메뉴 건너뛰기




Volumn 23, Issue 6, 2013, Pages 690-708

A non-enzymatic function of Golgi glycosyltransferases: Mediation of Golgi fragmentation by interaction with non-muscle myosin IIA

Author keywords

brefeldin A; glycosyltransferase; non muscle myosin IIA; restoration of fragmented Golgi in cancer cells to a compact phenotype; stress induced Golgi fragmentation

Indexed keywords

BREFELDIN A; COATOMER PROTEIN; GLYCOSYLTRANSFERASE; MYOSIN IIA; TUNICAMYCIN;

EID: 84877300116     PISSN: 09596658     EISSN: 14602423     Source Type: Journal    
DOI: 10.1093/glycob/cwt009     Document Type: Article
Times cited : (20)

References (82)
  • 1
    • 84869237251 scopus 로고    scopus 로고
    • Golgi phosphoprotein 3 determines cell binding properties under dynamic flow by controlling Golgi localization of core 2 N-acetylglucosaminyltransferase 1
    • Ali MF, Chachadi VB, Petrosyan A, Cheng PW. 2012. Golgi phosphoprotein 3 determines cell binding properties under dynamic flow by controlling Golgi localization of core 2 N-acetylglucosaminyltransferase 1. J Biol Chem. 287:39564-39577.
    • (2012) J Biol Chem , vol.287 , pp. 39564-39577
    • Ali, M.F.1    Chachadi, V.B.2    Petrosyan, A.3    Cheng, P.W.4
  • 3
    • 0021738607 scopus 로고
    • Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine
    • Balch WE, Dunphy WG, Braell WA, Rothman JE. 1984. Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine. Cell. 39:405-416.
    • (1984) Cell , vol.39 , pp. 405-416
    • Balch, W.E.1    Dunphy, W.G.2    Braell, W.A.3    Rothman, J.E.4
  • 4
    • 0021845762 scopus 로고
    • Ultrastructural localization of cytoskeletal proteins in pancreatic secretory cells
    • Bendayan M. 1985. Ultrastructural localization of cytoskeletal proteins in pancreatic secretory cells. Can J Biochem Cell Biol. 63:680-690.
    • (1985) Can J Biochem Cell Biol , vol.63 , pp. 680-690
    • Bendayan, M.1
  • 5
    • 0028363162 scopus 로고
    • Medial-Golgi retention of N-acetylglucosaminyltransferase I. Contribution from all domains of the enzyme
    • Burke J, Pettitt JM, Humphris D, Gleeson PA. 1994. Medial-Golgi retention of N-acetylglucosaminyltransferase I. Contribution from all domains of the enzyme. J Biol Chem. 269:12049-12059.
    • (1994) J Biol Chem , vol.269 , pp. 12049-12059
    • Burke, J.1    Pettitt, J.M.2    Humphris, D.3    Gleeson, P.A.4
  • 6
    • 8544242762 scopus 로고    scopus 로고
    • The endoplasmic reticulum glucosyltransferase recognizes nearly native glycoprotein folding intermediates
    • Caramelo JJ, Castro OA, de Prat-Gay G, Parodi AJ. 2004. The endoplasmic reticulum glucosyltransferase recognizes nearly native glycoprotein folding intermediates. J Biol Chem. 279:46280-46285.
    • (2004) J Biol Chem , vol.279 , pp. 46280-46285
    • Caramelo, J.J.1    Castro, O.A.2    De Prat-Gay, G.3    Parodi, A.J.4
  • 8
    • 18744393746 scopus 로고    scopus 로고
    • Activation of CMV promotercontrolled glycosyltransferase and beta-galactosidase glycogenes by butyrate, tricostatin A, and 5-aza-2′-deoxycytidine
    • Choi KH, Basma H, Singh J, Cheng PW. 2005. Activation of CMV promotercontrolled glycosyltransferase and beta-galactosidase glycogenes by butyrate, tricostatin A, and 5-aza-2′-deoxycytidine. Glycoconj J. 22:63-69.
    • (2005) Glycoconj J , vol.22 , pp. 63-69
    • Choi, K.H.1    Basma, H.2    Singh, J.3    Cheng, P.W.4
  • 9
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • Cole NB, Sciaky N, Marotta A, Song J, Lippincott-Schwartz J. 1996. Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol Biol Cell. 7:631-650.
    • (1996) Mol Biol Cell , vol.7 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 10
    • 33845432394 scopus 로고    scopus 로고
    • A guide to accurate fluorescence microscopy colocalization measurements
    • Comeau JW, Costantino S, Wiseman PW. 2006. A guide to accurate fluorescence microscopy colocalization measurements. Biophys J. 91:4611-4622.
    • (2006) Biophys J , vol.91 , pp. 4611-4622
    • Comeau, J.W.1    Costantino, S.2    Wiseman, P.W.3
  • 11
    • 39449101285 scopus 로고    scopus 로고
    • Nonmuscle myosin II moves in new directions
    • Conti MA, Adelstein RS. 2008. Nonmuscle myosin II moves in new directions. J Cell Sci. 121:11-18.
    • (2008) J Cell Sci , vol.121 , pp. 11-18
    • Conti, M.A.1    Adelstein, R.S.2
  • 12
    • 0036789924 scopus 로고    scopus 로고
    • A resident Golgi protein is excluded from peri-Golgi vesicles in NRK cells
    • Cosson P, Amherdt M, Rothman JE, Orci L. 2002. A resident Golgi protein is excluded from peri-Golgi vesicles in NRK cells. Proc Natl Acad Sci USA. 99:12831-12834.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12831-12834
    • Cosson, P.1    Amherdt, M.2    Rothman, J.E.3    Orci, L.4
  • 14
    • 58049099709 scopus 로고    scopus 로고
    • A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor
    • Deng Y, Golinelli-Cohen MP, Smirnova E, Jackson CL. 2009. A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor. EMBO Rep. 10:58-64.
    • (2009) EMBO Rep , vol.10 , pp. 58-64
    • Deng, Y.1    Golinelli-Cohen, M.P.2    Smirnova, E.3    Jackson, C.L.4
  • 15
    • 34748860590 scopus 로고    scopus 로고
    • Membrane associated nonmuscle myosin II functions as a motor for actin-based vesicle transport in clam oocyte extracts
    • DePina AS, Wlert T, Langford GM. 2007. Membrane associated nonmuscle myosin II functions as a motor for actin-based vesicle transport in clam oocyte extracts. Cell Motil Cytoskeleton. 64:739-755.
    • (2007) Cell Motil Cytoskeleton , vol.64 , pp. 739-755
    • Depina, A.S.1    Wlert, T.2    Langford, G.M.3
  • 18
    • 0031665311 scopus 로고    scopus 로고
    • Removal and degradation of the free MHC class II beta chain in the endoplasmic reticulum requires proteasomes and is accelerated by BFA
    • Dusseljee S, Wubbolts R, Verwoerd D, Tulp A, Janssen H, Calafat J, Neefjes J. 1998. Removal and degradation of the free MHC class II beta chain in the endoplasmic reticulum requires proteasomes and is accelerated by BFA. J Cell Sci. 111:2217-2226.
    • (1998) J Cell Sci , vol.111 , pp. 2217-2226
    • Dusseljee, S.1    Wubbolts, R.2    Verwoerd, D.3    Tulp, A.4    Janssen, H.5    Calafat, J.6    Neefjes, J.7
  • 19
    • 0027208856 scopus 로고
    • Cis-Golgi resident proteins and O-glycans are abnormally compartmentalized in the RER of colon cancer cells
    • Egea G, FrancC, Gamb G, Lesuffleur T, Zweibaum A, Real FX. 1993. cis-Golgi resident proteins and O-glycans are abnormally compartmentalized in the RER of colon cancer cells. J Cell Sci. 105:819-830.
    • (1993) J Cell Sci , vol.105 , pp. 819-830
    • Egea, G.1    Franc, C.2    Gamb, G.3    Lesuffleur, T.4    Zweibaum, A.5    Real, F.X.6
  • 22
    • 22244458555 scopus 로고    scopus 로고
    • Characterization of myosin-II binding to Golgi stacks in vitro
    • Fath KR. 2005. Characterization of myosin-II binding to Golgi stacks in vitro. Cell Motil Cytoskeleton. 60:222-235.
    • (2005) Cell Motil Cytoskeleton , vol.60 , pp. 222-235
    • Fath, K.R.1
  • 23
    • 84865739859 scopus 로고    scopus 로고
    • Glycosylation potential of human prostate cancer cell lines
    • Gao Y, Chachadi VB, Cheng PW, Brockhausen I. 2012. Glycosylation potential of human prostate cancer cell lines. Glycoconj J. 29:525-537.
    • (2012) Glycoconj J , vol.29 , pp. 525-537
    • Gao, Y.1    Chachadi, V.B.2    Cheng, P.W.3    Brockhausen, I.4
  • 24
    • 77953161781 scopus 로고    scopus 로고
    • Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes
    • Gill DJ, Chia J, Senewiratne J, Bard F. 2010. Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes. J Cell Biol. 189:843-858.
    • (2010) J Cell Biol , vol.189 , pp. 843-858
    • Gill, D.J.1    Chia, J.2    Senewiratne, J.3    Bard, F.4
  • 25
    • 0033579467 scopus 로고    scopus 로고
    • The cytoplasmic, transmembrane, and stem regions of glycosyltransferases specify their in vivo functional sublocalization and stability in the Golgi
    • Grabenhorst E, Conradt HS. 1999. The cytoplasmic, transmembrane, and stem regions of glycosyltransferases specify their in vivo functional sublocalization and stability in the Golgi. J Biol Chem. 274:36107-36116.
    • (1999) J Biol Chem , vol.274 , pp. 36107-36116
    • Grabenhorst, E.1    Conradt, H.S.2
  • 26
  • 27
    • 0033574528 scopus 로고    scopus 로고
    • Specific isoforms of actin-binding proteins on distinct populations of Golgi-derived vesicles
    • Heimann K, Percival JM, Weinberger R, Gunning P, Stow JL. 1999. Specific isoforms of actin-binding proteins on distinct populations of Golgi-derived vesicles. J Biol Chem. 274:10743-10750.
    • (1999) J Biol Chem , vol.274 , pp. 10743-10750
    • Heimann, K.1    Percival, J.M.2    Weinberger, R.3    Gunning, P.4    Stow, J.L.5
  • 28
    • 20544435937 scopus 로고    scopus 로고
    • Golgi structure in stress sensing and apoptosis
    • Hicks SW, Machamer CE. 2005. Golgi structure in stress sensing and apoptosis. Biochim Biophys Acta. 1744:406-414.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 406-414
    • Hicks, S.W.1    MacHamer, C.E.2
  • 29
    • 0031050419 scopus 로고    scopus 로고
    • Effects of shear stress on protein kinase C distribution in endothelial cells
    • Hu YL, Chien S. 1997. Effects of shear stress on protein kinase C distribution in endothelial cells. J Histochem Cytochem. 45:237-249.
    • (1997) J Histochem Cytochem , vol.45 , pp. 237-249
    • Hu, Y.L.1    Chien, S.2
  • 30
    • 0030820352 scopus 로고    scopus 로고
    • Myosin II is associated with Golgi membranes: Identification of p200 as nonmuscle myosin II on Golgi-derived vesicles
    • Ikonen E, de Almeid JB, Fath KR, Burgess DR, Ashman K, Simons K, Stow JL. 1997. Myosin II is associated with Golgi membranes: Identification of p200 as nonmuscle myosin II on Golgi-derived vesicles. J Cell Sci. 110:2155-2164.
    • (1997) J Cell Sci , vol.110 , pp. 2155-2164
    • Ikonen, E.1    De Almeid, J.B.2    Fath, K.R.3    Burgess, D.R.4    Ashman, K.5    Simons, K.6    Stow, J.L.7
  • 31
    • 0023205771 scopus 로고
    • Dolichol-linked glycoprotein synthesis in G1 is necessary for DNA synthesis in synchronized primary cultures of cerebral glia
    • Ishii S, Volpe JJ. 1987. Dolichol-linked glycoprotein synthesis in G1 is necessary for DNA synthesis in synchronized primary cultures of cerebral glia. J Neurochem. 49:1606-1612.
    • (1987) J Neurochem , vol.49 , pp. 1606-1612
    • Ishii, S.1    Volpe, J.J.2
  • 32
    • 17044370911 scopus 로고    scopus 로고
    • Cleavage of nonmuscle myosin heavy chain-A during apoptosis in human Jurkat T cells
    • Kato M, Fukuda H, Nonaka T, Imajoh-Ohmi S. 2005. Cleavage of nonmuscle myosin heavy chain-A during apoptosis in human Jurkat T cells. J Biochem. 137:157-166.
    • (2005) J Biochem , vol.137 , pp. 157-166
    • Kato, M.1    Fukuda, H.2    Nonaka, T.3    Imajoh-Ohmi, S.4
  • 33
    • 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. 2002. Abnormal glycosylation and altered Golgi structure in colorectal cancer: dependence on intra-Golgi pH. FEBS Lett. 516:217-224.
    • (2002) FEBS Lett , vol.516 , pp. 217-224
    • Kellokumpu, S.1    Sormunen, R.2    Kellokumpu, I.3
  • 34
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner RD, Donaldson JG, Lippincott-Schwartz J. 1992. Brefeldin A: Insights into the control of membrane traffic and organelle structure. J Cell Biol. 116:1071-1080.
    • (1992) J Cell Biol , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 37
    • 77955855991 scopus 로고    scopus 로고
    • Myosin II directly binds and inhibits Dbl family guanine nucleotide exchange factors: A possible link to Rho family GTPases
    • Lee CS, Choi CK, Shin EY, Schwartz MA, Kim EG. 2010. Myosin II directly binds and inhibits Dbl family guanine nucleotide exchange factors: A possible link to Rho family GTPases. J Cell Biol. 190:663-674.
    • (2010) J Cell Biol , vol.190 , pp. 663-674
    • Lee, C.S.1    Choi, C.K.2    Shin, E.Y.3    Schwartz, M.A.4    Kim, E.G.5
  • 38
    • 0027755659 scopus 로고
    • Membrane cycling between the ER and Golgi apparatus and its role in biosynthetic transport
    • Lippincott-Schwartz J. 1993. Membrane cycling between the ER and Golgi apparatus and its role in biosynthetic transport. Subcell Biochem. 21:95-119.
    • (1993) Subcell Biochem , vol.21 , pp. 95-119
    • Lippincott-Schwartz, J.1
  • 39
    • 0031809354 scopus 로고    scopus 로고
    • GPIIb-IIIa antagonists cause rapid disaggregation of platelets pre-treated with cytochalasin D. Evidence that the stability of platelet aggregates depends on normal cytoskeletal assembly
    • May JA, Ratan H, Glenn JR, Lche W, Spangenberg P, Heptinstall S. 1998. GPIIb-IIIa antagonists cause rapid disaggregation of platelets pre-treated with cytochalasin D. Evidence that the stability of platelet aggregates depends on normal cytoskeletal assembly. Platelets. 9:227-232.
    • (1998) Platelets , vol.9 , pp. 227-232
    • May, J.A.1    Ratan, H.2    Glenn, J.R.3    Lche, W.4    Spangenberg, P.5    Heptinstall, S.6
  • 42
    • 33947198314 scopus 로고    scopus 로고
    • Fragmentation of the Golgi apparatus: An early apoptotic event independent of the cytoskeleton
    • Mukherjee S, Chiu R, Leung SM, Shields D. 2007. Fragmentation of the Golgi apparatus: An early apoptotic event independent of the cytoskeleton. Traffic. 8:369-378.
    • (2007) Traffic , vol.8 , pp. 369-378
    • Mukherjee, S.1    Chiu, R.2    Leung, S.M.3    Shields, D.4
  • 43
    • 79551659086 scopus 로고    scopus 로고
    • Identification of a gain-of-function mutation in a Golgi P-type ATPase that enhances Mn2+ efflux and protects against toxicity
    • Mukhopadhyay S, Linstedt AD. 2011. Identification of a gain-of-function mutation in a Golgi P-type ATPase that enhances Mn2+ efflux and protects against toxicity. Proc Natl Acad Sci USA. 108:858-863.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 858-863
    • Mukhopadhyay, S.1    Linstedt, A.D.2
  • 44
    • 80053308562 scopus 로고    scopus 로고
    • What is the Golgi apparatus, and why are we asking
    • Munro S. 2011. What is the Golgi apparatus, and why are we asking BMC Biol. 9:63.
    • (2011) BMC Biol , vol.9 , pp. 63
    • Munro, S.1
  • 45
    • 0040971539 scopus 로고    scopus 로고
    • Myosin II is involved in the production of constitutive transport vesicles from the TGN
    • Mch A, Cohen D, Rodriguez-Boulan E. 1997. Myosin II is involved in the production of constitutive transport vesicles from the TGN. J Cell Biol. 138:291-306.
    • (1997) J Cell Biol , vol.138 , pp. 291-306
    • McH, A.1    Cohen, D.2    Rodriguez-Boulan, E.3
  • 47
    • 0030884364 scopus 로고    scopus 로고
    • N-glycosylation is requisite for the enzyme activity and Golgi retention of N-acetylglucosaminyltransferase III
    • Nagai K, Ihara Y, Wada Y, Taniguchi N. 1997. N-glycosylation is requisite for the enzyme activity and Golgi retention of N-acetylglucosaminyltransferase III. Glycobiology. 7:769-776.
    • (1997) Glycobiology , vol.7 , pp. 769-776
    • Nagai, K.1    Ihara, Y.2    Wada, Y.3    Taniguchi, N.4
  • 48
    • 77952855534 scopus 로고    scopus 로고
    • Modification of sphingoglycolipids and sulfolipids in kidney cell lines under heat stress: Activation of monohexosylceramide synthesis as a ceramide scavenger
    • Niimura Y, Moue T, Takahashi N, Nagai K. 2010. Modification of sphingoglycolipids and sulfolipids in kidney cell lines under heat stress: Activation of monohexosylceramide synthesis as a ceramide scavenger. Glycobiology. 20:710-717.
    • (2010) Glycobiology , vol.20 , pp. 710-717
    • Niimura, Y.1    Moue, T.2    Takahashi, N.3    Nagai, K.4
  • 49
    • 0029890064 scopus 로고    scopus 로고
    • The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase i in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells
    • Nilsson T, Rabouille C, Hui N, Watson R, Warren G. 1996. The role of the membrane-spanning domain and stalk region of N-acetylglucosaminyltransferase I in retention, kin recognition and structural maintenance of the Golgi apparatus in HeLa cells. J Cell Sci. 109:1975-1989.
    • (1996) J Cell Sci , vol.109 , pp. 1975-1989
    • Nilsson, T.1    Rabouille, C.2    Hui, N.3    Watson, R.4    Warren, G.5
  • 50
    • 41449115539 scopus 로고    scopus 로고
    • The cytoplasmic region of alpha-1,6-mannosyltransferase Mnn9p is crucial for retrograde transport from the Golgi apparatus to the endoplasmic reticulum in Saccharomyces cerevisiae
    • Okamoto M, Yoko-o T, Miyakawa T, Jigami Y. 2008. The cytoplasmic region of alpha-1,6-mannosyltransferase Mnn9p is crucial for retrograde transport from the Golgi apparatus to the endoplasmic reticulum in Saccharomyces cerevisiae. Eukaryot Cell. 7:310-318.
    • (2008) Eukaryot Cell , vol.7 , pp. 310-318
    • Okamoto, M.1    Yoko-O, T.2    Miyakawa, T.3    Jigami, Y.4
  • 51
    • 0030472766 scopus 로고    scopus 로고
    • Switching aminoterminal cytoplasmic domains of alpha(1,2) fucosyltransferase and alpha (1,3)galactosyltransferase alters the expression of H substance and Galalpha(1,3)Gal
    • Osman N, McKenzie IF, Mouhtouris E, Sandrin MS. 1996. Switching aminoterminal cytoplasmic domains of alpha(1,2)fucosyltransferase and alpha (1,3)galactosyltransferase alters the expression of H substance and Galalpha(1,3)Gal. J Biol Chem. 271:33105-33109.
    • (1996) J Biol Chem , vol.271 , pp. 33105-33109
    • Osman, N.1    McKenzie, I.F.2    Mouhtouris, E.3    Sandrin, M.S.4
  • 52
    • 0027263507 scopus 로고
    • Binding of coatomer to Golgi membranes requires ADP-ribosylation factor
    • Palmer DJ, Helms JB, Beckers CJ, Orci L, Rothman JE. 1993. Binding of coatomer to Golgi membranes requires ADP-ribosylation factor. J Biol Chem. 268:12083-12089.
    • (1993) J Biol Chem , vol.268 , pp. 12083-12089
    • Palmer, D.J.1    Helms, J.B.2    Beckers, C.J.3    Orci, L.4    Rothman, J.E.5
  • 53
    • 0024431691 scopus 로고
    • Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation
    • Paulson JC, Colley KJ. 1989. Glycosyltransferases. Structure, localization, and control of cell type-specific glycosylation. J Biol Chem. 264:17615-17618.
    • (1989) J Biol Chem , vol.264 , pp. 17615-17618
    • Paulson, J.C.1    Colley, K.J.2
  • 54
    • 84868332764 scopus 로고    scopus 로고
    • Glycosyltransferase-specific Golgi targeting mechanisms
    • Petrosyan A, Ali MF, Cheng PW. 2012. Glycosyltransferase-specific Golgi targeting mechanisms. J Biol Chem. 287:37621-37627.
    • (2012) J Biol Chem , vol.287 , pp. 37621-37627
    • Petrosyan, A.1    Ali, M.F.2    Cheng, P.W.3
  • 55
    • 84861227003 scopus 로고    scopus 로고
    • Non-muscle myosin IIA transports a Golgi glycosyltransferase to the endoplasmic reticulum by binding to its cytoplasmic tail
    • Petrosyan A, Ali MF, Verma SK, Cheng H, Cheng PW. 2012. Non-muscle myosin IIA transports a Golgi glycosyltransferase to the endoplasmic reticulum by binding to its cytoplasmic tail. Int J Biochem Cell Biol. 44:1153-1165.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1153-1165
    • Petrosyan, A.1    Ali, M.F.2    Verma, S.K.3    Cheng, H.4    Cheng, P.W.5
  • 56
    • 33751258283 scopus 로고    scopus 로고
    • Lectin-enzyme assay as a method of estimation of immunoglobulins glycosylation
    • Petrosyan A, Britan A. 2006. Lectin-enzyme assay as a method of estimation of immunoglobulins glycosylation. Ukrainski biokhimicheski zhurnal. 78:151-159.
    • (2006) Ukrainski Biokhimicheski Zhurnal , vol.78 , pp. 151-159
    • Petrosyan, A.1    Britan, A.2
  • 57
    • 84888275650 scopus 로고    scopus 로고
    • Activity of blood serum proteinases and inhibitors of proteinases as an index of gastric cancer patients' severity
    • Petrosyan A, Kharchenko V. 2006. Activity of blood serum proteinases and inhibitors of proteinases as an index of gastric cancer patients' severity. Oncologiya. 9:303-306.
    • (2006) Oncologiya , vol.9 , pp. 303-306
    • Petrosyan, A.1    Kharchenko, V.2
  • 58
    • 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. 2011. Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery. Glycobiology. 21:1554-1569.
    • (2011) Glycobiology , vol.21 , pp. 1554-1569
    • Pokrovskaya, I.D.1    Willett, R.2    Smith, R.D.3    Morelle, W.4    Kudlyk, T.5    Lupashin, V.V.6
  • 59
    • 27744552385 scopus 로고    scopus 로고
    • N-glycans of core2 beta (1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): Effects on P-, L-and E-selectin binding
    • Prorok-Hamon M, Notel F, Mathieu S, Langlet C, Fukuda M, El-Battari A. 2005. N-glycans of core2 beta(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of alpha(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): Effects on P-, L-and E-selectin binding. Biochem J. 391:491-502.
    • (2005) Biochem J. , vol.391 , pp. 491-502
    • Prorok-Hamon, M.1    Notel, F.2    Mathieu, S.3    Langlet, C.4    Fukuda, M.5    El-Battari, A.6
  • 60
    • 43549109222 scopus 로고    scopus 로고
    • Calsenilin and CALP interact with the cytoplasmic tail of UDP-Gal:GA2/GM2/GD2 beta-1,3-galactosyltransferase
    • Quintero CA, Valdez-Taubas J, Ferrari ML, Haedo SD, Maccioni HJ. 2008. Calsenilin and CALP interact with the cytoplasmic tail of UDP-Gal:GA2/GM2/GD2 beta-1,3-galactosyltransferase. Biochem J. 412:19-26.
    • (2008) Biochem J , vol.412 , pp. 19-26
    • Quintero, C.A.1    Valdez-Taubas, J.2    Ferrari, M.L.3    Haedo, S.D.4    MacCioni, H.J.5
  • 61
    • 0026352595 scopus 로고
    • Mucin biosyn thesis: Purification and characterization of a mucin N-acetylglucosaminyltransferase
    • Ropp PA, Little MR, Cheng P-W. 1991. Mucin biosynthesis: Purification and characterization of a mucin N-acetylglucosaminyltransferase. J Biol Chem. 266:23863-23871.
    • (1991) J Biol Chem , vol.266 , pp. 23863-23871
    • Ropp, P.A.1    Little, M.R.2    Cheng, P.-W.3
  • 63
    • 0035661433 scopus 로고    scopus 로고
    • Distribution, transport, and degradation of apolipoprotein B-100 in HepG2 cells
    • Sakata N, Phillips TE, Dixon JL. 2001. Distribution, transport, and degradation of apolipoprotein B-100 in HepG2 cells. J Lipid Res. 42:1947-1958.
    • (2001) J Lipid Res , vol.42 , pp. 1947-1958
    • Sakata, N.1    Phillips, T.E.2    Dixon, J.L.3
  • 64
    • 33845428100 scopus 로고    scopus 로고
    • Transition of galactosyltransferase 1 from trans-Golgi cisterna to the trans-Golgi network is signal mediated
    • Schaub BE, Berger B, Berger EG, Rohrer J. 2006. Transition of galactosyltransferase 1 from trans-Golgi cisterna to the trans-Golgi network is signal mediated. Mol Biol Cell. 17:5153-5162.
    • (2006) Mol Biol Cell , vol.17 , pp. 5153-5162
    • Schaub, B.E.1    Berger, B.2    Berger, E.G.3    Rohrer, J.4
  • 65
    • 0030938305 scopus 로고    scopus 로고
    • Dissociation of coatomer from membranes is required for brefeldin A-induced transfer of Golgi enzymes to the endoplasmic reticulum
    • Scheel J, Pepperkok R, Lowe M, Griffiths G, Kreis TE. 1997. Dissociation of coatomer from membranes is required for brefeldin A-induced transfer of Golgi enzymes to the endoplasmic reticulum. J Cell Biol. 137:319-333.
    • (1997) J Cell Biol , vol.137 , pp. 319-333
    • Scheel, J.1    Pepperkok, R.2    Lowe, M.3    Griffiths, G.4    Kreis, T.E.5
  • 67
    • 0037449756 scopus 로고    scopus 로고
    • Fragmentation of the Golgi apparatus. A role for beta III spectrin and synthesis of phosphatidylinositol 4,5-bisphosphate
    • Siddhanta A, Radulescu A, Stankewich MC, Morrow JS, Shields D. 2003. Fragmentation of the Golgi apparatus. A role for beta III spectrin and synthesis of phosphatidylinositol 4,5-bisphosphate. J Biol Chem. 278:1957-1965.
    • (2003) J Biol Chem , vol.278 , pp. 1957-1965
    • Siddhanta, A.1    Radulescu, A.2    Stankewich, M.C.3    Morrow, J.S.4    Shields, D.5
  • 68
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes MA, Rothman JE. 1993. The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell. 73:999-1005.
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 71
    • 0742288022 scopus 로고    scopus 로고
    • Nonmuscle myosin IIA and IIB have distinct functions in the exocytosis-dependent process of cell membrane repair
    • Togo T, Steinhardt RA. 2004. Nonmuscle myosin IIA and IIB have distinct functions in the exocytosis-dependent process of cell membrane repair. Mol Biol Cell. 15:688-695.
    • (2004) Mol Biol Cell , vol.15 , pp. 688-695
    • Togo, T.1    Steinhardt, R.A.2
  • 72
    • 0024432435 scopus 로고
    • The response of the Golgi complex to microtubule alterations: The roles of metabolic energy and membrane traffic in Golgi complex organization
    • Turner JR, Tartakoff AM. 1989. The response of the Golgi complex to microtubule alterations: The roles of metabolic energy and membrane traffic in Golgi complex organization. J Cell Biol. 109:2081-2088.
    • (1989) J Cell Biol , vol.109 , pp. 2081-2088
    • Turner, J.R.1    Tartakoff, A.M.2
  • 73
    • 33745844491 scopus 로고    scopus 로고
    • Cytoplasmic tails of SialT2 and GalNAcT impose their respective proximal and distal Golgi localization
    • Uliana AS, Giraudo CG, Maccioni HJ. 2006. Cytoplasmic tails of SialT2 and GalNAcT impose their respective proximal and distal Golgi localization. Traffic. 7:604-612.
    • (2006) Traffic , vol.7 , pp. 604-612
    • Uliana, A.S.1    Giraudo, C.G.2    MacCioni, H.J.3
  • 74
    • 0034800091 scopus 로고    scopus 로고
    • Actin microfilaments facilitate the retrograde transport from the Golgi complex to the endoplasmic reticulum in mammalian cells
    • Valderrama F, Dur JM, BabiT, Barth H, Renau-Piqueras J, Egea G. 2001. Actin microfilaments facilitate the retrograde transport from the Golgi complex to the endoplasmic reticulum in mammalian cells. Traffic. 2:717-726.
    • (2001) Traffic , vol.2 , pp. 717-726
    • Valderrama, F.1    Dur, J.M.2    Babi, T.3    Barth, H.4    Renau-Piqueras, J.5    Egea, G.6
  • 75
    • 77249120547 scopus 로고    scopus 로고
    • A non-muscle myosin II motor links NR1 to retrograde trafficking and proteasomal degradation in PC12 cells
    • Vazhappilly R, Wee KS, Sucher NJ, Low CM. 2010. A non-muscle myosin II motor links NR1 to retrograde trafficking and proteasomal degradation in PC12 cells. Neurochem Int. 56:569-576.
    • (2010) Neurochem Int , vol.56 , pp. 569-576
    • Vazhappilly, R.1    Wee, K.S.2    Sucher, N.J.3    Low, C.M.4
  • 78
    • 0034941494 scopus 로고    scopus 로고
    • Functional interaction between the SSeCKS scaffolding protein and the cytoplasmic domain of beta1,4-galactosyltransferase
    • Wassler MJ, Foote CI, Gelman IH, Shur BD. 2001. Functional interaction between the SSeCKS scaffolding protein and the cytoplasmic domain of beta1,4-galactosyltransferase. J Cell Sci. 114:2291-2300.
    • (2001) J Cell Sci , vol.114 , pp. 2291-2300
    • Wassler, M.J.1    Foote, C.I.2    Gelman, I.H.3    Shur, B.D.4
  • 79
    • 0025957468 scopus 로고
    • Coatomer A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles
    • Waters MG, Serafini T, Rothman JE. 1991. 'Coatomer': A cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles. Nature. 349:248-251.
    • (1991) Nature , vol.349 , pp. 248-251
    • Waters, M.G.1    Serafini, T.2    Rothman, J.E.3
  • 80
    • 0030905585 scopus 로고    scopus 로고
    • A transfected sialyltransferase that is elevated in breast cancer and localizes to the medial/trans-Golgi apparatus inhibits the development of core-2-based O-glycans
    • Whitehouse C, Burchell J, Gschmeissner S, Brockhausen I, Lloyd KO, Taylor-Papadimitriou J. 1997. A transfected sialyltransferase that is elevated in breast cancer and localizes to the medial/trans-Golgi apparatus inhibits the development of core-2-based O-glycans. J Cell Biol. 137:1229-1241.
    • (1997) J Cell Biol , vol.137 , pp. 1229-1241
    • Whitehouse, C.1    Burchell, J.2    Gschmeissner, S.3    Brockhausen, I.4    Lloyd, K.O.5    Taylor-Papadimitriou, J.6
  • 81
    • 0029067675 scopus 로고
    • Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha-and beta-tubulins
    • Yamaguchi N, Fukuda MN. 1995. Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha-and beta-tubulins. J Biol Chem. 270:12170-12176.
    • (1995) J Biol Chem , vol.270 , pp. 12170-12176
    • Yamaguchi, N.1    Fukuda, M.N.2
  • 82
    • 0034212740 scopus 로고    scopus 로고
    • Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells
    • Yokota S, Kitahara M, Nagata K. 2000. Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells. Cancer Res. 60:2942-2948.
    • (2000) Cancer Res , vol.60 , pp. 2942-2948
    • Yokota, S.1    Kitahara, M.2    Nagata, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.