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Volumn 80, Issue 5, 2014, Pages 809-822

The transmembrane domain of N -acetylglucosaminyltransferase i is the key determinant for its Golgi subcompartmentation

Author keywords

Arabidopsis thaliana; glycosyltransferase; Golgi apparatus; N glycan processing; Nicotiana benthamiana; protein protein interaction; transmembrane domain; type II membrane protein

Indexed keywords

ACTIVATION ANALYSIS; CELL PROLIFERATION; PLANTS (BOTANY); POLYSACCHARIDES; BIOLOGICAL MEMBRANES;

EID: 84928011518     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/tpj.12671     Document Type: Article
Times cited : (22)

References (51)
  • 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, M.F., Chachadi, V.B., Petrosyan, A., and, Cheng, P.W., (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
  • 2
    • 0035956939 scopus 로고    scopus 로고
    • Galactose-extended glycans of antibodies produced by transgenic plants
    • Bakker, H., Bardor, M., Molthoff, J., et al. (2001) Galactose-extended glycans of antibodies produced by transgenic plants. Proc. Natl Acad. Sci. USA, 98, 2899-2904.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 2899-2904
    • Bakker, H.1    Bardor, M.2    Molthoff, J.3
  • 3
    • 33646737444 scopus 로고    scopus 로고
    • An antibody produced in tobacco expressing a hybrid beta-1,4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes
    • Bakker, H., Rouwendal, G., Karnoup, A., Florack, D., Stoopen, G., Helsper, J., van Ree, R., van Die, I., and, Bosch, D., (2006) An antibody produced in tobacco expressing a hybrid beta-1,4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes. Proc. Natl Acad. Sci. USA, 103, 7577-7582.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 7577-7582
    • Bakker, H.1    Rouwendal, G.2    Karnoup, A.3    Florack, D.4    Stoopen, G.5    Helsper, J.6    Van Ree, R.7    Van Die, I.8    Bosch, D.9
  • 4
    • 0033082668 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy: Spatial resolution of biochemical processes in the cell
    • Bastiaens, P.I., and, Squire, A., (1999) Fluorescence lifetime imaging microscopy: spatial resolution of biochemical processes in the cell. Trends Cell Biol. 9, 48-52.
    • (1999) Trends Cell Biol. , vol.9 , pp. 48-52
    • Bastiaens, P.I.1    Squire, A.2
  • 5
    • 0032144201 scopus 로고    scopus 로고
    • Stacks on tracks: The plant Golgi apparatus traffics on an actin/ER network
    • Boevink, P., Oparka, K., Santa Cruz, S., Martin, B., Betteridge, A., and, Hawes, C., (1998) Stacks on tracks: the plant Golgi apparatus traffics on an actin/ER network. Plant J. 15, 441-447.
    • (1998) Plant J. , vol.15 , pp. 441-447
    • Boevink, P.1    Oparka, K.2    Santa Cruz, S.3    Martin, B.4    Betteridge, A.5    Hawes, C.6
  • 6
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S., and, Cordelières, F.P., (2006) A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 224, 213-232.
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelières, F.P.2
  • 7
    • 0036016439 scopus 로고    scopus 로고
    • The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain
    • Brandizzi, F., Frangne, N., Marc-Martin, S., Hawes, C., Neuhaus, J., and, Paris, N., (2002a) The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain. Plant Cell, 14, 1077-1092.
    • (2002) Plant Cell , vol.14 , pp. 1077-1092
    • Brandizzi, F.1    Frangne, N.2    Marc-Martin, S.3    Hawes, C.4    Neuhaus, J.5    Paris, N.6
  • 8
    • 0035983848 scopus 로고    scopus 로고
    • Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: Evidence from selective photobleaching
    • Brandizzi, F., Snapp, E., Roberts, A., Lippincott-Schwartz, J., and, Hawes, C., (2002b) Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching. Plant Cell, 14, 1293-1309.
    • (2002) Plant Cell , vol.14 , pp. 1293-1309
    • Brandizzi, F.1    Snapp, E.2    Roberts, A.3    Lippincott-Schwartz, J.4    Hawes, C.5
  • 9
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher, M., and, Munro, S., (1993) Cholesterol and the Golgi apparatus. Science, 261, 1280-1281.
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.1    Munro, S.2
  • 10
    • 0028363162 scopus 로고
    • Medial-Golgi retention of N-acetylglucosaminyltransferase I. Contribution from all domains of the enzyme
    • Burke, J., Pettitt, J., Humphris, D., and, Gleeson, P., (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.2    Humphris, D.3    Gleeson, P.4
  • 11
    • 78650121974 scopus 로고    scopus 로고
    • Subcompartment localization of the side chain xyloglucan-synthesizing enzymes within Golgi stacks of tobacco suspension-cultured cells
    • Chevalier, L., Bernard, S., Ramdani, Y., Lamour, R., Bardor, M., Lerouge, P., Follet-Gueye, M.L., and, Driouich, A., (2010) Subcompartment localization of the side chain xyloglucan-synthesizing enzymes within Golgi stacks of tobacco suspension-cultured cells. Plant J. 64, 977-989.
    • (2010) Plant J. , vol.64 , pp. 977-989
    • Chevalier, L.1    Bernard, S.2    Ramdani, Y.3    Lamour, R.4    Bardor, M.5    Lerouge, P.6    Follet-Gueye, M.L.7    Driouich, A.8
  • 13
    • 84898024932 scopus 로고    scopus 로고
    • Galactosyltransferases from Arabidopsis thaliana in the biosynthesis of type II arabinogalactan: Molecular interaction enhances enzyme activity
    • Dilokpimol, A., Poulsen, C.P., Vereb, G., Kaneko, S., Schulz, A., and, Geshi, N., (2014) Galactosyltransferases from Arabidopsis thaliana in the biosynthesis of type II arabinogalactan: molecular interaction enhances enzyme activity. BMC Plant Biol. 14, 90.
    • (2014) BMC Plant Biol. , vol.14 , pp. 90
    • Dilokpimol, A.1    Poulsen, C.P.2    Vereb, G.3    Kaneko, S.4    Schulz, A.5    Geshi, N.6
  • 14
    • 14044256547 scopus 로고    scopus 로고
    • Multiple signals are required for alpha2,6-sialyltransferase (ST6Gal I) oligomerization and Golgi localization
    • Fenteany, F., and, Colley, K., (2005) Multiple signals are required for alpha2,6-sialyltransferase (ST6Gal I) oligomerization and Golgi localization. J. Biol. Chem. 280, 5423-5429.
    • (2005) J. Biol. Chem. , vol.280 , pp. 5423-5429
    • Fenteany, F.1    Colley, K.2
  • 15
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation
    • Gadella, T.W., and, Jovin, T.M., (1995) Oligomerization of epidermal growth factor receptors on A431 cells studied by time-resolved fluorescence imaging microscopy. A stereochemical model for tyrosine kinase receptor activation. J. Cell Biol. 129, 1543-1558.
    • (1995) J. Cell Biol. , vol.129 , pp. 1543-1558
    • Gadella, T.W.1    Jovin, T.M.2
  • 16
    • 84863097595 scopus 로고    scopus 로고
    • The Golgi-localized Arabidopsis endomembrane protein12 contains both endoplasmic reticulum export and Golgi retention signals at its C terminus
    • Gao, C., Yu, C.K., Qu, S., San, M.W., Li, K.Y., Lo, S.W., and, Jiang, L., (2012) The Golgi-localized Arabidopsis endomembrane protein12 contains both endoplasmic reticulum export and Golgi retention signals at its C terminus. Plant Cell, 24, 2086-2104.
    • (2012) Plant Cell , vol.24 , pp. 2086-2104
    • Gao, C.1    Yu, C.K.2    Qu, S.3    San, M.W.4    Li, K.Y.5    Lo, S.W.6    Jiang, L.7
  • 17
    • 0141521617 scopus 로고    scopus 로고
    • Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1
    • Giraudo, C., and, Maccioni, H., (2003) Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1. Mol. Biol. Cell, 14, 3753-3766.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3753-3766
    • Giraudo, C.1    MacCioni, H.2
  • 18
    • 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., and, Conradt, H., (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.2
  • 19
    • 77952944920 scopus 로고    scopus 로고
    • Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme complexes in live cells
    • Hassinen, A., Rivinoja, A., Kauppila, A., and, Kellokumpu, S., (2010) Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme complexes in live cells. J. Biol. Chem. 285, 17771-17777.
    • (2010) J. Biol. Chem. , vol.285 , pp. 17771-17777
    • Hassinen, A.1    Rivinoja, A.2    Kauppila, A.3    Kellokumpu, S.4
  • 20
    • 84860015488 scopus 로고    scopus 로고
    • Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulum-associated degradation of glycoproteins
    • Hüttner, S., Veit, C., Schoberer, J., Grass, J., and, Strasser, R., (2012) Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulum-associated degradation of glycoproteins. Plant Mol. Biol. 79, 21-33.
    • (2012) Plant Mol. Biol. , vol.79 , pp. 21-33
    • Hüttner, S.1    Veit, C.2    Schoberer, J.3    Grass, J.4    Strasser, R.5
  • 21
    • 44449138388 scopus 로고    scopus 로고
    • Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus
    • Kang, J.S., Frank, J., Kang, C.H., et al. (2008) Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus. Proc. Natl Acad. Sci. USA, 105, 5933-5938.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 5933-5938
    • Kang, J.S.1    Frank, J.2    Kang, C.H.3
  • 22
    • 0141509840 scopus 로고    scopus 로고
    • Quantitative imaging of protein-protein interactions by multiphoton fluorescence lifetime imaging microscopy using a streak camera
    • Krishnan, R.V., Masuda, A., Centonze, V.E., and, Herman, B., (2003) Quantitative imaging of protein-protein interactions by multiphoton fluorescence lifetime imaging microscopy using a streak camera. J. Biomed. Opt. 8, 362-367.
    • (2003) J. Biomed. Opt. , vol.8 , pp. 362-367
    • Krishnan, R.V.1    Masuda, A.2    Centonze, V.E.3    Herman, B.4
  • 23
    • 0025946217 scopus 로고
    • Golgi retention signals: Do membranes hold the key?
    • Machamer, C.E., (1991) Golgi retention signals: do membranes hold the key? Trends Cell Biol. 1, 141-144.
    • (1991) Trends Cell Biol. , vol.1 , pp. 141-144
    • MacHamer, C.E.1
  • 24
    • 0029165107 scopus 로고
    • An investigation of the role of transmembrane domains in Golgi protein retention
    • Munro, S., (1995) An investigation of the role of transmembrane domains in Golgi protein retention. EMBO J. 14, 4695-4704.
    • (1995) EMBO J. , vol.14 , pp. 4695-4704
    • Munro, S.1
  • 26
    • 0026072695 scopus 로고
    • The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization
    • Nilsson, T., Lucocq, J.M., Mackay, D., and, Warren, G., (1991) The membrane spanning domain of beta-1,4-galactosyltransferase specifies trans Golgi localization. EMBO J. 10, 3567-3575.
    • (1991) EMBO J. , vol.10 , pp. 3567-3575
    • Nilsson, T.1    Lucocq, J.M.2    MacKay, D.3    Warren, G.4
  • 28
    • 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., and, 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
  • 29
    • 84871719148 scopus 로고    scopus 로고
    • Golgi-localized enzyme complexes for plant cell wall biosynthesis
    • Oikawa, A., Lund, C.H., Sakuragi, Y., and, Scheller, H.V., (2013) Golgi-localized enzyme complexes for plant cell wall biosynthesis. Trends Plant Sci. 18, 49-58.
    • (2013) Trends Plant Sci. , vol.18 , pp. 49-58
    • Oikawa, A.1    Lund, C.H.2    Sakuragi, Y.3    Scheller, H.V.4
  • 30
    • 67649887900 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging of interactions between Golgi tethering factors and small GTPases in plants
    • Osterrieder, A., Carvalho, C., Latijnhouwers, M., Johansen, J., Stubbs, C., Botchway, S., and, Hawes, C., (2009) Fluorescence lifetime imaging of interactions between Golgi tethering factors and small GTPases in plants. Traffic, 10, 1034-1046.
    • (2009) Traffic , vol.10 , pp. 1034-1046
    • Osterrieder, A.1    Carvalho, C.2    Latijnhouwers, M.3    Johansen, J.4    Stubbs, C.5    Botchway, S.6    Hawes, C.7
  • 31
    • 0033551250 scopus 로고    scopus 로고
    • Stable expression of human beta1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns
    • Palacpac, N., Yoshida, S., Sakai, H., Kimura, Y., Fujiyama, K., Yoshida, T., and, Seki, T., (1999) Stable expression of human beta1,4-galactosyltransferase in plant cells modifies N-linked glycosylation patterns. Proc. Natl Acad. Sci. USA, 96, 4692-4697.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 4692-4697
    • Palacpac, N.1    Yoshida, S.2    Sakai, H.3    Kimura, Y.4    Fujiyama, K.5    Yoshida, T.6    Seki, T.7
  • 32
    • 28444472038 scopus 로고    scopus 로고
    • Opinion: The maturing role of COPI vesicles in intra-Golgi transport
    • Rabouille, C., and, Klumperman, J., (2005) Opinion: the maturing role of COPI vesicles in intra-Golgi transport. Nat. Rev. Mol. Cell Biol. 6, 812-817.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 812-817
    • Rabouille, C.1    Klumperman, J.2
  • 34
    • 23744476301 scopus 로고    scopus 로고
    • Identification and characterization of AtCASP, a plant transmembrane Golgi matrix protein
    • Renna, L., Hanton, S., Stefano, G., Bortolotti, L., Misra, V., and, Brandizzi, F., (2005) Identification and characterization of AtCASP, a plant transmembrane Golgi matrix protein. Plant Mol. Biol. 58, 109-122.
    • (2005) Plant Mol. Biol. , vol.58 , pp. 109-122
    • Renna, L.1    Hanton, S.2    Stefano, G.3    Bortolotti, L.4    Misra, V.5    Brandizzi, F.6
  • 36
    • 41649090365 scopus 로고    scopus 로고
    • Golgi localization of glycosyltransferases requires a Vps74p oligomer
    • Schmitz, K., Liu, J., Li, S., Setty, T., Wood, C., Burd, C., and, Ferguson, K., (2008) Golgi localization of glycosyltransferases requires a Vps74p oligomer. Dev. Cell, 14, 523-534.
    • (2008) Dev. Cell , vol.14 , pp. 523-534
    • Schmitz, K.1    Liu, J.2    Li, S.3    Setty, T.4    Wood, C.5    Burd, C.6    Ferguson, K.7
  • 37
    • 79953185070 scopus 로고    scopus 로고
    • Sub-compartmental organization of Golgi-resident N-glycan processing enzymes in plants
    • Schoberer, J., and, Strasser, R., (2011) Sub-compartmental organization of Golgi-resident N-glycan processing enzymes in plants. Mol. Plant, 4, 220-228.
    • (2011) Mol. Plant , vol.4 , pp. 220-228
    • Schoberer, J.1    Strasser, R.2
  • 38
    • 58149185093 scopus 로고    scopus 로고
    • Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes
    • Schoberer, J., Vavra, U., Stadlmann, J., Hawes, C., Mach, L., Steinkellner, H., and, Strasser, R., (2009) Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes. Traffic, 10, 101-115.
    • (2009) Traffic , vol.10 , pp. 101-115
    • Schoberer, J.1    Vavra, U.2    Stadlmann, J.3    Hawes, C.4    MacH, L.5    Steinkellner, H.6    Strasser, R.7
  • 39
    • 78649478925 scopus 로고    scopus 로고
    • Sequential depletion and acquisition of proteins during Golgi stack disassembly and reformation
    • Schoberer, J., Runions, J., Steinkellner, H., Strasser, R., Hawes, C., and, Osterrieder, A., (2010) Sequential depletion and acquisition of proteins during Golgi stack disassembly and reformation. Traffic, 11, 1429-1444.
    • (2010) Traffic , vol.11 , pp. 1429-1444
    • Schoberer, J.1    Runions, J.2    Steinkellner, H.3    Strasser, R.4    Hawes, C.5    Osterrieder, A.6
  • 40
    • 84875714380 scopus 로고    scopus 로고
    • Time-resolved fluorescence imaging reveals differential interactions of N-glycan processing enzymes across the Golgi stack in planta
    • Schoberer, J., Liebminger, E., Botchway, S.W., Strasser, R., and, Hawes, C., (2013) Time-resolved fluorescence imaging reveals differential interactions of N-glycan processing enzymes across the Golgi stack in planta. Plant Physiol. 161, 1737-1754.
    • (2013) Plant Physiol. , vol.161 , pp. 1737-1754
    • Schoberer, J.1    Liebminger, E.2    Botchway, S.W.3    Strasser, R.4    Hawes, C.5
  • 41
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe, H., Stevens, T., and, Munro, S., (2010) A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell, 142, 158-169.
    • (2010) Cell , vol.142 , pp. 158-169
    • Sharpe, H.1    Stevens, T.2    Munro, S.3
  • 42
    • 77953177103 scopus 로고    scopus 로고
    • Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties
    • Sparkes, I., Tolley, N., Aller, I., Svozil, J., Osterrieder, A., Botchway, S., Mueller, C., Frigerio, L., and, Hawes, C., (2010) Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties. Plant Cell, 22, 1333-1343.
    • (2010) Plant Cell , vol.22 , pp. 1333-1343
    • Sparkes, I.1    Tolley, N.2    Aller, I.3    Svozil, J.4    Osterrieder, A.5    Botchway, S.6    Mueller, C.7    Frigerio, L.8    Hawes, C.9
  • 43
    • 48949089988 scopus 로고    scopus 로고
    • Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides
    • Stadlmann, J., Pabst, M., Kolarich, D., Kunert, R., and, Altmann, F., (2008) Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides. Proteomics, 8, 2858-2871.
    • (2008) Proteomics , vol.8 , pp. 2858-2871
    • Stadlmann, J.1    Pabst, M.2    Kolarich, D.3    Kunert, R.4    Altmann, F.5
  • 44
    • 1542358140 scopus 로고    scopus 로고
    • Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose
    • Strasser, R., Altmann, F., Mach, L., Glössl, J., and, Steinkellner, H., (2004) Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose. FEBS Lett. 561, 132-136.
    • (2004) FEBS Lett. , vol.561 , pp. 132-136
    • Strasser, R.1    Altmann, F.2    MacH, L.3    Glössl, J.4    Steinkellner, H.5
  • 45
    • 68949137116 scopus 로고    scopus 로고
    • Improved virus neutralization by plant-produced anti-HIV antibodies with a homogeneous beta1,4-galactosylated N-glycan profile
    • Strasser, R., Castilho, A., Stadlmann, J., et al. (2009) Improved virus neutralization by plant-produced anti-HIV antibodies with a homogeneous beta1,4-galactosylated N-glycan profile. J. Biol. Chem. 284, 20479-20485.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20479-20485
    • Strasser, R.1    Castilho, A.2    Stadlmann, J.3
  • 46
    • 25444471326 scopus 로고    scopus 로고
    • The use of time-resolved fluorescence imaging in the study of protein kinase C localisation in cells
    • Stubbs, C.D., Botchway, S.W., Slater, S.J., and, Parker, A.W., (2005) The use of time-resolved fluorescence imaging in the study of protein kinase C localisation in cells. BMC Cell Biol. 6, 22.
    • (2005) BMC Cell Biol. , vol.6 , pp. 22
    • Stubbs, C.D.1    Botchway, S.W.2    Slater, S.J.3    Parker, A.W.4
  • 47
    • 73749085462 scopus 로고    scopus 로고
    • Localization of Golgi-resident glycosyltransferases
    • Tu, L., and, Banfield, D., (2010) Localization of Golgi-resident glycosyltransferases. Cell. Mol. Life Sci. 67, 29-41.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 29-41
    • Tu, L.1    Banfield, D.2
  • 48
    • 47749141468 scopus 로고    scopus 로고
    • Signal-mediated dynamic retention of glycosyltransferases in the Golgi
    • Tu, L., Tai, W., Chen, L., and, Banfield, D., (2008) Signal-mediated dynamic retention of glycosyltransferases in the Golgi. Science, 321, 404-407.
    • (2008) Science , vol.321 , pp. 404-407
    • Tu, L.1    Tai, W.2    Chen, L.3    Banfield, D.4
  • 49
    • 33745844491 scopus 로고    scopus 로고
    • Cytoplasmic tails of SialT2 and GalNAcT impose their respective proximal and distal Golgi localization
    • Uliana, A., Giraudo, C., and, Maccioni, H., (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.1    Giraudo, C.2    MacCioni, H.3
  • 50
    • 0032191992 scopus 로고    scopus 로고
    • Targeting of active sialyltransferase to the plant Golgi apparatus
    • Wee, E., Sherrier, D., Prime, T., and, Dupree, P., (1998) Targeting of active sialyltransferase to the plant Golgi apparatus. Plant Cell, 10, 1759-1768.
    • (1998) Plant Cell , vol.10 , pp. 1759-1768
    • Wee, E.1    Sherrier, D.2    Prime, T.3    Dupree, P.4


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