메뉴 건너뛰기




Volumn 19, Issue 6, 2018, Pages 463-480

More than just sugars: Conserved oligomeric Golgi complex deficiency causes glycosylation-independent cellular defects

Author keywords

cathepsin D; CDG; COG complex; COG CDG; endolysosome; GALE; glycosylation; Golgi; Lamp2; MGAT1

Indexed keywords

ALPHA 1,3 MANNOSYL GLYCOPROTEIN 2 BETA N ACETYLGLUCOSAMINYLTRANSFERASE; CATHEPSIN D; GLUCOSE REGULATED PROTEIN 78; N ACETYLGLUCOSAMINYLTRANSFERASE; SECRETORY PROTEIN; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSE 4 EPIMERASE; CARBOHYDRATE; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 85045948828     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/tra.12564     Document Type: Article
Times cited : (27)

References (91)
  • 1
    • 0037193464 scopus 로고    scopus 로고
    • Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function
    • Ungar D, Oka T, Brittle EE, et al. Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function. J Cell Biol. 2002;157(3):405-415.
    • (2002) J Cell Biol , vol.157 , Issue.3 , pp. 405-415
    • Ungar, D.1    Oka, T.2    Brittle, E.E.3
  • 2
    • 85046605729 scopus 로고    scopus 로고
    • Yeast COG complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNARES and with COPI vesicle coat proteins
    • Lupashin VV, Suvorova ES, Duden R. Yeast COG complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNARES and with COPI vesicle coat proteins. FEMS Congress of European Microbiologists Abstract Book. 2003.
    • (2003) FEMS Congress of European Microbiologists Abstract Book
    • Lupashin, V.V.1    Suvorova, E.S.2    Duden, R.3
  • 3
    • 85063599923 scopus 로고    scopus 로고
    • Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells
    • Zolov S, Lupashin V. Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells. Mol Biol Cell. 2004;15:460A-460A.
    • (2004) Mol Biol Cell , vol.15 , pp. 460A
    • Zolov, S.1    Lupashin, V.2
  • 4
    • 84887478931 scopus 로고    scopus 로고
    • The Golgi puppet master: COG complex at center stage of membrane trafficking interactions
    • Willett R, Ungar D, Lupashin V. The Golgi puppet master: COG complex at center stage of membrane trafficking interactions. Histochem Cell Biol. 2013;140(3):271-283.
    • (2013) Histochem Cell Biol , vol.140 , Issue.3 , pp. 271-283
    • Willett, R.1    Ungar, D.2    Lupashin, V.3
  • 5
    • 84924083459 scopus 로고    scopus 로고
    • Multipronged interaction of the COG complex with intracellular membranes
    • Willett R, Pokrovskaya I, Kudlyk T, Lupashin V. Multipronged interaction of the COG complex with intracellular membranes. Cell Logist. 2014;4(1):e27888.
    • (2014) Cell Logist , vol.4 , Issue.1
    • Willett, R.1    Pokrovskaya, I.2    Kudlyk, T.3    Lupashin, V.4
  • 6
    • 84979017473 scopus 로고    scopus 로고
    • COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe a sub-complex
    • Willett R, Blackburn JB, Climer L, et al. COG lobe B sub-complex engages v-SNARE GS15 and functions via regulated interaction with lobe a sub-complex. Sci Rep. 2016;6:29139.
    • (2016) Sci Rep , vol.6 , pp. 29139
    • Willett, R.1    Blackburn, J.B.2    Climer, L.3
  • 7
    • 0035489304 scopus 로고    scopus 로고
    • The SeC34/35 golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic
    • Whyte JRC, Munro S. The SeC34/35 golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic. Dev Cell. 2001;1(4):527-537.
    • (2001) Dev Cell , vol.1 , Issue.4 , pp. 527-537
    • Whyte, J.R.C.1    Munro, S.2
  • 8
    • 0035999979 scopus 로고    scopus 로고
    • Identification of Sec36p, Sec37p, and Sec38p: components of yeast complex that contains Sec34p and Sec35p
    • Ram RJ, Li BJ, Kaiser CA. Identification of Sec36p, Sec37p, and Sec38p: components of yeast complex that contains Sec34p and Sec35p. Mol Biol Cell. 2002;13(5):1484-1500.
    • (2002) Mol Biol Cell , vol.13 , Issue.5 , pp. 1484-1500
    • Ram, R.J.1    Li, B.J.2    Kaiser, C.A.3
  • 9
    • 0032491437 scopus 로고    scopus 로고
    • Purification and characterization of a novel 13 S hetero-oligomeric protein complex that stimulates in vitro Golgi transport
    • Walter DM, Paul KS, Waters MG. Purification and characterization of a novel 13 S hetero-oligomeric protein complex that stimulates in vitro Golgi transport. J Biol Chem. 1998;273(45):29565-29576.
    • (1998) J Biol Chem , vol.273 , Issue.45 , pp. 29565-29576
    • Walter, D.M.1    Paul, K.S.2    Waters, M.G.3
  • 10
    • 2442696341 scopus 로고    scopus 로고
    • Mutation of the COG complex subunit gene COG7 causes a lethal congenital disorder
    • Wu X, Steet RA, Bohorov O, et al. Mutation of the COG complex subunit gene COG7 causes a lethal congenital disorder. Nat Med. 2004;10(5):518-523.
    • (2004) Nat Med , vol.10 , Issue.5 , pp. 518-523
    • Wu, X.1    Steet, R.A.2    Bohorov, O.3
  • 11
    • 70349165974 scopus 로고    scopus 로고
    • COG defects, birth and rise!
    • Foulquier F. COG defects, birth and rise! Biochim Biophys Acta. 2009;1792(9):896-902.
    • (2009) Biochim Biophys Acta , vol.1792 , Issue.9 , pp. 896-902
    • Foulquier, F.1
  • 12
    • 84979048532 scopus 로고    scopus 로고
    • COG complex complexities: detailed characterization of a complete set of HEK293T cells lacking individual COG subunits
    • Bailey Blackburn J, Pokrovskaya I, Fisher P, Ungar D, Lupashin VV. COG complex complexities: detailed characterization of a complete set of HEK293T cells lacking individual COG subunits. Front Cell Dev Biol. 2016;4:23.
    • (2016) Front Cell Dev Biol , vol.4 , pp. 23
    • Bailey Blackburn, J.1    Pokrovskaya, I.2    Fisher, P.3    Ungar, D.4    Lupashin, V.V.5
  • 13
    • 81855168333 scopus 로고    scopus 로고
    • Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery
    • Pokrovskaya ID, Willett R, Smith RD, Morelle W, Kudlyk T, Lupashin VV. Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery. Glycobiology. 2011;21(12):1554-1569.
    • (2011) Glycobiology , vol.21 , Issue.12 , pp. 1554-1569
    • Pokrovskaya, I.D.1    Willett, R.2    Smith, R.D.3    Morelle, W.4    Kudlyk, T.5    Lupashin, V.V.6
  • 14
    • 34447330452 scopus 로고    scopus 로고
    • COG8 deficiency causes new congenital disorder of glycosylation type IIh
    • Kranz C, Ng BG, Sun L, et al. COG8 deficiency causes new congenital disorder of glycosylation type IIh. Hum Mol Genet. 2007;16(7):731-741.
    • (2007) Hum Mol Genet , vol.16 , Issue.7 , pp. 731-741
    • Kranz, C.1    Ng, B.G.2    Sun, L.3
  • 15
    • 70350690698 scopus 로고    scopus 로고
    • Deficiency in COG5 causes a moderate form of congenital disorders of glycosylation
    • Paesold-Burda P, Maag C, Troxler H, et al. Deficiency in COG5 causes a moderate form of congenital disorders of glycosylation. Hum Mol Genet. 2009;18(22):4350-4356.
    • (2009) Hum Mol Genet , vol.18 , Issue.22 , pp. 4350-4356
    • Paesold-Burda, P.1    Maag, C.2    Troxler, H.3
  • 16
    • 68749117665 scopus 로고    scopus 로고
    • Golgi function and dysfunction in the first COG4-deficient CDG type II patient
    • Reynders E, Foulquier F, Leao Teles E, et al. Golgi function and dysfunction in the first COG4-deficient CDG type II patient. Hum Mol Genet. 2009;18(17):3244-3256.
    • (2009) Hum Mol Genet , vol.18 , Issue.17 , pp. 3244-3256
    • Reynders, E.1    Foulquier, F.2    Leao Teles, E.3
  • 17
    • 77956096967 scopus 로고    scopus 로고
    • Fatal outcome due to deficiency of subunit 6 of the conserved oligomeric Golgi complex leading to a new type of congenital disorders of glycosylation
    • Lubbehusen J, Thiel C, Rind N, et al. Fatal outcome due to deficiency of subunit 6 of the conserved oligomeric Golgi complex leading to a new type of congenital disorders of glycosylation. Hum Mol Genet. 2010;19(18):3623-3633.
    • (2010) Hum Mol Genet , vol.19 , Issue.18 , pp. 3623-3633
    • Lubbehusen, J.1    Thiel, C.2    Rind, N.3
  • 18
    • 84926657074 scopus 로고    scopus 로고
    • Mutations in COG2 encoding a subunit of the conserved oligomeric Golgi complex cause a congenital disorder of glycosylation
    • Kodera H, Ando N, Yuasa I, et al. Mutations in COG2 encoding a subunit of the conserved oligomeric Golgi complex cause a congenital disorder of glycosylation. Clin Genet. 2015;87(5):455-460.
    • (2015) Clin Genet , vol.87 , Issue.5 , pp. 455-460
    • Kodera, H.1    Ando, N.2    Yuasa, I.3
  • 19
    • 33644853797 scopus 로고    scopus 로고
    • Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II
    • Foulquier F, Vasile E, Schollen E, et al. Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II. Proc Natl Acad Sci U S A. 2006;103(10):3764-3769.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , Issue.10 , pp. 3764-3769
    • Foulquier, F.1    Vasile, E.2    Schollen, E.3
  • 21
    • 84943345353 scopus 로고
    • Congenital disorders of N-linked glycosylation and multiple pathway overview
    • In, Adam MP, Ardinger HH, Pagon RA, eds., [Internet]., Seattle, WA, University of Washington, Seattle;, –2018. Available from
    • Sparks SE, Krasnewich DM. Congenital disorders of N-linked glycosylation and multiple pathway overview. In: Adam MP, Ardinger HH, Pagon RA, et al., eds. GeneReviews(R) [Internet]. Seattle, WA; University of Washington, Seattle; 1993–2018. Available from: https://www.ncbi.nlm.nih.gov/books/NBK1332/
    • (1993) GeneReviews(R)
    • Sparks, S.E.1    Krasnewich, D.M.2
  • 22
    • 84946559140 scopus 로고    scopus 로고
    • Defects in the COG complex and COG-related trafficking regulators affect neuronal Golgi function
    • Climer LK, Dobretsov M, Lupashin V. Defects in the COG complex and COG-related trafficking regulators affect neuronal Golgi function. Front Neurosci. 2015;9:405.
    • (2015) Front Neurosci , vol.9 , pp. 405
    • Climer, L.K.1    Dobretsov, M.2    Lupashin, V.3
  • 24
    • 36849029786 scopus 로고    scopus 로고
    • Deficiencies in subunits of the conserved oligomeric Golgi (COG) complex define a novel group of congenital disorders of glycosylation
    • Zeevaert R, Foulquier F, Jaeken J, Matthijs G. Deficiencies in subunits of the conserved oligomeric Golgi (COG) complex define a novel group of congenital disorders of glycosylation. Mol Genet Metab. 2008;93(1):15-21.
    • (2008) Mol Genet Metab , vol.93 , Issue.1 , pp. 15-21
    • Zeevaert, R.1    Foulquier, F.2    Jaeken, J.3    Matthijs, G.4
  • 25
    • 84979048532 scopus 로고    scopus 로고
    • COG complex complexities: detailed characterization of a complete set of HEK293T cells lacking individual COG subunits
    • Bailey Blackburn J, Pokrovskaya I, Fisher P, Ungar D, Lupashin V. COG complex complexities: detailed characterization of a complete set of HEK293T cells lacking individual COG subunits. Front Cell Dev Biol. 2016;4:23.
    • (2016) Front Cell Dev Biol , vol.4 , pp. 23
    • Bailey Blackburn, J.1    Pokrovskaya, I.2    Fisher, P.3    Ungar, D.4    Lupashin, V.5
  • 26
    • 78650657539 scopus 로고    scopus 로고
    • Cog2 null mutant CHO cells show defective sphingomyelin synthesis
    • Spessott W, Uliana A, Maccioni HJ. Cog2 null mutant CHO cells show defective sphingomyelin synthesis. J Biol Chem. 2010;285(53):41472-41482.
    • (2010) J Biol Chem , vol.285 , Issue.53 , pp. 41472-41482
    • Spessott, W.1    Uliana, A.2    Maccioni, H.J.3
  • 27
    • 0028027799 scopus 로고
    • LDLC encodes a brefeldin A-sensitive, peripheral Golgi protein required for normal Golgi function
    • Podos SD, Reddy P, Ashkenas J, Krieger M. LDLC encodes a brefeldin A-sensitive, peripheral Golgi protein required for normal Golgi function. J Cell Biol. 1994;127(3):679-691.
    • (1994) J Cell Biol , vol.127 , Issue.3 , pp. 679-691
    • Podos, S.D.1    Reddy, P.2    Ashkenas, J.3    Krieger, M.4
  • 28
    • 33745372525 scopus 로고    scopus 로고
    • COG-7-deficient human fibroblasts exhibit altered recycling of Golgi proteins
    • Steet R, Kornfeld S. COG-7-deficient human fibroblasts exhibit altered recycling of Golgi proteins. Mol Biol Cell. 2006;17(5):2312-2321.
    • (2006) Mol Biol Cell , vol.17 , Issue.5 , pp. 2312-2321
    • Steet, R.1    Kornfeld, S.2
  • 29
    • 0024408670 scopus 로고
    • Transfection of a human gene that corrects the Lec1 glycosylation defect: evidence for transfer of the structural gene for N-acetylglucosaminyltransferase I
    • Kumar R, Stanley P. Transfection of a human gene that corrects the Lec1 glycosylation defect: evidence for transfer of the structural gene for N-acetylglucosaminyltransferase I. Mol Cell Biol. 1989;9(12):5713-5717.
    • (1989) Mol Cell Biol , vol.9 , Issue.12 , pp. 5713-5717
    • Kumar, R.1    Stanley, P.2
  • 30
    • 0037234471 scopus 로고    scopus 로고
    • Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I
    • Chen W, Stanley P. Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I. Glycobiology. 2003;13(1):43-50.
    • (2003) Glycobiology , vol.13 , Issue.1 , pp. 43-50
    • Chen, W.1    Stanley, P.2
  • 31
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG. Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc Natl Acad Sci U S A. 2002;99(21):13419-13424.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.21 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 32
    • 7644233735 scopus 로고    scopus 로고
    • Inactivation of the Mgat1 gene in oocytes impairs oogenesis, but embryos lacking complex and hybrid N-glycans develop and implant
    • Shi S, Williams SA, Seppo A, et al. Inactivation of the Mgat1 gene in oocytes impairs oogenesis, but embryos lacking complex and hybrid N-glycans develop and implant. Mol Cell Biol. 2004;24(22):9920-9929.
    • (2004) Mol Cell Biol , vol.24 , Issue.22 , pp. 9920-9929
    • Shi, S.1    Williams, S.A.2    Seppo, A.3
  • 33
    • 0025148186 scopus 로고
    • Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38)
    • Luzio JP, Brake B, Banting G, Howell KE, Braghetta P, Stanley KK. Identification, sequencing and expression of an integral membrane protein of the trans-Golgi network (TGN38). Biochem J. 1990;270(1):97-102.
    • (1990) Biochem J , vol.270 , Issue.1 , pp. 97-102
    • Luzio, J.P.1    Brake, B.2    Banting, G.3    Howell, K.E.4    Braghetta, P.5    Stanley, K.K.6
  • 34
    • 3042721973 scopus 로고    scopus 로고
    • N-Glycan branching requirement in neuronal and postnatal viability
    • Ye Z, Marth JD. N-Glycan branching requirement in neuronal and postnatal viability. Glycobiology. 2004;14(6):547-558.
    • (2004) Glycobiology , vol.14 , Issue.6 , pp. 547-558
    • Ye, Z.1    Marth, J.D.2
  • 35
    • 0021126647 scopus 로고
    • Receptor-mediated endocytosis of low density lipoprotein: somatic cell mutants define multiple genes required for expression of surface- receptor activity
    • Kingsley DM, Krieger M. Receptor-mediated endocytosis of low density lipoprotein: somatic cell mutants define multiple genes required for expression of surface- receptor activity. Proc Natl Acad Sci U S A. 1984;81(17):5454-5458.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , Issue.17 , pp. 5454-5458
    • Kingsley, D.M.1    Krieger, M.2
  • 36
    • 0022527678 scopus 로고
    • Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-gal/UDP-GalNAc 4-epimerase deficient mutant
    • Kingsley DM, Kozarsky KF, Hobbie L, Krieger M. Reversible defects in O-linked glycosylation and LDL receptor expression in a UDP-gal/UDP-GalNAc 4-epimerase deficient mutant. Cell. 1986;44(5):749-759.
    • (1986) Cell , vol.44 , Issue.5 , pp. 749-759
    • Kingsley, D.M.1    Kozarsky, K.F.2    Hobbie, L.3    Krieger, M.4
  • 37
    • 0022455528 scopus 로고
    • Three types of low density lipoprotein receptor-deficient mutant have pleiotropic defects in the synthesis of N-linked, O-linked, and lipid-linked carbohydrate chains
    • Kingsley DM, Kozarsky KF, Segal M, Krieger M. Three types of low density lipoprotein receptor-deficient mutant have pleiotropic defects in the synthesis of N-linked, O-linked, and lipid-linked carbohydrate chains. J Cell Biol. 1986;102(5):1576-1585.
    • (1986) J Cell Biol , vol.102 , Issue.5 , pp. 1576-1585
    • Kingsley, D.M.1    Kozarsky, K.F.2    Segal, M.3    Krieger, M.4
  • 38
    • 0037071543 scopus 로고    scopus 로고
    • The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins
    • Suvorova ES, Duden R, Lupashin VV. The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins. J Cell Biol. 2002;157(4):631-643.
    • (2002) J Cell Biol , vol.157 , Issue.4 , pp. 631-643
    • Suvorova, E.S.1    Duden, R.2    Lupashin, V.V.3
  • 39
    • 14744272136 scopus 로고    scopus 로고
    • Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells
    • Zolov SN, Lupashin VV. Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells. J Cell Biol. 2005;168(5):747-759.
    • (2005) J Cell Biol , vol.168 , Issue.5 , pp. 747-759
    • Zolov, S.N.1    Lupashin, V.V.2
  • 40
    • 33645131266 scopus 로고    scopus 로고
    • COG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylation
    • Shestakova A, Zolov S, Lupashin V. COG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylation. Traffic. 2006;7(2):191-204.
    • (2006) Traffic , vol.7 , Issue.2 , pp. 191-204
    • Shestakova, A.1    Zolov, S.2    Lupashin, V.3
  • 41
    • 45049084097 scopus 로고    scopus 로고
    • Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation
    • Smith RD, Lupashin VV. Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation. Carbohydr Res. 2008;343(12):2024-2031.
    • (2008) Carbohydr Res , vol.343 , Issue.12 , pp. 2024-2031
    • Smith, R.D.1    Lupashin, V.V.2
  • 42
    • 69449100200 scopus 로고    scopus 로고
    • Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene
    • Richardson BC, Smith RD, Ungar D, et al. Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene. Proc Natl Acad Sci U S A. 2009;106(32):13329-13334.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.32 , pp. 13329-13334
    • Richardson, B.C.1    Smith, R.D.2    Ungar, D.3
  • 43
    • 85014847875 scopus 로고    scopus 로고
    • Bridging the gap between glycosylation and vesicle traffic
    • Fisher P, Ungar D. Bridging the gap between glycosylation and vesicle traffic. Front Cell Dev Biol. 2016;4:15.
    • (2016) Front Cell Dev Biol , vol.4 , pp. 15
    • Fisher, P.1    Ungar, D.2
  • 44
    • 79958798009 scopus 로고    scopus 로고
    • How Golgi glycosylation meets and needs trafficking: the case of the COG complex
    • Reynders E, Foulquier F, Annaert W, Matthijs G. How Golgi glycosylation meets and needs trafficking: the case of the COG complex. Glycobiology. 2011;21(7):853-863.
    • (2011) Glycobiology , vol.21 , Issue.7 , pp. 853-863
    • Reynders, E.1    Foulquier, F.2    Annaert, W.3    Matthijs, G.4
  • 46
    • 25444466999 scopus 로고    scopus 로고
    • Genetic analysis of the subunit organization and function of the conserved oligomeric Golgi (COG) complex: studies of COG5- and COG7-deficient mammalian cells
    • Oka T, Vasile E, Penman M, et al. Genetic analysis of the subunit organization and function of the conserved oligomeric Golgi (COG) complex: studies of COG5- and COG7-deficient mammalian cells. J Biol Chem. 2005;280(38):32736-32745.
    • (2005) J Biol Chem , vol.280 , Issue.38 , pp. 32736-32745
    • Oka, T.1    Vasile, E.2    Penman, M.3
  • 47
    • 84874817783 scopus 로고    scopus 로고
    • Mucin-type O-glycosylation during development
    • Tran DT, Ten Hagen KG. Mucin-type O-glycosylation during development. J Biol Chem. 2013;288(10):6921-6929.
    • (2013) J Biol Chem , vol.288 , Issue.10 , pp. 6921-6929
    • Tran, D.T.1    Ten Hagen, K.G.2
  • 48
    • 0000318091 scopus 로고
    • Purification and characterization of Griffonia simplicifolia leaf lectins
    • Lamb JE, Shibata S, Goldstein IJ. Purification and characterization of Griffonia simplicifolia leaf lectins. Plant Physiol. 1983;71(4):879-887.
    • (1983) Plant Physiol , vol.71 , Issue.4 , pp. 879-887
    • Lamb, J.E.1    Shibata, S.2    Goldstein, I.J.3
  • 49
    • 0022337371 scopus 로고
    • Lectin binding affinities of induced pancreatic lesions in the hamster model
    • Pour PM, Burnett D, Uchida E. Lectin binding affinities of induced pancreatic lesions in the hamster model. Carcinogenesis. 1985;6(12):1775-1780.
    • (1985) Carcinogenesis , vol.6 , Issue.12 , pp. 1775-1780
    • Pour, P.M.1    Burnett, D.2    Uchida, E.3
  • 50
    • 0023278648 scopus 로고
    • Helix pomatia and Ulex europeus lectin binding in human breast carcinoma
    • Fenlon S, Ellis IO, Bell J, Todd JH, Elston CW, Blamey RW. Helix pomatia and Ulex europeus lectin binding in human breast carcinoma. J Pathol. 1987;152(3):169-176.
    • (1987) J Pathol , vol.152 , Issue.3 , pp. 169-176
    • Fenlon, S.1    Ellis, I.O.2    Bell, J.3    Todd, J.H.4    Elston, C.W.5    Blamey, R.W.6
  • 51
    • 0026337287 scopus 로고
    • Helix pomatia agglutinin binding activity is a predictor of survival time for patients with gastric carcinoma
    • Kakeji Y, Tsujitani S, Mori M, Maehara Y, Sugimachi K. Helix pomatia agglutinin binding activity is a predictor of survival time for patients with gastric carcinoma. Cancer. 1991;68(11):2438-2442.
    • (1991) Cancer , vol.68 , Issue.11 , pp. 2438-2442
    • Kakeji, Y.1    Tsujitani, S.2    Mori, M.3    Maehara, Y.4    Sugimachi, K.5
  • 52
    • 0028072327 scopus 로고
    • Helix pomatia agglutinin binding is a useful prognostic indicator in colorectal carcinoma
    • Schumacher U, Higgs D, Loizidou M, Pickering R, Leathem A, Taylor I. Helix pomatia agglutinin binding is a useful prognostic indicator in colorectal carcinoma. Cancer. 1994;74(12):3104-3107.
    • (1994) Cancer , vol.74 , Issue.12 , pp. 3104-3107
    • Schumacher, U.1    Higgs, D.2    Loizidou, M.3    Pickering, R.4    Leathem, A.5    Taylor, I.6
  • 53
    • 35148865171 scopus 로고    scopus 로고
    • Structural basis for recognition of breast and colon cancer epitopes Tn antigen and Forssman disaccharide by helix pomatia lectin
    • Lescar J, Sanchez JF, Audfray A, et al. Structural basis for recognition of breast and colon cancer epitopes Tn antigen and Forssman disaccharide by helix pomatia lectin. Glycobiology. 2007;17(10):1077-1083.
    • (2007) Glycobiology , vol.17 , Issue.10 , pp. 1077-1083
    • Lescar, J.1    Sanchez, J.F.2    Audfray, A.3
  • 54
    • 2342467375 scopus 로고    scopus 로고
    • The COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteins
    • Oka T, Ungar D, Hughson FM, Krieger M. The COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteins. Mol Biol Cell. 2004;15(5):2423-2435.
    • (2004) Mol Biol Cell , vol.15 , Issue.5 , pp. 2423-2435
    • Oka, T.1    Ungar, D.2    Hughson, F.M.3    Krieger, M.4
  • 55
    • 70350378203 scopus 로고    scopus 로고
    • The COG complex, Rab6 and COPI define a novel Golgi retrograde trafficking pathway that is exploited by SubAB toxin
    • Smith RD, Willett R, Kudlyk T, et al. The COG complex, Rab6 and COPI define a novel Golgi retrograde trafficking pathway that is exploited by SubAB toxin. Traffic. 2009;10(10):1502-1517.
    • (2009) Traffic , vol.10 , Issue.10 , pp. 1502-1517
    • Smith, R.D.1    Willett, R.2    Kudlyk, T.3
  • 56
    • 80052572363 scopus 로고    scopus 로고
    • The COG complex interacts directly with Syntaxin 6 and positively regulates endosome-to-TGN retrograde transport
    • Laufman O, Hong W, Lev S. The COG complex interacts directly with Syntaxin 6 and positively regulates endosome-to-TGN retrograde transport. J Cell Biol. 2011;194(3):459-472.
    • (2011) J Cell Biol , vol.194 , Issue.3 , pp. 459-472
    • Laufman, O.1    Hong, W.2    Lev, S.3
  • 57
    • 84872045592 scopus 로고    scopus 로고
    • COG6 interacts with a subset of the Golgi SNAREs and is important for the Golgi complex integrity
    • Kudlyk T, Willett R, Pokrovskaya ID, Lupashin V. COG6 interacts with a subset of the Golgi SNAREs and is important for the Golgi complex integrity. Traffic. 2013;14(2):194-204.
    • (2013) Traffic , vol.14 , Issue.2 , pp. 194-204
    • Kudlyk, T.1    Willett, R.2    Pokrovskaya, I.D.3    Lupashin, V.4
  • 58
    • 34249730324 scopus 로고    scopus 로고
    • A new inborn error of glycosylation due to a Cog8 deficiency reveals a critical role for the Cog1-Cog8 interaction in COG complex formation
    • Foulquier F, Ungar D, Reynders E, et al. A new inborn error of glycosylation due to a Cog8 deficiency reveals a critical role for the Cog1-Cog8 interaction in COG complex formation. Hum Mol Genet. 2007;16(7):717-730.
    • (2007) Hum Mol Genet , vol.16 , Issue.7 , pp. 717-730
    • Foulquier, F.1    Ungar, D.2    Reynders, E.3
  • 59
    • 48749111661 scopus 로고    scopus 로고
    • Requirement of the human GARP complex for mannose 6-phosphate-receptor-dependent sorting of Cathepsin D to lysosomes
    • Perez-Victoria FJ, Mardones GA, Bonifacino JS. Requirement of the human GARP complex for mannose 6-phosphate-receptor-dependent sorting of Cathepsin D to lysosomes. Mol Biol Cell. 2008;19(6):2350-2362.
    • (2008) Mol Biol Cell , vol.19 , Issue.6 , pp. 2350-2362
    • Perez-Victoria, F.J.1    Mardones, G.A.2    Bonifacino, J.S.3
  • 60
    • 84983358990 scopus 로고    scopus 로고
    • 2+ -dependent Cab45 oligomerization at the trans-Golgi network
    • 2+ -dependent Cab45 oligomerization at the trans-Golgi network. J Cell Biol. 2016;213(3):305-314.
    • (2016) J Cell Biol , vol.213 , Issue.3 , pp. 305-314
    • Crevenna, A.H.1    Blank, B.2    Maiser, A.3
  • 61
    • 34248657552 scopus 로고    scopus 로고
    • Molecular and clinical characterization of a Moroccan Cog7 deficient patient
    • Ng BG, Kranz C, Hagebeuk EE, et al. Molecular and clinical characterization of a Moroccan Cog7 deficient patient. Mol Genet Metab. 2007;91(2):201-204.
    • (2007) Mol Genet Metab , vol.91 , Issue.2 , pp. 201-204
    • Ng, B.G.1    Kranz, C.2    Hagebeuk, E.E.3
  • 62
    • 2342467375 scopus 로고    scopus 로고
    • The COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteins
    • Oka T, Ungar D, Hughson FM, Krieger M. The COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteins. Mol Biol Cell. 2004;15(5):2423-2435.
    • (2004) Mol Biol Cell , vol.15 , Issue.5 , pp. 2423-2435
    • Oka, T.1    Ungar, D.2    Hughson, F.M.3    Krieger, M.4
  • 63
    • 84982792097 scopus 로고    scopus 로고
    • Arabidopsis COG complex subunits COG3 and COG8 modulate Golgi morphology, vesicle trafficking homeostasis and are essential for pollen tube growth
    • Tan X, Cao K, Liu F, et al. Arabidopsis COG complex subunits COG3 and COG8 modulate Golgi morphology, vesicle trafficking homeostasis and are essential for pollen tube growth. PLoS Genet. 2016;12(7):e1006140.
    • (2016) PLoS Genet , vol.12 , Issue.7
    • Tan, X.1    Cao, K.2    Liu, F.3
  • 64
    • 85032803343 scopus 로고    scopus 로고
    • COG7 deficiency in drosophila generates multifaceted developmental, behavioral and protein glycosylation phenotypes
    • Frappaolo A, Sechi S, Kumagai T, et al. COG7 deficiency in drosophila generates multifaceted developmental, behavioral and protein glycosylation phenotypes. J Cell Sci. 2017;130(21):3637-3649.
    • (2017) J Cell Sci , vol.130 , Issue.21 , pp. 3637-3649
    • Frappaolo, A.1    Sechi, S.2    Kumagai, T.3
  • 65
    • 78349291116 scopus 로고    scopus 로고
    • Interaction of Golgin-84 with the COG complex mediates the intra-Golgi retrograde transport
    • Sohda M, Misumi Y, Yamamoto A, et al. Interaction of Golgin-84 with the COG complex mediates the intra-Golgi retrograde transport. Traffic. 2010;11(12):1552-1566.
    • (2010) Traffic , vol.11 , Issue.12 , pp. 1552-1566
    • Sohda, M.1    Misumi, Y.2    Yamamoto, A.3
  • 66
    • 34247482798 scopus 로고    scopus 로고
    • The interaction of two tethering factors, p115 and COG complex, is required for Golgi integrity
    • Sohda M, Misumi Y, Yoshimura S, et al. The interaction of two tethering factors, p115 and COG complex, is required for Golgi integrity. Traffic. 2007;8(3):270-284.
    • (2007) Traffic , vol.8 , Issue.3 , pp. 270-284
    • Sohda, M.1    Misumi, Y.2    Yoshimura, S.3
  • 67
    • 78651310761 scopus 로고    scopus 로고
    • Defective GM3 synthesis in Cog2 null mutant CHO cells associates to mislocalization of lactosylceramide sialyltransferase in the Golgi complex
    • Spessott W, Uliana A, Maccioni HJ. Defective GM3 synthesis in Cog2 null mutant CHO cells associates to mislocalization of lactosylceramide sialyltransferase in the Golgi complex. Neurochem Res. 2010;35(12):2161-2167.
    • (2010) Neurochem Res , vol.35 , Issue.12 , pp. 2161-2167
    • Spessott, W.1    Uliana, A.2    Maccioni, H.J.3
  • 68
    • 0032544440 scopus 로고    scopus 로고
    • Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis
    • Lowe M, Rabouille C, Nakamura N, et al. Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis. Cell. 1998;94(6):783-793.
    • (1998) Cell , vol.94 , Issue.6 , pp. 783-793
    • Lowe, M.1    Rabouille, C.2    Nakamura, N.3
  • 69
    • 85032450378 scopus 로고    scopus 로고
    • The function of the Golgi ribbon structure – an enduring mystery unfolds!
    • Gosavi P, Gleeson PA. The function of the Golgi ribbon structure – an enduring mystery unfolds! BioEssays. 2017;39(11):1700063.
    • (2017) BioEssays , vol.39 , Issue.11 , pp. 1700063
    • Gosavi, P.1    Gleeson, P.A.2
  • 70
    • 84946571044 scopus 로고    scopus 로고
    • The GOLPH3 pathway regulates Golgi shape and function and is activated by DNA damage
    • Buschman MD, Xing M, Field SJ. The GOLPH3 pathway regulates Golgi shape and function and is activated by DNA damage. Front Neurosci. 2015;9:362.
    • (2015) Front Neurosci , vol.9 , pp. 362
    • Buschman, M.D.1    Xing, M.2    Field, S.J.3
  • 71
    • 59649092835 scopus 로고    scopus 로고
    • Chlamydia causes fragmentation of the Golgi compartment to ensure reproduction
    • Heuer D, Lipinski AR, Machuy N, et al. Chlamydia causes fragmentation of the Golgi compartment to ensure reproduction. Nature. 2008;457:731.
    • (2008) Nature , vol.457 , pp. 731
    • Heuer, D.1    Lipinski, A.R.2    Machuy, N.3
  • 72
    • 33744531110 scopus 로고    scopus 로고
    • Fragmentation of the Golgi apparatus in neurodegenerative diseases and cell death
    • Gonatas NK, Stieber A, Gonatas JO. Fragmentation of the Golgi apparatus in neurodegenerative diseases and cell death. J Neurol Sci. 2006;246(1):21-30.
    • (2006) J Neurol Sci , vol.246 , Issue.1 , pp. 21-30
    • Gonatas, N.K.1    Stieber, A.2    Gonatas, J.O.3
  • 73
    • 85016972374 scopus 로고    scopus 로고
    • Golgi ribbon disassembly during mitosis, differentiation and disease progression
    • Wei J-H, Seemann J. Golgi ribbon disassembly during mitosis, differentiation and disease progression. Curr Opin Cell Biol. 2017;47:43-51.
    • (2017) Curr Opin Cell Biol , vol.47 , pp. 43-51
    • Wei, J.-H.1    Seemann, J.2
  • 74
    • 84999514935 scopus 로고    scopus 로고
    • Onco-Golgi: is fragmentation a gate to cancer progression?
    • Petrosyan A. Onco-Golgi: is fragmentation a gate to cancer progression? Biochem Mol Biol J. 2015;1(1):16.
    • (2015) Biochem Mol Biol J , vol.1 , Issue.1 , pp. 16
    • Petrosyan, A.1
  • 75
    • 84954490786 scopus 로고    scopus 로고
    • Golgi fragmentation in ALS motor neurons. New mechanisms targeting microtubules, tethers, and transport vesicles
    • Haase G, Rabouille C. Golgi fragmentation in ALS motor neurons. New mechanisms targeting microtubules, tethers, and transport vesicles. Front Neurosci. 2015;9:448.
    • (2015) Front Neurosci , vol.9 , pp. 448
    • Haase, G.1    Rabouille, C.2
  • 76
    • 0037051978 scopus 로고    scopus 로고
    • Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra-Golgi pH
    • Kellokumpu S, Sormunen R, Kellokumpu I. Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra-Golgi pH. FEBS Lett. 2002;516(1–3):217-224.
    • (2002) FEBS Lett , vol.516 , Issue.1–3 , pp. 217-224
    • Kellokumpu, S.1    Sormunen, R.2    Kellokumpu, I.3
  • 77
    • 77956492133 scopus 로고    scopus 로고
    • The SPCA1 Ca2+ pump and intracellular membrane trafficking
    • Micaroni M, Perinetti G, Berrie CP, Mironov AA. The SPCA1 Ca2+ pump and intracellular membrane trafficking. Traffic. 2010;11(10):1315-1333.
    • (2010) Traffic , vol.11 , Issue.10 , pp. 1315-1333
    • Micaroni, M.1    Perinetti, G.2    Berrie, C.P.3    Mironov, A.A.4
  • 78
    • 84868663716 scopus 로고    scopus 로고
    • High levels of Mn2+ inhibit secretory pathway Ca2+/Mn2+-ATPase (SPCA) activity and cause Golgi fragmentation in neurons and glia
    • Sepúlveda MR, Wuytack F, Mata AM. High levels of Mn2+ inhibit secretory pathway Ca2+/Mn2+-ATPase (SPCA) activity and cause Golgi fragmentation in neurons and glia. J Neurochem. 2012;123(5):824-836.
    • (2012) J Neurochem , vol.123 , Issue.5 , pp. 824-836
    • Sepúlveda, M.R.1    Wuytack, F.2    Mata, A.M.3
  • 80
    • 48749111661 scopus 로고    scopus 로고
    • Requirement of the human GARP complex for mannose 6-phosphate-receptor-dependent sorting of Cathepsin D to lysosomes
    • Pérez-Victoria FJ, Mardones GA, Bonifacino JS. Requirement of the human GARP complex for mannose 6-phosphate-receptor-dependent sorting of Cathepsin D to lysosomes. Mol Biol Cell. 2008;19(6):2350-2362.
    • (2008) Mol Biol Cell , vol.19 , Issue.6 , pp. 2350-2362
    • Pérez-Victoria, F.J.1    Mardones, G.A.2    Bonifacino, J.S.3
  • 81
    • 84890884015 scopus 로고    scopus 로고
    • Tethering the assembly of SNARE complexes
    • Hong W, Lev S. Tethering the assembly of SNARE complexes. Trends Cell Biol. 2014;24(1):35-43.
    • (2014) Trends Cell Biol , vol.24 , Issue.1 , pp. 35-43
    • Hong, W.1    Lev, S.2
  • 82
    • 84858698808 scopus 로고    scopus 로고
    • Mannose-6-phosphate pathway: a review on its role in lysosomal function and dysfunction
    • Coutinho MF, Prata MJ, Alves S. Mannose-6-phosphate pathway: a review on its role in lysosomal function and dysfunction. Mol Genet Metab. 2012;105(4):542-550.
    • (2012) Mol Genet Metab , vol.105 , Issue.4 , pp. 542-550
    • Coutinho, M.F.1    Prata, M.J.2    Alves, S.3
  • 83
    • 25144464491 scopus 로고    scopus 로고
    • Clinical and biochemical presentation of siblings with COG-7 deficiency, a lethal multiple O- and N-glycosylation disorder
    • Spaapen LJM, Bakker JA, SBvd M, et al. Clinical and biochemical presentation of siblings with COG-7 deficiency, a lethal multiple O- and N-glycosylation disorder. J Inherit Metab Dis. 2005;28(5):707-714.
    • (2005) J Inherit Metab Dis , vol.28 , Issue.5 , pp. 707-714
    • Spaapen, L.J.M.1    Bakker, J.A.2
  • 85
    • 0035158369 scopus 로고    scopus 로고
    • Sphingomyelin-enriched microdomains at the Golgi complex
    • Gkantiragas I, Brügger B, Stüven E, et al. Sphingomyelin-enriched microdomains at the Golgi complex. Mol Biol Cell. 2001;12(6):1819-1833.
    • (2001) Mol Biol Cell , vol.12 , Issue.6 , pp. 1819-1833
    • Gkantiragas, I.1    Brügger, B.2    Stüven, E.3
  • 86
    • 85018464605 scopus 로고    scopus 로고
    • The interactome of the copper transporter ATP7A belongs to a network of neurodevelopmental and neurodegeneration factors
    • Comstra HS, McArthy J, Rudin-Rush S, et al. The interactome of the copper transporter ATP7A belongs to a network of neurodevelopmental and neurodegeneration factors. eLife. 2017;29:6.
    • (2017) eLife , vol.29 , pp. 6
    • Comstra, H.S.1    McArthy, J.2    Rudin-Rush, S.3
  • 87
    • 84883654492 scopus 로고    scopus 로고
    • Deficiency of the Cog8 subunit in normal and CDG-derived cells impairs the assembly of the COG and Golgi SNARE complexes
    • Laufman O, Freeze HH, Hong W, Lev S. Deficiency of the Cog8 subunit in normal and CDG-derived cells impairs the assembly of the COG and Golgi SNARE complexes. Traffic. 2013;14(10):1065-1077.
    • (2013) Traffic , vol.14 , Issue.10 , pp. 1065-1077
    • Laufman, O.1    Freeze, H.H.2    Hong, W.3    Lev, S.4
  • 88
    • 84880494649 scopus 로고    scopus 로고
    • Fluorescent microscopy as a tool to elucidate dysfunction and mislocalization of Golgi glycosyltransferases in COG complex depleted mammalian cells
    • Willett RA, Pokrovskaya ID, Lupashin VV. Fluorescent microscopy as a tool to elucidate dysfunction and mislocalization of Golgi glycosyltransferases in COG complex depleted mammalian cells. Methods Mol Biol. 2013;1022:61-72.
    • (2013) Methods Mol Biol , vol.1022 , pp. 61-72
    • Willett, R.A.1    Pokrovskaya, I.D.2    Lupashin, V.V.3
  • 89
    • 3142696899 scopus 로고    scopus 로고
    • A new family of potent AB(5) cytotoxins produced by Shiga toxigenic Escherichia coli
    • Paton AW, Srimanote P, Talbot UM, Wang H, Paton JC. A new family of potent AB(5) cytotoxins produced by Shiga toxigenic Escherichia coli. J Exp Med. 2004;200(1):35-46.
    • (2004) J Exp Med , vol.200 , Issue.1 , pp. 35-46
    • Paton, A.W.1    Srimanote, P.2    Talbot, U.M.3    Wang, H.4    Paton, J.C.5
  • 90
    • 84987722769 scopus 로고    scopus 로고
    • Creating knockouts of conserved oligomeric Golgi complex subunits using CRISPR-mediated gene editing paired with a selection strategy based on glycosylation defects associated with impaired COG complex function
    • In, Brown WJ, ed., New York, NY, Springer, -
    • Blackburn JB, Lupashin VV. Creating knockouts of conserved oligomeric Golgi complex subunits using CRISPR-mediated gene editing paired with a selection strategy based on glycosylation defects associated with impaired COG complex function. In: Brown WJ, ed. The Golgi Complex: Methods and Protocols. New York, NY: Springer; 2016:145-161.
    • (2016) The Golgi Complex: Methods and Protocols , pp. 145-161
    • Blackburn, J.B.1    Lupashin, V.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.