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Volumn 46, Issue 1, 2006, Pages 95-110

In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery

Author keywords

Anterograde transport; COPI; Endoplasmic reticulum export sites

Indexed keywords

FLUORESCENCE; PLANT CELL CULTURE; PLANTS (BOTANY); TOBACCO;

EID: 33646832927     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2006.02675.x     Document Type: Article
Times cited : (89)

References (56)
  • 2
    • 0035423555 scopus 로고    scopus 로고
    • ER export: Public transportation by the COPII coach
    • Antonny B. Schekman R. 2001 ER export: public transportation by the COPII coach. Curr. Opin. Cell Biol. 13, 438 443.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 438-443
    • Antonny, B.1    Schekman, R.2
  • 3
    • 0031131603 scopus 로고    scopus 로고
    • Characterization of AtSEC12 and AtSAR1. Proteins likely involved in endoplasmic reticulum and Golgi transport
    • Bar-Peled M. Raikhel N.V. 1997 Characterization of AtSEC12 and AtSAR1. Proteins likely involved in endoplasmic reticulum and Golgi transport. Plant Physiol. 114, 315 324.
    • (1997) Plant Physiol. , vol.114 , pp. 315-324
    • Bar-Peled, M.1    Raikhel, N.V.2
  • 4
    • 0036701908 scopus 로고    scopus 로고
    • COPII-dependent transport from the endoplasmic reticulum
    • Barlowe C. 2002a COPII-dependent transport from the endoplasmic reticulum. Curr. Opin. Cell Biol. 14, 417 422.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 417-422
    • Barlowe, C.1
  • 5
    • 0036775934 scopus 로고    scopus 로고
    • Three-dimensional structure of a COPII prebudding complex
    • Barlowe C. 2002b Three-dimensional structure of a COPII prebudding complex. Dev Cell, 3, 467 468.
    • (2002) Dev Cell , vol.3 , pp. 467-468
    • Barlowe, C.1
  • 6
    • 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
    • Batoko H. Zheng H.Q. Hawes C. Moore I. 2000 A rab1 GTPase is required for transport between the endoplasmic reticulum and Golgi apparatus and for normal Golgi movement in plants. Plant Cell, 12, 2201 2218.
    • (2000) Plant Cell , vol.12 , pp. 2201-2218
    • Batoko, H.1    Zheng, H.Q.2    Hawes, C.3    Moore, I.4
  • 7
    • 0037136560 scopus 로고    scopus 로고
    • Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat
    • Bi X. Corpina R.A. Goldberg J. 2002 Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat. Nature, 419, 271 277.
    • (2002) Nature , vol.419 , pp. 271-277
    • Bi, X.1    Corpina, R.A.2    Goldberg, J.3
  • 9
    • 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.L. Roberts A.G. Lippincott-Schwartz J. Hawes C. 2002 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.L.2    Roberts, A.G.3    Lippincott-Schwartz, J.4    Hawes, C.5
  • 11
    • 0043262923 scopus 로고    scopus 로고
    • Identification and localization of a beta-COP-like protein involved in the morphodynamics of the plant Golgi apparatus
    • Couchy I. Bolte S. Crosnier M.T. Brown S. Satiat-Jeunemaitre B. 2003 Identification and localization of a beta-COP-like protein involved in the morphodynamics of the plant Golgi apparatus. J. Exp. Bot. 54, 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
  • 13
    • 0026523624 scopus 로고
    • Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope
    • Denecke J. De Rycke R. Botterman J. 1992 Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope. EMBO J. 11, 2345 2355.
    • (1992) EMBO J. , vol.11 , pp. 2345-2355
    • Denecke, J.1    De Rycke, R.2    Botterman, J.3
  • 14
    • 0036715728 scopus 로고    scopus 로고
    • The Golgi localization of Arabidopsis thaliana beta1,2-xylosyltransferase in plant cells is dependent on its cytoplasmic and transmembrane sequences
    • Dirnberger D. Bencur P. Mach L. Steinkellner H. 2002 The Golgi localization of Arabidopsis thaliana beta1,2-xylosyltransferase in plant cells is dependent on its cytoplasmic and transmembrane sequences. Plant Mol. Biol. 50, 273 281.
    • (2002) Plant Mol. Biol. , vol.50 , pp. 273-281
    • Dirnberger, D.1    Bencur, P.2    MacH, L.3    Steinkellner, H.4
  • 17
    • 15844404207 scopus 로고    scopus 로고
    • Crossing the divide - Transport between the endoplasmic reticulum and Golgi apparatus in plants
    • Hanton S.L. Bortolotti L.E. Renna L. Stefano G. Brandizzi F. 2005 Crossing the divide - transport between the endoplasmic reticulum and Golgi apparatus in plants. Traffic, 6, 267 277 Hodge S. 1997 Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly. Proc. Natl Acad. Sci. USA, 94, 2122 2127.
    • (2005) Traffic , vol.6 , pp. 267-277
    • Hanton, S.L.1    Bortolotti, L.E.2    Renna, L.3    Stefano, G.4    Brandizzi, F.5
  • 18
    • 23844519400 scopus 로고    scopus 로고
    • The plant Golgi apparatus - Going with the flow
    • Hawes C. Satiat-Jeunemaitre B. 2005 The plant Golgi apparatus - going with the flow. Biochim. Biophys. Acta, 1744, 466 480.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 466-480
    • Hawes, C.1    Satiat-Jeunemaitre, B.2
  • 20
    • 9444272907 scopus 로고    scopus 로고
    • MRNA localization and ER-based protein sorting mechanisms dictate the use of transitional endoplasmic reticulum-Golgi units involved in gurken transport in Drosophila oocytes
    • Herpers B. Rabouille C. 2004 mRNA localization and ER-based protein sorting mechanisms dictate the use of transitional endoplasmic reticulum-Golgi units involved in gurken transport in Drosophila oocytes. Mol. Biol. Cell, 15, 5306 5317.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5306-5317
    • Herpers, B.1    Rabouille, C.2
  • 21
    • 0042672956 scopus 로고    scopus 로고
    • A novel role for dp115 in the organization of tER sites in Drosophila
    • Kondylis V. Rabouille C. 2003 A novel role for dp115 in the organization of tER sites in Drosophila. J. Cell Biol. 162, 185 198.
    • (2003) J. Cell Biol. , vol.162 , pp. 185-198
    • Kondylis, V.1    Rabouille, C.2
  • 22
    • 13444301232 scopus 로고    scopus 로고
    • AtRabF2b (Ara7) acts on the vacuolar trafficking pathway in tobacco leaf epidermal cells
    • Kotzer A.M. Brandizzi F. Neumann U. Paris N. Moore I. Hawes C. 2004 AtRabF2b (Ara7) acts on the vacuolar trafficking pathway in tobacco leaf epidermal cells. J. Cell Sci. 117, 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
  • 24
    • 0027361048 scopus 로고
    • The Arabidopsis endoplasmic reticulum retention receptor functions in yeast
    • Lee H.I. Gal S. Newman T.C. Raikhel N.V. 1993 The Arabidopsis endoplasmic reticulum retention receptor functions in yeast. Proc. Natl Acad. Sci. USA, 90, 11433 11437.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11433-11437
    • Lee, H.I.1    Gal, S.2    Newman, T.C.3    Raikhel, N.V.4
  • 25
    • 0037008335 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 of Arabidopsis plays a critical role in intracellular trafficking and maintenance of endoplasmic reticulum morphology in Arabidopsis
    • Lee M.H. Min M.K. Lee Y.J. Jin J.B. Shin D.H. Kim D.H. Lee K.H. Hwang I. 2002 ADP-ribosylation factor 1 of Arabidopsis plays a critical role in intracellular trafficking and maintenance of endoplasmic reticulum morphology in Arabidopsis. Plant Physiol. 129, 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
  • 26
    • 0037418882 scopus 로고    scopus 로고
    • Development and use of fluorescent protein markers in living cells
    • Lippincott-Schwartz J. Patterson G.H. 2003 Development and use of fluorescent protein markers in living cells. Science, 300, 87 91.
    • (2003) Science , vol.300 , pp. 87-91
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 28
    • 3042689728 scopus 로고    scopus 로고
    • The role of ADP-ribosylation factor and SAR1 in vesicular trafficking in plants
    • Memon A.R. 2004 The role of ADP-ribosylation factor and SAR1 in vesicular trafficking in plants. Biochim. Biophys. Acta, 1664, 9 30.
    • (2004) Biochim. Biophys. Acta , vol.1664 , pp. 9-30
    • Memon, A.R.1
  • 29
    • 0037112755 scopus 로고    scopus 로고
    • Cargo selection into COPII vesicles is driven by the Sec24p subunit
    • Miller E. Antonny B. Hamamoto S. Schekman R. 2002 Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J. 21, 6105 6113.
    • (2002) EMBO J. , vol.21 , pp. 6105-6113
    • Miller, E.1    Antonny, B.2    Hamamoto, S.3    Schekman, R.4
  • 31
    • 0033117623 scopus 로고    scopus 로고
    • Arabidopsis Sec21p and Sec23p homologs. Probable coat proteins of plant COP-coated vesicles
    • Movafeghi A. Happel N. Pimpl P. Tai G.H. Robinson D.G. 1999 Arabidopsis Sec21p and Sec23p homologs. Probable coat proteins of plant COP-coated vesicles. Plant Physiol. 119, 1437 1446.
    • (1999) Plant Physiol. , vol.119 , pp. 1437-1446
    • Movafeghi, A.1    Happel, N.2    Pimpl, P.3    Tai, G.H.4    Robinson, D.G.5
  • 34
    • 0038366776 scopus 로고    scopus 로고
    • The GTPase ARF1p controls the sequence-specific vacuolar sorting route to the lytic vacuole
    • Pimpl P. Hanton S.L. Taylor J.P. Pinto-daSilva L.L. Denecke J. 2003 The GTPase ARF1p controls the sequence-specific vacuolar sorting route to the lytic vacuole. Plant Cell, 15, 1242 1256.
    • (2003) Plant Cell , vol.15 , pp. 1242-1256
    • Pimpl, P.1    Hanton, S.L.2    Taylor, J.P.3    Pinto-Dasilva, L.L.4    Denecke, J.5
  • 37
    • 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
    • Ritzenthaler C. Nebenführ A. Movafeghi A. Stussi-Garaud C. Behnia L. Pimpl P. Staehelin L.A. Robinson D.G. 2002 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, 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
  • 38
    • 0034730123 scopus 로고    scopus 로고
    • Binding site of brefeldin a at the interface between the small G protein ADP-ribosylation factor 1 (ARF1) and the nucleotide-exchange factor Sec7 domain
    • Robineau S. Chabre M. Antonny B. 2000 Binding site of brefeldin A at the interface between the small G protein ADP-ribosylation factor 1 (ARF1) and the nucleotide-exchange factor Sec7 domain. Proc. Natl Acad. Sci. USA, 97, 9913 9918.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9913-9918
    • Robineau, S.1    Chabre, M.2    Antonny, B.3
  • 39
    • 0026627966 scopus 로고
    • Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: Effects of brefeldin a and G protein activators
    • Robinson M.S. Kreis T.E. 1992 Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators. Cell, 69, 129 138.
    • (1992) Cell , vol.69 , pp. 129-138
    • Robinson, M.S.1    Kreis, T.E.2
  • 40
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae
    • Rossanese O.W. Soderholm J. Bevis B.J. Sears I.B. O'Connor J. Williamson E.K. Glick B.S. 1999 Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J. Cell Biol. 145, 69 81.
    • (1999) J. Cell Biol. , vol.145 , pp. 69-81
    • Rossanese, O.W.1    Soderholm, J.2    Bevis, B.J.3    Sears, I.B.4    O'Connor, J.5    Williamson, E.K.6    Glick, B.S.7
  • 41
    • 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
    • Saint-Jore C.M. Evins J. Batoko H. Brandizzi F. Moore I. Hawes C. 2002 Redistribution of membrane proteins between the Golgi apparatus and endoplasmic reticulum in plants is reversible and not dependent on cytoskeletal networks. Plant J. 29, 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
  • 42
    • 0034525262 scopus 로고    scopus 로고
    • Cell wall alterations in the Arabidopsis emb30 mutant
    • Shevell D.E. Kunkel T. Chua N.H. 2000 Cell wall alterations in the Arabidopsis emb30 mutant. Plant Cell, 12, 2047 2060.
    • (2000) Plant Cell , vol.12 , pp. 2047-2060
    • Shevell, D.E.1    Kunkel, T.2    Chua, N.H.3
  • 43
    • 3142706602 scopus 로고    scopus 로고
    • Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells
    • daSilva L.L. Snapp E.L. Denecke J. Lippincott-Schwartz J. Hawes C. Brandizzi F. 2004 Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells. Plant Cell, 16, 1753 1771.
    • (2004) Plant Cell , vol.16 , pp. 1753-1771
    • Dasilva, L.L.1    Snapp, E.L.2    Denecke, J.3    Lippincott-Schwartz, J.4    Hawes, C.5    Brandizzi, F.6
  • 44
    • 0347683331 scopus 로고    scopus 로고
    • An Arabidopsis pex10 null mutant is embryo lethal, implicating peroxisomes in an essential role during plant embryogenesis
    • Sparkes I.A. Brandizzi F. Slocombe S.P. El-Shami M. Hawes C. Baker A. 2003 An Arabidopsis pex10 null mutant is embryo lethal, implicating peroxisomes in an essential role during plant embryogenesis. Plant Physiol. 133, 1809 1819.
    • (2003) Plant Physiol. , vol.133 , pp. 1809-1819
    • Sparkes, I.A.1    Brandizzi, F.2    Slocombe, S.P.3    El-Shami, M.4    Hawes, C.5    Baker, A.6
  • 45
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes M.A. Rothman J.E. 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
  • 46
    • 0037087610 scopus 로고    scopus 로고
    • Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells
    • Stephens D.J. 2003 De novo formation, fusion and fission of mammalian COPII-coated endoplasmic reticulum exit sites. EMBO Rep. 4, 210 217 Pepperkok R. 2002 Imaging of procollagen transport reveals COPI-dependent cargo sorting during ER-to-Golgi transport in mammalian cells. J. Cell Sci. 115, 1149 1160.
    • (2002) J. Cell Sci. , vol.115 , pp. 1149-1160
    • Stephens, D.J.1    Pepperkok, R.2
  • 47
    • 0033917563 scopus 로고    scopus 로고
    • COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites
    • Stephens D.J. Lin-Marq N. Pagano A. Pepperkok R. Paccaud J.P. 2000 COPI-coated ER-to-Golgi transport complexes segregate from COPII in close proximity to ER exit sites. J. Cell Sci. 113, 2177 2185.
    • (2000) J. Cell Sci. , vol.113 , pp. 2177-2185
    • Stephens, D.J.1    Lin-Marq, N.2    Pagano, A.3    Pepperkok, R.4    Paccaud, J.P.5
  • 48
    • 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 cultured cells
    • Takeuchi M. Ueda T. Sato K. Abe H. Nagata T. Nakano A. 2000 A dominant negative mutant of sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells. Plant J. 23, 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
  • 49
    • 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
    • Takeuchi M. Ueda T. Yahara N. Nakano A. 2002 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, 499 515.
    • (2002) Plant J. , vol.31 , pp. 499-515
    • Takeuchi, M.1    Ueda, T.2    Yahara, N.3    Nakano, A.4
  • 50
    • 0028124181 scopus 로고
    • An activating mutation in ARF1 stabilizes coatomer binding to Golgi membranes
    • Teal S.B. Hsu V.W. Peters P.J. Klausner R.D. Donaldson J.G. 1994 An activating mutation in ARF1 stabilizes coatomer binding to Golgi membranes. J. Biol. Chem. 269, 3135 3138.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3135-3138
    • Teal, S.B.1    Hsu, V.W.2    Peters, P.J.3    Klausner, R.D.4    Donaldson, J.G.5
  • 51
    • 4444309237 scopus 로고    scopus 로고
    • Systematic analysis of SNARE molecules in Arabidopsis: Dissection of the post-Golgi network in plant cells
    • Uemura T. Ueda T. Ohniwa R.L. Nakano A. Takeyasu K. Sato M.H. 2004 Systematic analysis of SNARE molecules in Arabidopsis: dissection of the post-Golgi network in plant cells. Cell Struct. Funct. 29, 49 65.
    • (2004) Cell Struct. Funct. , vol.29 , pp. 49-65
    • Uemura, T.1    Ueda, T.2    Ohniwa, R.L.3    Nakano, A.4    Takeyasu, K.5    Sato, M.H.6
  • 52
    • 0031802483 scopus 로고    scopus 로고
    • The distribution and translocation of the G protein ADP-ribosylation factor 1 in live cells is determined by its GTPase activity
    • Vasudevan C. Han W. Tan Y. Nie Y. Li D. Shome K. Watkins S.C. Levitan E.S. Romero G. 1998 The distribution and translocation of the G protein ADP-ribosylation factor 1 in live cells is determined by its GTPase activity. J. Cell Sci. 111, 1277 1285.
    • (1998) J. Cell Sci. , vol.111 , pp. 1277-1285
    • Vasudevan, C.1    Han, W.2    Tan, Y.3    Nie, Y.4    Li, D.5    Shome, K.6    Watkins, S.C.7    Levitan, E.S.8    Romero, G.9
  • 55
    • 21744446803 scopus 로고    scopus 로고
    • Dissection of Arabidopsis ADP-RIBOSYLATION FACTOR 1 function in epidermal cell polarity
    • Xu J. Scheres B. 2005 Dissection of Arabidopsis ADP-RIBOSYLATION FACTOR 1 function in epidermal cell polarity. Plant Cell, 17, 525 536.
    • (2005) Plant Cell , vol.17 , pp. 525-536
    • Xu, J.1    Scheres, B.2
  • 56
    • 26844472700 scopus 로고    scopus 로고
    • Visualization of COPII and Golgi dynamics in Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with ER exit sites
    • Yang Y.D. El Amawi R. Bubeck J. Pepperkok R. Ritzenthaler C. Robinson D.G. 2005 Visualization of COPII and Golgi dynamics in Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with ER exit sites. Plant Cell, 17, 1513 1531.
    • (2005) Plant Cell , vol.17 , pp. 1513-1531
    • Yang, Y.D.1    El Amawi, R.2    Bubeck, J.3    Pepperkok, R.4    Ritzenthaler, C.5    Robinson, D.G.6


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