메뉴 건너뛰기




Volumn 9, Issue 2, 2014, Pages

Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA1,2 MANNOTRIOSE; CARGO RECEPTOR; ENDOPLASMIC RETICULUM GOLGI INTERMEDIATE COMPARTMENT PROTEIN 53; GLUCOSE; GLYCAN; GLYCOPROTEIN; LECTIN; MANNOSE; MULTICOAGULATION FACTOR DEFICIENCY 2; TRISACCHARIDE; UNCLASSIFIED DRUG; VIP36 PROTEIN;

EID: 84896861605     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0087963     Document Type: Article
Times cited : (29)

References (40)
  • 1
    • 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
  • 2
    • 35048842895 scopus 로고    scopus 로고
    • Structural views of glycoprotein-fate determination in cells
    • DOI 10.1093/glycob/cwm046
    • Kato K, Kamiya Y (2007) Structural views of glycoprotein-fate determination in cells. Glycobiology 17: 1031-1044. (Pubitemid 47553527)
    • (2007) Glycobiology , vol.17 , Issue.10 , pp. 1031-1044
    • Kato, K.1    Kamiya, Y.2
  • 3
    • 70349855203 scopus 로고    scopus 로고
    • Glycoprotein folding, quality control and ER-associated degradation
    • Lederkremer GZ (2009) Glycoprotein folding, quality control and ER-associated degradation. Curr Opin Struct Biol 19: 515-523.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 515-523
    • Lederkremer, G.Z.1
  • 4
    • 70549101180 scopus 로고    scopus 로고
    • Chemical approaches toward understanding glycan-mediated protein quality control
    • Takeda Y, Totani K, Matsuo I, Ito Y (2009) Chemical approaches toward understanding glycan-mediated protein quality control. Curr Opin Chem Biol 13: 582-591.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 582-591
    • Takeda, Y.1    Totani, K.2    Matsuo, I.3    Ito, Y.4
  • 6
    • 77952583769 scopus 로고    scopus 로고
    • UDP-GlC:Glycoprotein glucosyl-transferase-glucosidase II, the ying-yang of the ER quality control
    • D'Alessio C, Caramelo JJ, Parodi AJ (2010) UDP-GlC:glycoprotein glucosyl-transferase-glucosidase II, the ying-yang of the ER quality control. Semin Cell Dev Biol 21: 491-499.
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 491-499
    • D'Alessio, C.1    Caramelo, J.J.2    Parodi, A.J.3
  • 7
    • 84862851683 scopus 로고    scopus 로고
    • Molecular and structural basis for N-glycandependent determination of glycoprotein fates in cells
    • Kamiya Y, Satoh T, Kato K (2012) Molecular and structural basis for N-glycandependent determination of glycoprotein fates in cells. Biochim Biophys Acta 1820: 1327-1337.
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 1327-1337
    • Kamiya, Y.1    Satoh, T.2    Kato, K.3
  • 8
    • 0028209329 scopus 로고
    • VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells
    • Fiedler K, Parton RG, Kellner R, Etzold T, Simons K (1994) VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells. EMBO J 13: 1729-1740. (Pubitemid 24114725)
    • (1994) EMBO Journal , vol.13 , Issue.7 , pp. 1729-1740
    • Fiedler, K.1    Parton, R.G.2    Kellner, R.3    Etzold, T.4    Simons, K.5
  • 10
    • 0030042401 scopus 로고    scopus 로고
    • Structural basis of trimannoside recognition by concanavalin A
    • DOI 10.1074/jbc.271.2.972
    • Naismith JH, Field RA (1996) Structural basis of trimannoside recognition by concanavalin A. J Biol Chem 271: 972-976. (Pubitemid 26034954)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.2 , pp. 972-976
    • Naismith, J.H.1    Field, R.A.2
  • 11
    • 0033202958 scopus 로고    scopus 로고
    • The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
    • Appenzeller C, Andersson H, Kappeler F, Hauri HP (1999) The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Nat Cell Biol 1: 330-334. (Pubitemid 129493573)
    • (1999) Nature Cell Biology , vol.1 , Issue.6 , pp. 330-334
    • Appenzeller, C.1    Andersson, H.2    Kappeler, F.3    Hauri, H.-P.4
  • 13
    • 0033106137 scopus 로고    scopus 로고
    • Mapping of structural determinants for the oligomerization of p58, a lectin-like protein of the intermediate compartment and cis-Golgi
    • DOI 10.1046/j.1432-1327.1999.00158.x
    • Lahtinen U, Svensson K, Pettersson RF (1999) Mapping of structural determinants for the oligomerization of p58, a lectin-like protein of the intermediate compartment and cis-Golgi. Eur J Biochem 260: 392-397. (Pubitemid 29122534)
    • (1999) European Journal of Biochemistry , vol.260 , Issue.2 , pp. 392-397
    • Lahtinen, U.1    Svensson, K.2    Pettersson, R.F.3
  • 14
    • 21844438479 scopus 로고    scopus 로고
    • LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway
    • DOI 10.1074/jbc.M502160200
    • Zhang B, Kaufman RJ, Ginsburg D (2005) LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway. J Biol Chem 280: 25881-25886. (Pubitemid 40962299)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.27 , pp. 25881-25886
    • Zhang, B.1    Kaufman, R.J.2    Ginsburg, D.3
  • 15
    • 33749510461 scopus 로고    scopus 로고
    • Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex
    • DOI 10.1111/j.1600-0854.2006.00483.x
    • Nyfeler B, Zhang B, Ginsburg D, Kaufman RJ, Hauri HP (2006) Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex. Traffic 7: 1473-1481. (Pubitemid 44524520)
    • (2006) Traffic , vol.7 , Issue.11 , pp. 1473-1481
    • Nyfeler, B.1    Zhang, B.2    Ginsburg, D.3    Kaufman, R.J.4    Hauri, H.-P.5
  • 16
    • 61849174315 scopus 로고    scopus 로고
    • Recent developments in the understanding of the combined deficiency of FV and FVIII
    • Zhang B (2009) Recent developments in the understanding of the combined deficiency of FV and FVIII. Br J Haematol 145: 15-23.
    • (2009) Br J Haematol , vol.145 , pp. 15-23
    • Zhang, B.1
  • 17
    • 0032879945 scopus 로고    scopus 로고
    • VIP36 localisation to the early secretory pathway
    • Füllekrug J, Scheiffele P, Simons K (1999) VIP36 localisation to the early secretory pathway. J Cell Sci 112 (Pt 17): 2813-2821. (Pubitemid 29430027)
    • (1999) Journal of Cell Science , vol.112 , Issue.17 , pp. 2813-2821
    • Fullekrug, J.1    Scheiffele, P.2    Simons, K.3
  • 18
    • 77958122966 scopus 로고    scopus 로고
    • Role of the lectin VIP36 in post-ER quality control of human a1-antitrypsin
    • Reiterer V, Nyfeler B, Hauri HP (2010) Role of the lectin VIP36 in post-ER quality control of human a1-antitrypsin. Traffic 11: 1044-1055.
    • (2010) Traffic , vol.11 , pp. 1044-1055
    • Reiterer, V.1    Nyfeler, B.2    Hauri, H.P.3
  • 19
    • 83355163390 scopus 로고    scopus 로고
    • VIP36 protein is a target of ectodomain shedding and regulates phagocytosis in macrophage Raw 264.7 cells
    • Shirakabe K, Hattori S, Seiki M, Koyasu S, Okada Y (2011) VIP36 protein is a target of ectodomain shedding and regulates phagocytosis in macrophage Raw 264.7 cells. J Biol Chem 286: 43154-43163.
    • (2011) J Biol Chem , vol.286 , pp. 43154-43163
    • Shirakabe, K.1    Hattori, S.2    Seiki, M.3    Koyasu, S.4    Okada, Y.5
  • 20
    • 0013202445 scopus 로고    scopus 로고
    • Profile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum protein
    • DOI 10.1074/jbc.M211199200
    • Nufer O, Mitrovic S, Hauri HP (2003) Profile-based data base scanning for animal L-type lectins and characterization of VIPL, a novel VIP36-like endoplasmic reticulum protein. J Biol Chem 278: 15886-15896. (Pubitemid 36799704)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.18 , pp. 15886-15896
    • Nufer, O.1    Mitrovic, S.2    Hauri, H.-P.3
  • 22
    • 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, et al. (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
  • 23
    • 0023733211 scopus 로고
    • Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus
    • DOI 10.1083/jcb.107.5.1643
    • Schweizer A, Fransen JA, Bächi T, Ginsel L, Hauri HP (1988) Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus. J Cell Biol 107: 1643-1653. (Pubitemid 18263538)
    • (1988) Journal of Cell Biology , vol.107 , Issue.5 , pp. 1643-1653
    • Schweizer, A.1    Fransen, J.A.M.2    Bachi, T.3    Ginsel, L.4    Hauri, H.-P.5
  • 24
    • 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
  • 25
    • 84868583210 scopus 로고    scopus 로고
    • Subcellular localization of ERGIC-53 under endoplasmic reticulum stress condition
    • Qin SY, Kawasaki N, Hu D, Tozawa H, Matsumoto N, et al. (2012) Subcellular localization of ERGIC-53 under endoplasmic reticulum stress condition. Glycobiology 22: 1709-1720.
    • (2012) Glycobiology , vol.22 , pp. 1709-1720
    • Qin, S.Y.1    Kawasaki, N.2    Hu, D.3    Tozawa, H.4    Matsumoto, N.5
  • 26
    • 0344873595 scopus 로고    scopus 로고
    • The Crystal Structure of the Carbohydrate-recognition Domain of the Glycoprotein Sorting Receptor p58/ERGIC-53 Reveals an Unpredicted Metal-binding Site and Conformational Changes Associated with Calcium Ion Binding
    • DOI 10.1016/j.jmb.2003.10.031
    • Velloso LM, Svensson K, Pettersson RF, Lindqvist Y (2003) The crystal structure of the carbohydrate-recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-binding site and conformational changes associated with calcium ion binding. J Mol Biol 334: 845-851. (Pubitemid 37485674)
    • (2003) Journal of Molecular Biology , vol.334 , Issue.5 , pp. 845-851
    • Velloso, L.M.1    Svensson, K.2    Pettersson, R.F.3    Lindqvist, Y.4
  • 27
    • 0037013292 scopus 로고    scopus 로고
    • Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum
    • DOI 10.1074/jbc.M112098200
    • Velloso LM, Svensson K, Schneider G, Pettersson RF, Lindqvist Y (2002) Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum. J Biol Chem 277: 15979-15984. (Pubitemid 34967880)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.18 , pp. 15979-15984
    • Velloso, L.M.1    Svensson, K.2    Schneider, G.3    Pettersson, R.F.4    Lindqvist, Y.5
  • 28
    • 77749233842 scopus 로고    scopus 로고
    • Structural basis for the cooperative interplay between the two causative gene products of combined factor V and factor VIII deficiency
    • Nishio M, Kamiya Y, Mizushima T, Wakatsuki S, Sasakawa H, et al. (2010) Structural basis for the cooperative interplay between the two causative gene products of combined factor V and factor VIII deficiency. Proc Natl Acad Sci U S A 107: 4034-4039.
    • (2010) Proc Natl Acad Sci U S a , vol.107 , pp. 4034-4039
    • Nishio, M.1    Kamiya, Y.2    Mizushima, T.3    Wakatsuki, S.4    Sasakawa, H.5
  • 29
    • 76749118043 scopus 로고    scopus 로고
    • Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII
    • Wigren E, Bourhis JM, Kursula I, Guy JE, Lindqvist Y (2010) Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII. FEBS Lett 584: 878-882.
    • (2010) FEBS Lett , vol.584 , pp. 878-882
    • Wigren, E.1    Bourhis, J.M.2    Kursula, I.3    Guy, J.E.4    Lindqvist, Y.5
  • 31
    • 84880070996 scopus 로고    scopus 로고
    • Structural Characterization of Carbohydrate Binding by LMAN1 Protein Provides New Insight into the Endoplasmic Reticulum Export of Factors V (FV) and VIII (FVIII)
    • Zheng C, Page RC, Das V, Nix JC, Wigren E, et al. (2013) Structural Characterization of Carbohydrate Binding by LMAN1 Protein Provides New Insight into the Endoplasmic Reticulum Export of Factors V (FV) and VIII (FVIII). J Biol Chem 288: 20499-20509.
    • (2013) J Biol Chem , vol.288 , pp. 20499-20509
    • Zheng, C.1    Page, R.C.2    Das, V.3    Nix, J.C.4    Wigren, E.5
  • 33
    • 0029876344 scopus 로고    scopus 로고
    • ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins
    • Itin C, Roche AC, Monsigny M, Hauri HP (1996) ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins. Mol Biol Cell 7: 483-493. (Pubitemid 26090895)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.3 , pp. 483-493
    • Itin, C.1    Roche, A.-C.2    Monsigny, M.3    Hauri, H.-P.4
  • 34
    • 0032586737 scopus 로고    scopus 로고
    • Man a1-2 Man α-OMe-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition
    • DOI 10.1093/glycob/9.6.539
    • Moothoo DN, Canan B, Field RA, Naismith JH (1999) Man a1-2 Man α-O-Meconcanavalin A complex reveals a balance of forces involved in carbohydrate recognition. Glycobiology 9: 539-545. (Pubitemid 29250920)
    • (1999) Glycobiology , vol.9 , Issue.6 , pp. 539-545
    • Moothoo, D.N.1    Canan, B.2    Field, R.A.3    Naismith, J.H.4
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology 276: 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin A, Teplyakov A (1997) MOLREP: An automated program for molecular replacement. J Appl Crystallogr 30: 1022-1025. (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 40
    • 13244253766 scopus 로고    scopus 로고
    • pdb-care (PDB carbohydrate residue check): A program to support annotation of complex carbohydrate structures in PDB files
    • Lütteke T, von der Lieth CW (2004) pdb-care (PDB carbohydrate residue check): a program to support annotation of complex carbohydrate structures in PDB files. BMC Bioinformatics 5: 69.
    • (2004) BMC Bioinformatics , vol.5 , pp. 69
    • Lütteke, T.1    Von Der Lieth, C.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.