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Volumn 1744, Issue 2, 2005, Pages 93-107

The plant Golgi apparatus - Going with the flow

Author keywords

Membrane flow; Plant Golgi apparatus; Protein trafficking

Indexed keywords

GUANOSINE TRIPHOSPHATASE;

EID: 20444386846     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2005.03.009     Document Type: Review
Times cited : (41)

References (167)
  • 1
    • 0001402447 scopus 로고
    • Cytological and cytochemical characteristics of the Golgi substance of epithelial cells of the epididymis-in situ, in homogenates and after isolation
    • A.J. Dalton, and M.D. Felix Cytological and cytochemical characteristics of the Golgi substance of epithelial cells of the epididymis-in situ, in homogenates and after isolation Am. J. Anat. 94 1954 171 208
    • (1954) Am. J. Anat. , vol.94 , pp. 171-208
    • Dalton, A.J.1    Felix, M.D.2
  • 2
    • 0018650756 scopus 로고
    • The Golgi apparatus, the plasma membrane, and functional integration
    • D.G. Whaley, and M. Dauwalder The Golgi apparatus, the plasma membrane, and functional integration Int. Rev. Cytol. 58 1979 199 245
    • (1979) Int. Rev. Cytol. , vol.58 , pp. 199-245
    • Whaley, D.G.1    Dauwalder, M.2
  • 4
    • 0141497248 scopus 로고    scopus 로고
    • Protein transport in plant cells: In and out of the Golgi
    • U. Neumann, F. Brandizzi, and C. Hawes Protein transport in plant cells: in and out of the Golgi Ann. Bot. 92 2003 167 180
    • (2003) Ann. Bot. , vol.92 , pp. 167-180
    • Neumann, U.1    Brandizzi, F.2    Hawes, C.3
  • 5
    • 8444223534 scopus 로고    scopus 로고
    • Membrane trafficking in plants
    • G. Jürgens Membrane trafficking in plants Ann. Rev. Cell Dev. Biol. 20 2004 481 504
    • (2004) Ann. Rev. Cell Dev. Biol. , vol.20 , pp. 481-504
    • Jürgens, G.1
  • 6
    • 11144295188 scopus 로고    scopus 로고
    • Cell biology of the plant Golgi apparatus
    • C. Hawes Cell biology of the plant Golgi apparatus New Phytol. 165 2005 29 44
    • (2005) New Phytol. , vol.165 , pp. 29-44
    • Hawes, C.1
  • 7
    • 3042603709 scopus 로고    scopus 로고
    • The Golgi apparatus in mammalian and higher plant cells: A comparison
    • D.G. Robinson Blackwell Oxford, UK
    • M. Pavelka, and D.G. Robinson The Golgi apparatus in mammalian and higher plant cells: a comparison D.G. Robinson The Golgi Apparatus and the Plant Secretory Pathway 2003 Blackwell Oxford, UK 16 36
    • (2003) The Golgi Apparatus and the Plant Secretory Pathway , pp. 16-36
    • Pavelka, M.1    Robinson, D.G.2
  • 9
    • 2142750167 scopus 로고    scopus 로고
    • GFP is the way to glow: Bioimaging of the plant endomembrane system
    • F. Brandizzi, S.L. Irons, J. Johansen, A. Kotzer, and U. Neumann GFP is the way to glow: bioimaging of the plant endomembrane system J. Microsc. 214 2004 138 158
    • (2004) J. Microsc. , vol.214 , pp. 138-158
    • Brandizzi, F.1    Irons, S.L.2    Johansen, J.3    Kotzer, A.4    Neumann, U.5
  • 10
    • 0001048021 scopus 로고
    • The Golgi apparatus
    • P. Stumpf E. Conn Academic Press New York
    • H.H. Mollenhauer, and D.J. Morré The Golgi apparatus P. Stumpf E. Conn The Biochemistry of Plants 1980 Academic Press New York 437 488
    • (1980) The Biochemistry of Plants , pp. 437-488
    • Mollenhauer, H.H.1    Morré, D.J.2
  • 12
    • 0027095663 scopus 로고
    • Redistribution of a Golgi glycoprotein in plant cells treated wit Brefeldin a
    • B. Satiat-Jeunemaitre, and C. Hawes Redistribution of a Golgi glycoprotein in plant cells treated wit Brefeldin A J. Cell Sci. 103 1992 1153 1166
    • (1992) J. Cell Sci. , vol.103 , pp. 1153-1166
    • Satiat-Jeunemaitre, B.1    Hawes, C.2
  • 15
    • 0035212730 scopus 로고    scopus 로고
    • Mobile factories: Golgi dynamics in plant cells
    • A. Nebenführ, and L.A. Staehelin Mobile factories: Golgi dynamics in plant cells Trends Plant Sci. 6 2001 160 167
    • (2001) Trends Plant Sci. , vol.6 , pp. 160-167
    • Nebenführ, A.1    Staehelin, L.A.2
  • 17
    • 0842265856 scopus 로고    scopus 로고
    • Dynamics of proteins in Golgi membranes: Comparisons between mammalian and plant cells highlighted by photobleaching techniques
    • T.H. Ward, and F. Brandizzi Dynamics of proteins in Golgi membranes: comparisons between mammalian and plant cells highlighted by photobleaching techniques Cell Mol. Life Sci. 61 2004 172 185
    • (2004) Cell Mol. Life Sci. , vol.61 , pp. 172-185
    • Ward, T.H.1    Brandizzi, F.2
  • 18
    • 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
    • F. Brandizzi, E.L. Snapp, A.G. Roberts, J. Lippincott-Schwartz, and C. Hawes 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 2002 1293 1309
    • (2002) Plant Cell , vol.14 , pp. 1293-1309
    • Brandizzi, F.1    Snapp, E.L.2    Roberts, A.G.3    Lippincott-Schwartz, J.4    Hawes, C.5
  • 19
    • 0036006196 scopus 로고    scopus 로고
    • Redistribution of membrane proteins between the Golgi apparatus and endoplasmic reticulum in plants is reversible and not dependent on cytoskeletal networks
    • C.M. Saint-Jore, J. Evins, H. Batoko, F. Brandizzi, I. Moore, and C. Hawes Redistribution of membrane proteins between the Golgi apparatus and endoplasmic reticulum in plants is reversible and not dependent on cytoskeletal networks Plant J. 29 2002 661 678
    • (2002) Plant J. , vol.29 , pp. 661-678
    • Saint-Jore, C.M.1    Evins, J.2    Batoko, H.3    Brandizzi, F.4    Moore, I.5    Hawes, C.6
  • 21
    • 16544368038 scopus 로고    scopus 로고
    • ER-derived compartments are formed by highly regulated processes and have special functions in plants
    • G. Galili ER-derived compartments are formed by highly regulated processes and have special functions in plants Plant Physiol. 136 2004 3411 3413
    • (2004) Plant Physiol. , vol.136 , pp. 3411-3413
    • Galili, G.1
  • 22
    • 16544378458 scopus 로고    scopus 로고
    • Diversity and formation of endoplasmic reticulum-derived compartments in plants. Are these compartments specific to plant cells?
    • I. Hara-Nishimura, R. Matsushima, T. Shimada, and M. Nishimura Diversity and formation of endoplasmic reticulum-derived compartments in plants. Are these compartments specific to plant cells? Plant Physiol. 136 2004 3435 3439
    • (2004) Plant Physiol. , vol.136 , pp. 3435-3439
    • Hara-Nishimura, I.1    Matsushima, R.2    Shimada, T.3    Nishimura, M.4
  • 23
    • 16544394131 scopus 로고    scopus 로고
    • Protein quality control mechanisms and protein storage in the endoplasmic reticulum. a conflict of interests?
    • A. Vitale, and A. Ceriotti Protein quality control mechanisms and protein storage in the endoplasmic reticulum. A conflict of interests? Plant Physiol. 136 2004 3420 3426
    • (2004) Plant Physiol. , vol.136 , pp. 3420-3426
    • Vitale, A.1    Ceriotti, A.2
  • 24
    • 0031795695 scopus 로고    scopus 로고
    • Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles
    • I. Hara-Nishimura, T. Shiada, K. Hatano, Y. Takeuchi, and M. Nishimura Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles Plant Cell 10 1998 825 836
    • (1998) Plant Cell , vol.10 , pp. 825-836
    • Hara-Nishimura, I.1    Shiada, T.2    Hatano, K.3    Takeuchi, Y.4    Nishimura, M.5
  • 25
    • 0002986778 scopus 로고    scopus 로고
    • The cell wall
    • B.B. Buchanan W. Gruissem R.L. Jones American Society of Plant Physiology Rockville MD, USA
    • N.C. Carpita, and M. McCann The cell wall B.B. Buchanan W. Gruissem R.L. Jones Biochemistry and Molecular Biology of Plants 2000 American Society of Plant Physiology Rockville MD, USA 52 108
    • (2000) Biochemistry and Molecular Biology of Plants , pp. 52-108
    • Carpita, N.C.1    McCann, M.2
  • 26
    • 2442610818 scopus 로고    scopus 로고
    • Glycosyltransferases and cell wall biosynthesis: Novel players and insights
    • W.-R. Scheible, and M. Pauly Glycosyltransferases and cell wall biosynthesis: novel players and insights Curr. Opin. Plant Biol. 7 2004 285 295
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 285-295
    • Scheible, W.-R.1    Pauly, M.2
  • 27
    • 0033367395 scopus 로고    scopus 로고
    • Molecular domains of the cellulose/xyloglucan network in the cell walls of higher plants
    • M. Pauly, P. Albersheim, A. Darvill, and W.S. York Molecular domains of the cellulose/xyloglucan network in the cell walls of higher plants Plant J. 20 1999 629 639
    • (1999) Plant J. , vol.20 , pp. 629-639
    • Pauly, M.1    Albersheim, P.2    Darvill, A.3    York, W.S.4
  • 28
    • 1042278607 scopus 로고    scopus 로고
    • Primary cell wall metabolism: Tracking the careers of wall polymers in living plant cells
    • S.C. Fry Primary cell wall metabolism: tracking the careers of wall polymers in living plant cells New Phytol. 161 2004 641 675
    • (2004) New Phytol. , vol.161 , pp. 641-675
    • Fry, S.C.1
  • 29
    • 0028103135 scopus 로고
    • Localization of xylosylation ad fucosylation in the plant Golgi apparatus
    • A.C. Fitchette-Lainé, V. Gomord, A. Chekkafi, and L. Faye Localization of xylosylation ad fucosylation in the plant Golgi apparatus Plant J. 5 1994 673 682
    • (1994) Plant J. , vol.5 , pp. 673-682
    • Fitchette-Lainé, A.C.1    Gomord, V.2    Chekkafi, A.3    Faye, L.4
  • 30
    • 0002267444 scopus 로고    scopus 로고
    • The Golgi apparatus and pathways of vesicle trafficking
    • M. Smallwood P. Knox D. Bowles Bios Scientific Publishers Oxford
    • C. Hawes, L. Faye, and B. Satiat-Jeunemaitre The Golgi apparatus and pathways of vesicle trafficking M. Smallwood P. Knox D. Bowles Membranes: Specialized Functions in Plants 1996 Bios Scientific Publishers Oxford 337 365
    • (1996) Membranes: Specialized Functions in Plants , pp. 337-365
    • Hawes, C.1    Faye, L.2    Satiat-Jeunemaitre, B.3
  • 32
    • 0036715728 scopus 로고    scopus 로고
    • The Golgi localization of Arabidopsis thaliana beta 1,2- xylosyltransferase in plant cells is dependent on its cytoplasmic and transmembrane sequences
    • D. Dirnberger, P. Bencur, L. Mach, and H. Steinkellner The Golgi localization of Arabidopsis thaliana beta 1,2-xylosyltransferase in plant cells is dependent on its cytoplasmic and transmembrane sequences Plant Mol. Biol. 50 2002 273 281
    • (2002) Plant Mol. Biol. , vol.50 , pp. 273-281
    • Dirnberger, D.1    Bencur, P.2    MacH, L.3    Steinkellner, H.4
  • 33
    • 11244292123 scopus 로고    scopus 로고
    • Arabidopsis thaliana expresses multiple Golgi-localised nucleotide-sugar transporters related to GONST1
    • M.G. Handford, F. Sicilia, F. Brandizzi, J.H. Chung, and P. Dupree Arabidopsis thaliana expresses multiple Golgi-localised nucleotide-sugar transporters related to GONST1 Mol. Genet. Genomics 272 2004 397 410
    • (2004) Mol. Genet. Genomics , vol.272 , pp. 397-410
    • Handford, M.G.1    Sicilia, F.2    Brandizzi, F.3    Chung, J.H.4    Dupree, P.5
  • 35
    • 0037042193 scopus 로고    scopus 로고
    • Effects of brefeldin a and nordihydroguaiaretic acid on endomembrane dynamics and lipid synthesis in plant cells
    • P. Mérigout, F. Képès, A.-M. Perret, B. Satiat-Jeunemaitre, and P. Moreau Effects of brefeldin A and nordihydroguaiaretic acid on endomembrane dynamics and lipid synthesis in plant cells FEBS Lett. 518 2002 88 92
    • (2002) FEBS Lett. , vol.518 , pp. 88-92
    • Mérigout, P.1    Képès, F.2    Perret, A.-M.3    Satiat-Jeunemaitre, B.4    Moreau, P.5
  • 36
    • 11144305471 scopus 로고    scopus 로고
    • Phospholipid synthesis and dynamics in plant cells
    • J.-J. Bessoule, and P. Moreau Phospholipid synthesis and dynamics in plant cells Top. Curr. Genet. 6 2003 89 124
    • (2003) Top. Curr. Genet. , vol.6 , pp. 89-124
    • Bessoule, J.-J.1    Moreau, P.2
  • 37
    • 0032718565 scopus 로고    scopus 로고
    • Vacuoles
    • F. Marty Vacuoles Plant Cell 11 1999 587 599
    • (1999) Plant Cell , vol.11 , pp. 587-599
    • Marty, F.1
  • 38
    • 0842280199 scopus 로고    scopus 로고
    • Sorting of lytic enzymes in the plant Golgi apparatus
    • D.G. Robinson Blackwell Oxford, UK
    • L.W. Jiang, and J.C. Rogers Sorting of lytic enzymes in the plant Golgi apparatus D.G. Robinson The Golgi Apparatus and the Plant Secretory Pathway 2003 Blackwell Oxford, UK 114 140
    • (2003) The Golgi Apparatus and the Plant Secretory Pathway , pp. 114-140
    • Jiang, L.W.1    Rogers, J.C.2
  • 40
    • 1642372806 scopus 로고    scopus 로고
    • FM-dyes as experimental probes for dissecting vesicle trafficking in living plant cells
    • S. Bolte, C. Talbot, Y. Boutte, O. Catrice, N.D. Read, and B. Satiat-Jeunemaitre FM-dyes as experimental probes for dissecting vesicle trafficking in living plant cells J. Microsc. 214 2004 159 173
    • (2004) J. Microsc. , vol.214 , pp. 159-173
    • Bolte, S.1    Talbot, C.2    Boutte, Y.3    Catrice, O.4    Read, N.D.5    Satiat-Jeunemaitre, B.6
  • 41
    • 4344606680 scopus 로고    scopus 로고
    • The plant endosomal system-ist structure and role in signal transduction and plant development
    • N. Geldner The plant endosomal system-ist structure and role in signal transduction and plant development Planta 219 2004 547 560
    • (2004) Planta , vol.219 , pp. 547-560
    • Geldner, N.1
  • 42
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • J.E. Rothman Mechanisms of intracellular protein transport Nature 372 1994 55 63
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 43
    • 0032169017 scopus 로고    scopus 로고
    • The molecular characterization of transport vesicles
    • D.G. Robinson, G. Hinz, and S.E.H. Holstein The molecular characterization of transport vesicles Plant Mol. Biol. 38 1998 49 76
    • (1998) Plant Mol. Biol. , vol.38 , pp. 49-76
    • Robinson, D.G.1    Hinz, G.2    Holstein, S.E.H.3
  • 44
    • 0013905715 scopus 로고
    • Tubular connections between dictyosomes and forming secretory vesicles in plant Golgi apparatus
    • H.H. Mollenhauer, and D.J. Morré Tubular connections between dictyosomes and forming secretory vesicles in plant Golgi apparatus J. Cell Biol. 29 1966 373 376
    • (1966) J. Cell Biol. , vol.29 , pp. 373-376
    • Mollenhauer, H.H.1    Morré, D.J.2
  • 48
    • 0000401129 scopus 로고
    • Golgi apparatus activity and membrane flow during scale biogenesis in the green flagellate Scherffelia dubia (prasinophyceae) I. Flagellar regeneration
    • G.I. MacFadden, and M. Melkonian Golgi apparatus activity and membrane flow during scale biogenesis in the green flagellate Scherffelia dubia (prasinophyceae) I. Flagellar regeneration Protoplasma 130 1986 186 198
    • (1986) Protoplasma , vol.130 , pp. 186-198
    • MacFadden, G.I.1    Melkonian, M.2
  • 50
    • 10444243528 scopus 로고
    • Scale biogenesis in the green alga, Mesostigma viride
    • D.S. Domozych, B. Wells, and P.J. Shaw Scale biogenesis in the green alga, Mesostigma viride Protoplasma 167 1992 19 32
    • (1992) Protoplasma , vol.167 , pp. 19-32
    • Domozych, D.S.1    Wells, B.2    Shaw, P.J.3
  • 51
    • 0000122262 scopus 로고
    • Anterograde transport of algal scales through the Golgi complex is not mediated by vesicles
    • B. Becker, B. Bölinger, and M. Melkonian Anterograde transport of algal scales through the Golgi complex is not mediated by vesicles Trends Cell Biol. 5 1995 305 307
    • (1995) Trends Cell Biol. , vol.5 , pp. 305-307
    • Becker, B.1    Bölinger, B.2    Melkonian, M.3
  • 52
    • 0027263647 scopus 로고
    • The distribution of secretory products in plant cells is affected by Brefeldin a
    • B. Satiat-Jeunemaitre, and C. Hawes The distribution of secretory products in plant cells is affected by Brefeldin A Cell Biol. Int. 17 1993 183 193
    • (1993) Cell Biol. Int. , vol.17 , pp. 183-193
    • Satiat-Jeunemaitre, B.1    Hawes, C.2
  • 53
    • 0027573692 scopus 로고
    • Effect of brefeldin a on the structure of the Golgi apparatus and on the synthesis and secretion of proteins and polysaccharides in sycamore maple (Acer pseudoplatanus) suspension-cultured cells
    • A. Driouich, G.F. Zhang, and A.L. Staehelin Effect of brefeldin A on the structure of the Golgi apparatus and on the synthesis and secretion of proteins and polysaccharides in sycamore maple (Acer pseudoplatanus) suspension-cultured cells Plant Physiol. 101 1993 1363 1373
    • (1993) Plant Physiol. , vol.101 , pp. 1363-1373
    • Driouich, A.1    Zhang, G.F.2    Staehelin, A.L.3
  • 54
    • 0036007958 scopus 로고    scopus 로고
    • Reevaluation of the effects of Brefeldin a on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green fluorescent protein and COPI antisera
    • C. Ritzenthaler, A. Nebenführ, A. Movafeghi, C. Stussi-Garaud, L. Behnia, P. Pimpl, L.A. Staehelin, and D.G. Robinson Reevaluation of the effects of Brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green fluorescent protein and COPI antisera Plant Cell 14 2002 237 261
    • (2002) Plant Cell , vol.14 , pp. 237-261
    • Ritzenthaler, C.1    Nebenführ, A.2    Movafeghi, A.3    Stussi-Garaud, C.4    Behnia, L.5    Pimpl, P.6    Staehelin, L.A.7    Robinson, D.G.8
  • 55
    • 0033117122 scopus 로고    scopus 로고
    • The specificity of vesicle trafficking: Coat proteins and SNAREs
    • A.A. Sanderfoot, and N.V. Raikhel The specificity of vesicle trafficking: coat proteins and SNAREs Plant Cell 11 1999 629 641
    • (1999) Plant Cell , vol.11 , pp. 629-641
    • Sanderfoot, A.A.1    Raikhel, N.V.2
  • 56
    • 0036883448 scopus 로고    scopus 로고
    • Vesicle traffic in the endomembrane system: A tale of COPs, Rabs and SNAREs
    • A. Nebenführ Vesicle traffic in the endomembrane system: a tale of COPs, Rabs and SNAREs Curr. Opin. Plant Biol. 5 2002 507 512
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 507-512
    • Nebenführ, A.1
  • 61
    • 1542415665 scopus 로고    scopus 로고
    • The N-myristoylated Rab-GTPase m-Rabmc is involved in post-Golgi trafficking events to the lytic vacuole in plant cells
    • S. Bolte, S. Brown, and B. Satiat-Jeunemaitre The N-myristoylated Rab-GTPase m-Rabmc is involved in post-Golgi trafficking events to the lytic vacuole in plant cells J. Cell Sci. 117 2004 943 954
    • (2004) J. Cell Sci. , vol.117 , pp. 943-954
    • Bolte, S.1    Brown, S.2    Satiat-Jeunemaitre, B.3
  • 62
    • 0036883478 scopus 로고    scopus 로고
    • The Arabidopsis Rab GTPase family: Another enigma variation
    • S. Rutherford, and I. Moore The Arabidopsis Rab GTPase family: another enigma variation Curr. Opin. Plant Biol. 5 2002 518 528
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 518-528
    • Rutherford, S.1    Moore, I.2
  • 64
    • 0034525357 scopus 로고    scopus 로고
    • The Arabidopsis genome. An abundance of soluble N-ethylmaleimide- sensitive factor adaptor protein receptors
    • A.A. Sanderfoot, F.F. Assaad, and N.V. Raikhel The Arabidopsis genome. An abundance of soluble N-ethylmaleimide-sensitive factor adaptor protein receptors Plant Physiol. 124 2000 1558 1569
    • (2000) Plant Physiol. , vol.124 , pp. 1558-1569
    • Sanderfoot, A.A.1    Assaad, F.F.2    Raikhel, N.V.3
  • 65
    • 1842472709 scopus 로고    scopus 로고
    • SNARE components and mechanisms of exocytosis in plants
    • D.G. Robinson Blackwell Oxford, UK
    • M.R. Blatt, and G. Thiel SNARE components and mechanisms of exocytosis in plants D.G. Robinson The Golgi Apparatus and the Plant Secretory Pathway 2003 Blackwell Oxford, UK 208 237
    • (2003) The Golgi Apparatus and the Plant Secretory Pathway , pp. 208-237
    • Blatt, M.R.1    Thiel, G.2
  • 67
    • 0002547154 scopus 로고
    • Vesicle dynamics and membrane turnover in plant cells
    • C. Hawes J. Coleman D. Evans Cambridge Univ. Press Cambridge
    • M.W. Steer, and D. O'Driscoll Vesicle dynamics and membrane turnover in plant cells C. Hawes J. Coleman D. Evans Endocytosis, Exocytosis and Vesicle Traffic in Plants 1991 Cambridge Univ. Press Cambridge 129 142
    • (1991) Endocytosis, Exocytosis and Vesicle Traffic in Plants , pp. 129-142
    • Steer, M.W.1    O'Driscoll, D.2
  • 68
    • 0020625589 scopus 로고
    • The effect of cycloheximide on dictyosome activity in Tradescantia pollen tubes determined using cytochalasin D
    • J.M. Picton, and M.W. Steer The effect of cycloheximide on dictyosome activity in Tradescantia pollen tubes determined using cytochalasin D Eur. J. Cell Biol. 29 1983 133 138
    • (1983) Eur. J. Cell Biol. , vol.29 , pp. 133-138
    • Picton, J.M.1    Steer, M.W.2
  • 71
    • 0001629099 scopus 로고
    • Formation and disintegration of cisternae of the endoplasmic reticulum visualized in live cells by conventional fluorescence and confocal laser scanning microscopy: Evidence for involvement of calcium and the cytoskeleton
    • H. Quader Formation and disintegration of cisternae of the endoplasmic reticulum visualized in live cells by conventional fluorescence and confocal laser scanning microscopy: evidence for involvement of calcium and the cytoskeleton Protoplasma 155 1990 166 175
    • (1990) Protoplasma , vol.155 , pp. 166-175
    • Quader, H.1
  • 73
    • 10144263345 scopus 로고    scopus 로고
    • Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex
    • C. Kluge, T. Seidel, S. Bolte, S. Sharma, M. Hanitzsch, B. Satiat-Jeunemaitre, J. Rothmann, D. Golldack, and K.-J. Dietz Subcellular distribution of the V-ATPase complex in plant cells, and in vivo localisation of the 100 kDa subunit VHA-a within the complex BMC 5 2004 29
    • (2004) BMC , vol.5 , pp. 29
    • Kluge, C.1    Seidel, T.2    Bolte, S.3    Sharma, S.4    Hanitzsch, M.5    Satiat-Jeunemaitre, B.6    Rothmann, J.7    Golldack, D.8    Dietz, K.-J.9
  • 74
    • 0026752711 scopus 로고
    • Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic reticulum
    • R.M. Napier, L.C. Fowke, C. Hawes, M. Lewis, and H. Pelham Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic reticulum J. Cell Sci. 102 1992 261 271
    • (1992) J. Cell Sci. , vol.102 , pp. 261-271
    • Napier, R.M.1    Fowke, L.C.2    Hawes, C.3    Lewis, M.4    Pelham, H.5
  • 76
    • 0032799602 scopus 로고    scopus 로고
    • The N-terminal 77 amino acids from tobacco N- acetylglucosoaminyltransferase I are sufficient to retain a reporter protein in the Golgi apparatus of Nicotiana benthamiana cells
    • D. Essl, D. Dirnberger, V. Gomord, R. Strasser, L. Faye, J. Glössl, and H. Steinkellner The N-terminal 77 amino acids from tobacco N-acetylglucosoaminyltransferase I are sufficient to retain a reporter protein in the Golgi apparatus of Nicotiana benthamiana cells FEBS Lett. 453 1999 169 173
    • (1999) FEBS Lett. , vol.453 , pp. 169-173
    • Essl, D.1    Dirnberger, D.2    Gomord, V.3    Strasser, R.4    Faye, L.5    Glössl, J.6    Steinkellner, H.7
  • 77
    • 0034755283 scopus 로고    scopus 로고
    • Identification and characterization of GONST1, a Golgi-localized GDP-mannose transporter in Arabidopsis
    • T.C. Baldwin, M.G. Handford, M.I. Yuseff, A. Oorellana, and P. Dupree Identification and characterization of GONST1, a Golgi-localized GDP-mannose transporter in Arabidopsis Plant Cell 13 2001 2283 2295
    • (2001) Plant Cell , vol.13 , pp. 2283-2295
    • Baldwin, T.C.1    Handford, M.G.2    Yuseff, M.I.3    Oorellana, A.4    Dupree, P.5
  • 78
    • 0031976015 scopus 로고    scopus 로고
    • Localization of proteins to the Golgi apparatus
    • S. Munro Localization of proteins to the Golgi apparatus Trends Cell Biol. 8 1998 11 15
    • (1998) Trends Cell Biol. , vol.8 , pp. 11-15
    • Munro, S.1
  • 79
    • 0032191992 scopus 로고    scopus 로고
    • Targeting of active sialyl transferase to the plant Golgi apparatus
    • E.G.-T. Wee, D.J. Sherrier, T.A. Prime, and P. Dupree Targeting of active sialyl transferase to the plant Golgi apparatus Plant Cell 10 1998 1759 1768
    • (1998) Plant Cell , vol.10 , pp. 1759-1768
    • Wee, E.G.-T.1    Sherrier, D.J.2    Prime, T.A.3    Dupree, P.4
  • 80
    • 0001812897 scopus 로고    scopus 로고
    • Golgi-membrane dynamics are cytoskeleton dependent: A study on Golgi stack movement induced by brefeldin a
    • B. Satiat-Jeunemaitre, C. Steele, and C. Hawes Golgi-membrane dynamics are cytoskeleton dependent: a study on Golgi stack movement induced by brefeldin A Protoplasma 191 1996 21 33
    • (1996) Protoplasma , vol.191 , pp. 21-33
    • Satiat-Jeunemaitre, B.1    Steele, C.2    Hawes, C.3
  • 81
    • 12844281650 scopus 로고    scopus 로고
    • An internal motor kinesin is associated with the Golgi apparatus and plays a role in trichome morphogenesis in Arabidopsis
    • L. Liu, Y.R. Lee, R. Pan, J.N. Maloof, and B. Liu An internal motor kinesin is associated with the Golgi apparatus and plays a role in trichome morphogenesis in Arabidopsis Mol. Biol. Cell 16 2005 811 823
    • (2005) Mol. Biol. Cell , vol.16 , pp. 811-823
    • Liu, L.1    Lee, Y.R.2    Pan, R.3    Maloof, J.N.4    Liu, B.5
  • 82
    • 16644365802 scopus 로고    scopus 로고
    • A plant-specific kinesin binds to actin microfilaments and interacts with cortical microtubules in cotton fibers
    • M.L. Preuss, D.R. Kovar, Y.-R. Lee, C.T.J. Staiger, D.P. Delmer, and B. Liu A plant-specific kinesin binds to actin microfilaments and interacts with cortical microtubules in cotton fibers Plant Physiol. 136 2004 3945 3955
    • (2004) Plant Physiol. , vol.136 , pp. 3945-3955
    • Preuss, M.L.1    Kovar, D.R.2    Lee, Y.-R.3    Staiger, C.T.J.4    Delmer, D.P.5    Liu, B.6
  • 84
    • 0031131603 scopus 로고    scopus 로고
    • Characterization of AtSEC12 and AtSAR1. Proteins likely involved in endoplasmic reticulum and Golgi transport
    • M. Bar-Peled, and N. Raikhel Characterization of AtSEC12 and AtSAR1. Proteins likely involved in endoplasmic reticulum and Golgi transport Plant Physiol. 114 1997 315 324
    • (1997) Plant Physiol. , vol.114 , pp. 315-324
    • Bar-Peled, M.1    Raikhel, N.2
  • 85
    • 0026670522 scopus 로고
    • Fission yeast and a plant have functional homologues of the Sar1 and Sec12 proteins involved in ER to Golgi traffic in budding yeast
    • C. D'Enfert, M. Geusse, and C. Gaillardin Fission yeast and a plant have functional homologues of the Sar1 and Sec12 proteins involved in ER to Golgi traffic in budding yeast EMBO J. 11 1992 4205 4210
    • (1992) EMBO J. , vol.11 , pp. 4205-4210
    • D'Enfert, C.1    Geusse, M.2    Gaillardin, C.3
  • 86
    • 0033117623 scopus 로고    scopus 로고
    • Arabidopsis Sec21p and Sec23p homologs. Probable coat proteins of plant COP-coated vesicles
    • A. Movafeghi, N. Happel, P. Pimpl, G.H. Tai, and D.G. Robinson Arabidopsis Sec21p and Sec23p homologs. Probable coat proteins of plant COP-coated vesicles Plant Physiol. 119 1999 1437 1445
    • (1999) Plant Physiol. , vol.119 , pp. 1437-1445
    • Movafeghi, A.1    Happel, N.2    Pimpl, P.3    Tai, G.H.4    Robinson, D.G.5
  • 87
    • 0033838323 scopus 로고    scopus 로고
    • A dominant negative mutant of Sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis suspension cultured cells
    • M. Takeuchi, T. Ueda, K. Sato, H. Abe, T. Nagata, and A. Nakano A dominant negative mutant of Sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis suspension cultured cells Plant J. 23 2000 517 525
    • (2000) Plant J. , vol.23 , pp. 517-525
    • Takeuchi, M.1    Ueda, T.2    Sato, K.3    Abe, H.4    Nagata, T.5    Nakano, A.6
  • 88
    • 0141521617 scopus 로고    scopus 로고
    • Endoplasmic reticulum export of glycosyl transferases depends on interaction of a cytoplasmic dibasic motif with Sar1
    • C.G. Giraudo, and J.F. Maccioni Endoplasmic reticulum export of glycosyl transferases depends on interaction of a cytoplasmic dibasic motif with Sar1 Mol. Biol. Cell 14 2003 3753 3766
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3753-3766
    • Giraudo, C.G.1    MacCioni, J.F.2
  • 89
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organisation in Pichia pastoris and Saccharomyces cerevisia
    • O.W. Rossanese, J.S. Soderholm, B.J. Bevis, I.B. Sears, J. O'Connor, E.K. Williamsn, and B.S. Glick Golgi structure correlates with transitional endoplasmic reticulum organisation in Pichia pastoris and Saccharomyces cerevisia J. Cell Biol. 145 1999 69 81
    • (1999) J. Cell Biol. , vol.145 , pp. 69-81
    • Rossanese, O.W.1    Soderholm, J.S.2    Bevis, B.J.3    Sears, I.B.4    O'Connor, J.5    Williamsn, E.K.6    Glick, B.S.7
  • 90
    • 0036701908 scopus 로고    scopus 로고
    • COPII-dependent transport from the endoplasmic reticulum
    • C. Barlowe COPII-dependent transport from the endoplasmic reticulum Curr. Opin. Cell Biol. 14 2002 417 422
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 417-422
    • Barlowe, C.1
  • 92
    • 0442292206 scopus 로고    scopus 로고
    • Biogenesis of ER-to-Golgi transport carriers: Complex roles of COPII in ER export
    • K.J. Palmer, and D.J. Stephens Biogenesis of ER-to-Golgi transport carriers: complex roles of COPII in ER export Trends Cell Biol. 14 2004 57 61
    • (2004) Trends Cell Biol. , vol.14 , pp. 57-61
    • Palmer, K.J.1    Stephens, D.J.2
  • 94
    • 2542632045 scopus 로고    scopus 로고
    • Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer
    • I. Contreras, E. Ortiz-Zapater, and F. Aniento Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer Plant J. 38 2004 685 698
    • (2004) Plant J. , vol.38 , pp. 685-698
    • Contreras, I.1    Ortiz-Zapater, E.2    Aniento, F.3
  • 95
    • 0043262923 scopus 로고    scopus 로고
    • Identification and localization of a-COP-like protein involved in the morphodynamics of the plant Golgi apparatus
    • I. Couchy, S. Bolte, M.-T. Crosnier, S. Brown, and B. Satiat-Jeunemaitre Identification and localization of a-COP-like protein involved in the morphodynamics of the plant Golgi apparatus J. Exp. Bot. 54 2003 2053 2063
    • (2003) J. Exp. Bot. , vol.54 , pp. 2053-2063
    • Couchy, I.1    Bolte, S.2    Crosnier, M.-T.3    Brown, S.4    Satiat-Jeunemaitre, B.5
  • 97
    • 0036667381 scopus 로고    scopus 로고
    • Arf1 GTPase plays roles in the protein traffic between the ER and the Golgi apparatus in tobacco and Arabidopsis cultured cells
    • M. Takeuchi, T. Ueda, N. Yahara, and A. Nakano Arf1 GTPase plays roles in the protein traffic between the ER and the Golgi apparatus in tobacco and Arabidopsis cultured cells Plant J. 31 2002 499 515
    • (2002) Plant J. , vol.31 , pp. 499-515
    • Takeuchi, M.1    Ueda, T.2    Yahara, N.3    Nakano, A.4
  • 98
    • 0037008335 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 of arabidopsis plays a critical role in intracellular trafficking and maintenance of endoplasmic reticulu morphology in Arabidopsis
    • M.H. Lee, M.K. Min, Y.J. Lee, J.B. Jin, D.H. Shin, D.H. Kim, K.-H. Lee, and I. Hwang ADP-ribosylation factor 1 of arabidopsis plays a critical role in intracellular trafficking and maintenance of endoplasmic reticulu morphology in Arabidopsis Plant Physiol. 129 2002 1507 1520
    • (2002) Plant Physiol. , vol.129 , pp. 1507-1520
    • Lee, M.H.1    Min, M.K.2    Lee, Y.J.3    Jin, J.B.4    Shin, D.H.5    Kim, D.H.6    Lee, K.-H.7    Hwang, I.8
  • 99
    • 0036667381 scopus 로고    scopus 로고
    • Arf1 GTPase plays roles in the protein traffic between the endoplasmic reticulum and the Golgi apparatus in tobacco and Arabidopsis cultured cells
    • N. Yahara, and A. Nakano Arf1 GTPase plays roles in the protein traffic between the endoplasmic reticulum and the Golgi apparatus in tobacco and Arabidopsis cultured cells Plant J. 31 2002 499 515
    • (2002) Plant J. , vol.31 , pp. 499-515
    • Yahara, N.1    Nakano, A.2
  • 100
    • 0038366776 scopus 로고    scopus 로고
    • The GTPase ARF1p controls the sequence-specific vacuolar sorting route to the lytic vacuole
    • P. Pimpl, S. Hanton, J.P. Taylor, L.L. Pinto-daSilva, and J. Denecke The GTPase ARF1p controls the sequence-specific vacuolar sorting route to the lytic vacuole Plant Cell 15 2003 1242 1256
    • (2003) Plant Cell , vol.15 , pp. 1242-1256
    • Pimpl, P.1    Hanton, S.2    Taylor, J.P.3    Pinto-Dasilva, L.L.4    Denecke, J.5
  • 101
    • 0036707861 scopus 로고    scopus 로고
    • Protein secretion in plants: From the trans-Golgi network to the outer space
    • G. Jürgens, and N. Geldner Protein secretion in plants: from the trans-Golgi network to the outer space Traffic 3 2002 605 613
    • (2002) Traffic , vol.3 , pp. 605-613
    • Jürgens, G.1    Geldner, N.2
  • 102
    • 0142252552 scopus 로고    scopus 로고
    • Analysis of the small GTPase gene superfamily of Arabidopsis
    • V. Vernoud, A.C. Horton, Z. Yang, and E. Nielsen Analysis of the small GTPase gene superfamily of Arabidopsis Plant Physiol. 131 2003 1191 1208
    • (2003) Plant Physiol. , vol.131 , pp. 1191-1208
    • Vernoud, V.1    Horton, A.C.2    Yang, Z.3    Nielsen, E.4
  • 104
    • 4444309237 scopus 로고    scopus 로고
    • Systematic analyses of SNARE molecules in Arabidopsis: Dissection of the post-Golgi network in plant cells
    • T. Uemera, T. Ueda, R.L. Ohniwa, A. Nakano, K. Takeyasu, and M.H. Sato Systematic analyses of SNARE molecules in Arabidopsis: dissection of the post-Golgi network in plant cells Cell Struct. Funct. 29 2004 49 65
    • (2004) Cell Struct. Funct. , vol.29 , pp. 49-65
    • Uemera, T.1    Ueda, T.2    Ohniwa, R.L.3    Nakano, A.4    Takeyasu, K.5    Sato, M.H.6
  • 105
    • 0034525907 scopus 로고    scopus 로고
    • A Rab1 GTPase is required for transport between the endoplasmic reticulum and Golgi apparatus and for normal Golgi movement in plants
    • H. Batoko, H.Q. Zheng, C. Hawes, and I. Moore A Rab1 GTPase is required for transport between the endoplasmic reticulum and Golgi apparatus and for normal Golgi movement in plants Plant Cell 12 2000 2201 2217
    • (2000) Plant Cell , vol.12 , pp. 2201-2217
    • Batoko, H.1    Zheng, H.Q.2    Hawes, C.3    Moore, I.4
  • 106
    • 0035999380 scopus 로고    scopus 로고
    • Rab2 GTPase regulates trafficking between the endoplasmic reticulum and the Golgi bodies and is important for pollen tube growth
    • A.Y. Cheung, C.Y.-H. Chen, R.H. Glaven, B.H.J. de Graaff, L. Vidali, P.K. Hepler, and H.-M. Wu Rab2 GTPase regulates trafficking between the endoplasmic reticulum and the Golgi bodies and is important for pollen tube growth Plant Cell 14 2002 945 962
    • (2002) Plant Cell , vol.14 , pp. 945-962
    • Cheung, A.Y.1    Chen, C.Y.-H.2    Glaven, R.H.3    De Graaff, B.H.J.4    Vidali, L.5    Hepler, P.K.6    Wu, H.-M.7
  • 108
    • 0005593831 scopus 로고    scopus 로고
    • Endoplasmic reticulum in the cortex of plant cells
    • M. Smallwood J.P. Knox D.J. Bowles Bios Scientific Publishers
    • I.K. Lichtscheidl, and P.K. Hepler Endoplasmic reticulum in the cortex of plant cells M. Smallwood J.P. Knox D.J. Bowles Membranes Specialised Functions in Plants 1996 Bios Scientific Publishers 383 402
    • (1996) Membranes Specialised Functions in Plants , pp. 383-402
    • Lichtscheidl, I.K.1    Hepler, P.K.2
  • 109
    • 0000839516 scopus 로고
    • The relationship between dictyosomes and the forms of endoplasmic reticulum in plant cells with different export programs
    • B. Juniper, C.R. Hawes, and J.C. Horne The relationship between dictyosomes and the forms of endoplasmic reticulum in plant cells with different export programs Bot. Gaz. 143 1982 135 145
    • (1982) Bot. Gaz. , vol.143 , pp. 135-145
    • Juniper, B.1    Hawes, C.R.2    Horne, J.C.3
  • 110
    • 0002288932 scopus 로고
    • Connections between dictyosomes, ER and GERL in cotyledons of mung bean (Vigna radiata L.)
    • N. Harris, and K.J. Oparka Connections between dictyosomes, ER and GERL in cotyledons of mung bean (Vigna radiata L.) Protoplasma 114 1983 93 102
    • (1983) Protoplasma , vol.114 , pp. 93-102
    • Harris, N.1    Oparka, K.J.2
  • 111
    • 0000260364 scopus 로고
    • An observation on the functioning of the Golgi apparatus
    • H.H. Mollenhauer, and W.G. Whaley An observation on the functioning of the Golgi apparatus J. Cell Biol. 17 1963 222 225
    • (1963) J. Cell Biol. , vol.17 , pp. 222-225
    • Mollenhauer, H.H.1    Whaley, W.G.2
  • 112
    • 11144279521 scopus 로고    scopus 로고
    • Sorting of storage proteins in the plant Golgi apparatus
    • D.G. Robinson Blackwell Oxford, UK
    • G. Hinz, and E. Herman Sorting of storage proteins in the plant Golgi apparatus D.G. Robinson The Golgi Apparatus and the Plant Secretory Pathway 2003 Blackwell Oxford, UK 141 164
    • (2003) The Golgi Apparatus and the Plant Secretory Pathway , pp. 141-164
    • Hinz, G.1    Herman, E.2
  • 113
    • 12444262344 scopus 로고    scopus 로고
    • The cargo in vacuolar storage protein transport vesicles is stratified
    • B. Wenzel, G. Schauerman, A. von Lüpke, and G. Hinz The cargo in vacuolar storage protein transport vesicles is stratified Traffic 6 2005 1 11
    • (2005) Traffic , vol.6 , pp. 1-11
    • Wenzel, B.1    Schauerman, G.2    Von Lüpke, A.3    Hinz, G.4
  • 114
    • 0013878343 scopus 로고
    • Structure of isolated plant Golgi apparatus revealed by negative staining
    • W.P. Cunningham, D.J. Morré, and H.H. Mollenhauer Structure of isolated plant Golgi apparatus revealed by negative staining J. Cell Biol. 28 1966 169 179
    • (1966) J. Cell Biol. , vol.28 , pp. 169-179
    • Cunningham, W.P.1    Morré, D.J.2    Mollenhauer, H.H.3
  • 115
    • 1242316455 scopus 로고
    • The Golgi apparatus in developing endosperm of wheat triticum sativum L.
    • M.L. Parker, and C. Hawes The Golgi apparatus in developing endosperm of wheat triticum sativum L. Planta 154 1982 277 283
    • (1982) Planta , vol.154 , pp. 277-283
    • Parker, M.L.1    Hawes, C.2
  • 116
    • 0025697919 scopus 로고
    • Macromolecular differentiation of Golgi stacks in root tips of Arabidopsis and Nicotiana seedlings as visualized in high pressure frozen and freeze-substituted samples
    • L.A. Staehelin, T.H. Giddings Jr., J.Z. Kiss, and F.D. Sack Macromolecular differentiation of Golgi stacks in root tips of Arabidopsis and Nicotiana seedlings as visualized in high pressure frozen and freeze-substituted samples Protoplasma 157 1990 75 91
    • (1990) Protoplasma , vol.157 , pp. 75-91
    • Staehelin, L.A.1    Giddings Jr., T.H.2    Kiss, J.Z.3    Sack, F.D.4
  • 117
    • 1542370795 scopus 로고    scopus 로고
    • Identification of multivesicular bodies as prevacuolar compartments in Nicotiana tabacum BY-2 cells
    • Y.C. Tse, B. Mo, S. Hillmer, M. Zhao, S.W. Lo, D.G. Robinson, and L. Jiang Identification of multivesicular bodies as prevacuolar compartments in Nicotiana tabacum BY-2 cells Plant Cell 16 2004 672 693
    • (2004) Plant Cell , vol.16 , pp. 672-693
    • Tse, Y.C.1    Mo, B.2    Hillmer, S.3    Zhao, M.4    Lo, S.W.5    Robinson, D.G.6    Jiang, L.7
  • 119
    • 0035661728 scopus 로고    scopus 로고
    • Interactions between syntaxins identify at least five SNARE complexes within the Golgi/prevacuolar system of the Arabidopsis cell
    • A.A. Sanderfoot, V. Kovaleva, D.C. Bassham, and N.V. Raikhel Interactions between syntaxins identify at least five SNARE complexes within the Golgi/prevacuolar system of the Arabidopsis cell Mol. Biol. Cell 12 2001 3733 3743
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3733-3743
    • Sanderfoot, A.A.1    Kovaleva, V.2    Bassham, D.C.3    Raikhel, N.V.4
  • 120
    • 13444301232 scopus 로고    scopus 로고
    • AtRabF2b (Ara7) acts on the vacuolar trafficking pathway in tobacco leaf epidermal cells
    • A.M. Kotzer, F. Brandizzi, U. Neumann, N. Paris, I. Moore, and C. Hawes AtRabF2b (Ara7) acts on the vacuolar trafficking pathway in tobacco leaf epidermal cells J. Cell Sci. 117 2004 6377 6389
    • (2004) J. Cell Sci. , vol.117 , pp. 6377-6389
    • Kotzer, A.M.1    Brandizzi, F.2    Neumann, U.3    Paris, N.4    Moore, I.5    Hawes, C.6
  • 121
    • 0029965895 scopus 로고    scopus 로고
    • Brefeldin a effects in plant and fungal cells: Something new about vesicle trafficking?
    • B. Satiat-Jeunemaitre, L. Cole, T. Bourett, R. Howard, and C.R. Hawes Brefeldin A effects in plant and fungal cells: something new about vesicle trafficking? J. Microsc. 181 1996 162 177
    • (1996) J. Microsc. , vol.181 , pp. 162-177
    • Satiat-Jeunemaitre, B.1    Cole, L.2    Bourett, T.3    Howard, R.4    Hawes, C.R.5
  • 122
    • 3142683074 scopus 로고    scopus 로고
    • Targeting of a Nicotiana plumbaginifolia H+-ATPase to the plasma membrane is not by default and requires cytosolic structural determinants
    • B. Lefebvre, H. Batoko, G. Duby, and M. Boutry Targeting of a Nicotiana plumbaginifolia H+-ATPase to the plasma membrane is not by default and requires cytosolic structural determinants Plant Cell 16 2004 1772 1789
    • (2004) Plant Cell , vol.16 , pp. 1772-1789
    • Lefebvre, B.1    Batoko, H.2    Duby, G.3    Boutry, M.4
  • 123
    • 0033029795 scopus 로고    scopus 로고
    • Transport of virally expressed green fluorescent protein through the secretory pathway in tobacco leaves is inhibited by cold shock and Brefeldin a
    • P. Boevink, B. Martin, K.J. Oparka, S. Santa Cruz, and C. Hawes Transport of virally expressed green fluorescent protein through the secretory pathway in tobacco leaves is inhibited by cold shock and Brefeldin A Planta 208 1999 392 400
    • (1999) Planta , vol.208 , pp. 392-400
    • Boevink, P.1    Martin, B.2    Oparka, K.J.3    Santa Cruz, S.4    Hawes, C.5
  • 124
    • 12344317183 scopus 로고
    • Ultrastructural localisation of carbohydrates
    • J. Bailey Recent Developments in Cytochemistry and Affinity Methods Springer Verlag Berlin Heidelberg
    • B. Vian Ultrastructural localisation of carbohydrates J. Bailey Recent Developments in Cytochemistry and Affinity Methods NATO ASI Series vol. H1 1986 Springer Verlag Berlin Heidelberg 49 57
    • (1986) NATO ASI Series , vol.1 , pp. 49-57
    • Vian, B.1
  • 125
    • 0028003272 scopus 로고
    • Secretion of cell wall polysaccharides in Vicia root hairs
    • D.J. Sherrier, and K.A. Vanden Bosch Secretion of cell wall polysaccharides in Vicia root hairs Plant J. 5 1990 185 195
    • (1990) Plant J. , vol.5 , pp. 185-195
    • Sherrier, D.J.1    Vanden Bosch, K.A.2
  • 126
    • 0002679117 scopus 로고
    • Organisation of the secretory pathway of cell wall glycoproteins and complex poilysaccharides in plant cells
    • C. Hawes J. Coleman D. Evans Cambridge Univ. Press
    • L.A. Staehelin, T.H. Giddings, S. Levy, M.A Lynch, P.J. Moore, and K.M.M. Swords Organisation of the secretory pathway of cell wall glycoproteins and complex poilysaccharides in plant cells C. Hawes J. Coleman D. Evans Endocytosis, Exocytosis and Vesicle Traffic In Plants 1991 Cambridge Univ. Press 183 198
    • (1991) Endocytosis, Exocytosis and Vesicle Traffic in Plants , pp. 183-198
    • Staehelin, L.A.1    Giddings, T.H.2    Levy, S.3    Lynch, M.A.4    Moore, P.J.5    Swords, K.M.M.6
  • 127
    • 0033709686 scopus 로고    scopus 로고
    • Sorting of soluble proteins in the secretory pathway of plants
    • J.L. Hadlington, and J. Denecke Sorting of soluble proteins in the secretory pathway of plants Curr. Opin. Plant Biol. 3 2000 461 468
    • (2000) Curr. Opin. Plant Biol. , vol.3 , pp. 461-468
    • Hadlington, J.L.1    Denecke, J.2
  • 128
    • 0026903856 scopus 로고
    • Protein sorting to the vacuolar membrane
    • H. Hofte, and M.J. Chrispeels Protein sorting to the vacuolar membrane Plant Cell 4 1992 995 1004
    • (1992) Plant Cell , vol.4 , pp. 995-1004
    • Hofte, H.1    Chrispeels, M.J.2
  • 129
    • 0032894143 scopus 로고    scopus 로고
    • What do proteins need to reach different vacuoles?
    • A. Vitale, and N. Raikhel What do proteins need to reach different vacuoles? Trends Plant Sci. 4 1999 149 155
    • (1999) Trends Plant Sci. , vol.4 , pp. 149-155
    • Vitale, A.1    Raikhel, N.2
  • 130
    • 0036016439 scopus 로고    scopus 로고
    • The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain
    • F. Brandizzi, N. Frangne, S. Marc-Martin, C. Hawes, J.M. Neuhaus, and N. Paris N The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain Plant Cell 14 2002 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.M.5    Paris, N.N.6
  • 131
    • 0033593635 scopus 로고    scopus 로고
    • A tobaco syntaxin with a role in hormonal control of guard cell ion channels
    • B. Leymann, D. Geelen, F.J. Quintero, and M.R. Blatt A tobaco syntaxin with a role in hormonal control of guard cell ion channels Science 283 1999 537 540
    • (1999) Science , vol.283 , pp. 537-540
    • Leymann, B.1    Geelen, D.2    Quintero, F.J.3    Blatt, M.R.4
  • 132
    • 0035960024 scopus 로고    scopus 로고
    • Auxin transport inhibitors block PIN1 cycling and vesicle trafficking
    • N. Geldner, J. Friml, Y.D. Stierhof, G. Jürgens, and K. Palme Auxin transport inhibitors block PIN1 cycling and vesicle trafficking Nature 413 2001 425 428
    • (2001) Nature , vol.413 , pp. 425-428
    • Geldner, N.1    Friml, J.2    Stierhof, Y.D.3    Jürgens, G.4    Palme, K.5
  • 133
    • 0030034290 scopus 로고    scopus 로고
    • Cytokinesis in the Arabidopsis embryo involves the syntaxin-related KNOLLE gene products
    • W. Lukowitz, U. Mayer, and G. Jurgens Cytokinesis in the Arabidopsis embryo involves the syntaxin-related KNOLLE gene products Cell 84 1996 61 71
    • (1996) Cell , vol.84 , pp. 61-71
    • Lukowitz, W.1    Mayer, U.2    Jurgens, G.3
  • 134
    • 0036707863 scopus 로고    scopus 로고
    • Membrane trafficking during plant cytokinesis
    • S.Y. Bednarek, and T.G. Falbel Membrane trafficking during plant cytokinesis Traffic 3 2002 621 629
    • (2002) Traffic , vol.3 , pp. 621-629
    • Bednarek, S.Y.1    Falbel, T.G.2
  • 135
    • 8444251623 scopus 로고    scopus 로고
    • Cytokinesis: Membrane trafficking by default?
    • G. Jürgens, and T. Pacher Cytokinesis: membrane trafficking by default? Annu. Plant Rev. 9 2003 238 254
    • (2003) Annu. Plant Rev. , vol.9 , pp. 238-254
    • Jürgens, G.1    Pacher, T.2
  • 137
    • 0003603451 scopus 로고    scopus 로고
    • CSIRO publishing, Collinwood, Australia
    • D.N. De, Plant Cell Vacuoles, CSIRO publishing, Collinwood, Australia, 2000.
    • (2000) Plant Cell Vacuoles
    • De, D.N.1
  • 138
    • 0032583163 scopus 로고    scopus 로고
    • Integral membrane protein sorting to vacuoles in plant cells: Evidence for two pathways
    • L.W. Jiang, and J.C. Rogers Integral membrane protein sorting to vacuoles in plant cells: evidence for two pathways J. Cell Biol. 143 1998 1183 1199
    • (1998) J. Cell Biol. , vol.143 , pp. 1183-1199
    • Jiang, L.W.1    Rogers, J.C.2
  • 139
    • 0035825131 scopus 로고    scopus 로고
    • Vacuolar storage proteins are sorted in the cis-cisternae of the pea cotyledon Golgi apparatus
    • S. Hillmer, A. Movafeghi, D.G. Robinson, and G. Hinz Vacuolar storage proteins are sorted in the cis-cisternae of the pea cotyledon Golgi apparatus J. Cell Biol. 152 2001 41 50
    • (2001) J. Cell Biol. , vol.152 , pp. 41-50
    • Hillmer, S.1    Movafeghi, A.2    Robinson, D.G.3    Hinz, G.4
  • 140
    • 0032100925 scopus 로고    scopus 로고
    • Sorting of phaseolin to the vacuole is saturable and requires a short C-terminal peptide
    • L. Frigerio, M. de Virgilio, A. Prada, F. Faoro, and A. Vitale Sorting of phaseolin to the vacuole is saturable and requires a short C-terminal peptide Plant Cell 10 1998 1031 1042
    • (1998) Plant Cell , vol.10 , pp. 1031-1042
    • Frigerio, L.1    De Virgilio, M.2    Prada, A.3    Faoro, F.4    Vitale, A.5
  • 142
    • 0036909278 scopus 로고    scopus 로고
    • BP-80 as a vacuolar sorting receptor
    • N. Paris, and J.M. Neuhaus BP-80 as a vacuolar sorting receptor Plant Molec. Biol. 50 2002 903 914
    • (2002) Plant Molec. Biol. , vol.50 , pp. 903-914
    • Paris, N.1    Neuhaus, J.M.2
  • 143
    • 0034717573 scopus 로고    scopus 로고
    • The plant vacuolar sorting receptor AtELP is involved in transport of NH2-terminal propeptide-containing vacuolar proteins in Arabidopsis thaliana
    • S.U. Ahmed, E. Rokjo, S. Venkataraman, J.E. Dombrowski, K. Matsuoka, and N.V. Raikhel The plant vacuolar sorting receptor AtELP is involved in transport of NH2-terminal propeptide-containing vacuolar proteins in Arabidopsis thaliana J. Cell Biol. 149 2000 1335 1344
    • (2000) J. Cell Biol. , vol.149 , pp. 1335-1344
    • Ahmed, S.U.1    Rokjo, E.2    Venkataraman, S.3    Dombrowski, J.E.4    Matsuoka, K.5    Raikhel, N.V.6
  • 144
    • 0032699184 scopus 로고    scopus 로고
    • Vacuolar storage proteins and the putative vacuolar sorting receptor BP-80 exit the Golgi apparatus of developing pea cotyledons in different transport vesicles
    • G. Hinz, S. Hillmer, M. Baumer, and I. Hohl Vacuolar storage proteins and the putative vacuolar sorting receptor BP-80 exit the Golgi apparatus of developing pea cotyledons in different transport vesicles Plant Cell 11 1999 1509 1524
    • (1999) Plant Cell , vol.11 , pp. 1509-1524
    • Hinz, G.1    Hillmer, S.2    Baumer, M.3    Hohl, I.4
  • 145
    • 0033780821 scopus 로고    scopus 로고
    • Characterization of organelles in the vacuolar-sorting pathway by visualization with GFP in tobacco BY-2 cells
    • N. Mitsuhashi, T. Shimada, S. Mano, M. Nishimura, and I. Hara-Nishimura Characterization of organelles in the vacuolar-sorting pathway by visualization with GFP in tobacco BY-2 cells Plant Cell Physiol. 41 2000 993 1001
    • (2000) Plant Cell Physiol. , vol.41 , pp. 993-1001
    • Mitsuhashi, N.1    Shimada, T.2    Mano, S.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 150
    • 0008342761 scopus 로고
    • The morphology of multivesicular bodies in soybean protoplasts and their role in endocytosis
    • M.A. Tanchak, and L.C. Fowke The morphology of multivesicular bodies in soybean protoplasts and their role in endocytosis Protoplasma 138 1987 173 182
    • (1987) Protoplasma , vol.138 , pp. 173-182
    • Tanchak, M.A.1    Fowke, L.C.2
  • 151
    • 0001628825 scopus 로고
    • Endocytosis of cationized ferritin by coated vesicles of soybean protoplasts
    • M.A. Tanchak, L.R. Griffing, B.G. Mersey, and L.C. Fowke Endocytosis of cationized ferritin by coated vesicles of soybean protoplasts Planta 162 1984 481 486
    • (1984) Planta , vol.162 , pp. 481-486
    • Tanchak, M.A.1    Griffing, L.R.2    Mersey, B.G.3    Fowke, L.C.4
  • 152
    • 4944242360 scopus 로고    scopus 로고
    • Transport of ricin and 2S albumin precursors to the storage vacuoles of Ricinus comunis endosperm involves the Golgi and VSR-like receptors
    • N.A. Jolliffe, J.C. Brown, U. Neumann, M. Vicré, C. Hawes, A. Ceriotti, L.M. Roberts, and L. Frigerio Transport of ricin and 2S albumin precursors to the storage vacuoles of Ricinus comunis endosperm involves the Golgi and VSR-like receptors Plant J. 39 2004 821 833
    • (2004) Plant J. , vol.39 , pp. 821-833
    • Jolliffe, N.A.1    Brown, J.C.2    Neumann, U.3    Vicré, M.4    Hawes, C.5    Ceriotti, A.6    Roberts, L.M.7    Frigerio, L.8
  • 154
    • 0034923482 scopus 로고    scopus 로고
    • A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis
    • B.J. Jin, Y.A. Ki, S.J. Kim, S.H. Less, D.H. Kim, G.-W. Cheong, and I. Hwang A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis Plant Cell 13 2001 1511 1525
    • (2001) Plant Cell , vol.13 , pp. 1511-1525
    • Jin, B.J.1    Ki, Y.A.2    Kim, S.J.3    Less, S.H.4    Kim, D.H.5    Cheong, G.-W.6    Hwang, I.7
  • 155
    • 0028855261 scopus 로고
    • The plant Golgi apparatus: Structure, functional organization and trafficking mechanisms
    • L.A. Staehelin, and I. Moore The plant Golgi apparatus: structure, functional organization and trafficking mechanisms Annu. Rev. Plant Physiol. Plant Mol. Biol. 46 1995 261 288
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 261-288
    • Staehelin, L.A.1    Moore, I.2
  • 156
    • 0000337477 scopus 로고
    • Presence of a partially-coated reticulum in angiosperms
    • T.C. Pesacreta, and W.J. Lucas Presence of a partially-coated reticulum in angiosperms Protoplasma 125 1985 173 184
    • (1985) Protoplasma , vol.125 , pp. 173-184
    • Pesacreta, T.C.1    Lucas, W.J.2
  • 157
    • 0000066555 scopus 로고
    • The partially coated reticulum and its relationship to the Golgi apparatus in higher plants
    • S. Hillmer, H. Freundt, and D.G. Robinson The partially coated reticulum and its relationship to the Golgi apparatus in higher plants Eur. J. Cell Biol. 47 1988 206 212
    • (1988) Eur. J. Cell Biol. , vol.47 , pp. 206-212
    • Hillmer, S.1    Freundt, H.2    Robinson, D.G.3
  • 158
    • 0036799651 scopus 로고    scopus 로고
    • De novo formation of transitional ER sites and Golgi structures in Pichia pastoris
    • B.J. Bevis, A.T. Hammond, C.A. Reinke, and B.S. Glick De novo formation of transitional ER sites and Golgi structures in Pichia pastoris Nat. Cell Biol. 4 2002 750 756
    • (2002) Nat. Cell Biol. , vol.4 , pp. 750-756
    • Bevis, B.J.1    Hammond, A.T.2    Reinke, C.A.3    Glick, B.S.4
  • 160
    • 0010531422 scopus 로고
    • Intercisternal elements of the Golgi apparatus
    • F.R. Turner, and W.G. Whaley Intercisternal elements of the Golgi apparatus Science 147 1965 1303 1304
    • (1965) Science , vol.147 , pp. 1303-1304
    • Turner, F.R.1    Whaley, W.G.2
  • 161
    • 3142514373 scopus 로고    scopus 로고
    • The roles of enzyme localisation and complex formation in glycan assembly within the Golgi apparatus
    • C.L. de Graffenried, and C.R. Bertozzi The roles of enzyme localisation and complex formation in glycan assembly within the Golgi apparatus Curr. Opin. Cell Biol. 16 2004 356 363
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 356-363
    • De Graffenried, C.L.1    Bertozzi, C.R.2
  • 162
    • 0013085340 scopus 로고    scopus 로고
    • Golgins in the structure and dynamics of the Golgi apparatus
    • F.A. Barr, and B. Short Golgins in the structure and dynamics of the Golgi apparatus Curr. Opin. Cell Biol. 15 2003 403 416
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 403-416
    • Barr, F.A.1    Short, B.2
  • 163
    • 0033667627 scopus 로고    scopus 로고
    • The growing Golgi: In search of its independence
    • J. Klumperman The growing Golgi: in search of its independence Nat. Cell Biol. 2 2000 E1 E2
    • (2000) Nat. Cell Biol. , vol.2
    • Klumperman, J.1
  • 164
    • 0033938963 scopus 로고    scopus 로고
    • Transport between ER and Golgi
    • J. Klumperman Transport between ER and Golgi Curr. Opin. Cell Biol. 12 2000 445 449
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 445-449
    • Klumperman, J.1
  • 165
    • 0842309131 scopus 로고    scopus 로고
    • ER- to -Golgi transport and cytoskeletal interactions in animal cells
    • A. Murshid, and J.F. Presley ER- to -Golgi transport and cytoskeletal interactions in animal cells Cell. Mol. Life Sci. 61 2004 133 145
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 133-145
    • Murshid, A.1    Presley, J.F.2
  • 166
    • 1642506308 scopus 로고    scopus 로고
    • Genome-wide identification of Arabidopsis coiled-coil proteins and establishment of the ARABI-COIL database
    • A. Rose, M. Sankaraganesh, S.J. Schraegle, M.A. Maloy, E.A. Stahlberg, and I. Meier Genome-wide identification of Arabidopsis coiled-coil proteins and establishment of the ARABI-COIL database Plant Physiol. 134 2004 927 939
    • (2004) Plant Physiol. , vol.134 , pp. 927-939
    • Rose, A.1    Sankaraganesh, M.2    Schraegle, S.J.3    Maloy, M.A.4    Stahlberg, E.A.5    Meier, I.6


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