • Wang Y, Fu X, Gaiser S, Kottgen M, Kramer-Zucker A, Walz G, Wegierski T. 2007. OS-9 regulates the transit and polyubiquitination of TRPV4 in the endoplasmic reticulum. J Biol Chem. 282:36561-36570.
    • (2007) J Biol Chem , vol.282 , pp. 36561-36570
    • Wang, Y.1    Fu, X.2    Gaiser, S.3    Kottgen, M.4    Kramer-Zucker, A.5    Walz, G.6    Wegierski, T.7
  • 85
    • 0016836498 scopus 로고
    • Proteinase C (carboxypeptidase Y) mutant of yeast
    • Wolf DH, Fink GR. 1975. Proteinase C (carboxypeptidase Y) mutant of yeast. J Bacteriol. 123:1150-1156.
    • (1975) J Bacteriol , vol.123 , pp. 1150-1156
    • Wolf, D.H.1    Fink, G.R.2
  • 86
    • 67749101849 scopus 로고    scopus 로고
    • Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system
    • Xie W, Kanehara K, Sayeed A, Ng DT. 2009. Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system. Mol Biol Cell. 20:3317-3329.
    • (2009) Mol Biol Cell , vol.20 , pp. 3317-3329
    • Xie, W.1    Kanehara, K.2    Sayeed, A.3    Ng, D.T.4
  • 87
    • 33645108256 scopus 로고    scopus 로고
    • Structural diversity of cytosolic free oligosaccharides in the human hepatoma cell line
    • Yanagida K, Natsuka S, Hase S. 2006. Structural diversity of cytosolic free oligosaccharides in the human hepatoma cell line, HepG2. Glycobiology. 16:294-304
    • (2006) HepG2. Glycobiology. , vol.16 , pp. 294-304
    • Yanagida, K.1    Natsuka, S.2    Hase, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.