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Volumn 583, Issue 23, 2009, Pages 3752-3757

The plant Golgi apparatus: Last 10 years of answered and open questions

Author keywords

Endoplasmic reticulum; ER export site; Golgi; Golgin

Indexed keywords

CELL DIVISION; CELL FUNCTION; CELL STRUCTURE; CELL TRANSPORT; CELL VACUOLE; CELL WALL; CHLOROPLAST; ENDOPLASMIC RETICULUM; GOLGI COMPLEX; NONHUMAN; PLANT BIOTECHNOLOGY; PLANT METABOLISM; PRIORITY JOURNAL; PROTEIN TRANSPORT; REVIEW;

EID: 70450223698     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.09.046     Document Type: Review
Times cited : (38)

References (69)
  • 1
    • 47249152709 scopus 로고    scopus 로고
    • Targeting of nucleus-encoded proteins to chloroplasts in plants
    • Jarvis P. Targeting of nucleus-encoded proteins to chloroplasts in plants. New Phytol. 179 (2008) 257-285
    • (2008) New Phytol. , vol.179 , pp. 257-285
    • Jarvis, P.1
  • 2
    • 33749563351 scopus 로고    scopus 로고
    • Traffic between the plant endoplasmic reticulum and Golgi apparatus: to the Golgi and beyond
    • Matheson L.A., Hanton S.L., and Brandizzi F. Traffic between the plant endoplasmic reticulum and Golgi apparatus: to the Golgi and beyond. Curr. Opin. Plant Biol. 9 (2006) 601-609
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 601-609
    • Matheson, L.A.1    Hanton, S.L.2    Brandizzi, F.3
  • 3
    • 28544447361 scopus 로고    scopus 로고
    • Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast
    • Villarejo A., et al. Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast. Nat. Cell Biol. 7 (2005) 1224-1231
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1224-1231
    • Villarejo, A.1
  • 4
    • 33750974169 scopus 로고    scopus 로고
    • Rice plastidial N-glycosylated nucleotide pyrophosphatase/phosphodiesterase is transported from the ER-Golgi to the chloroplast through the secretory pathway
    • Nanjo Y., et al. Rice plastidial N-glycosylated nucleotide pyrophosphatase/phosphodiesterase is transported from the ER-Golgi to the chloroplast through the secretory pathway. Plant Cell 18 (2006) 2582-2592
    • (2006) Plant Cell , vol.18 , pp. 2582-2592
    • Nanjo, Y.1
  • 5
    • 33746368041 scopus 로고    scopus 로고
    • Evidence for an ER to Golgi to chloroplast protein transport pathway
    • Radhamony R., and Theg S. Evidence for an ER to Golgi to chloroplast protein transport pathway. Trends Cell Biol. 16 (2006) 385-387
    • (2006) Trends Cell Biol. , vol.16 , pp. 385-387
    • Radhamony, R.1    Theg, S.2
  • 6
    • 51849157397 scopus 로고    scopus 로고
    • Intermediate organelles of the plant secretory pathway: identity and function
    • Foresti O., and Denecke J. Intermediate organelles of the plant secretory pathway: identity and function. Traffic 9 (2008) 1599-1612
    • (2008) Traffic , vol.9 , pp. 1599-1612
    • Foresti, O.1    Denecke, J.2
  • 7
    • 43549085350 scopus 로고    scopus 로고
    • Rab-A2 and Rab-A3 GTPases define a trans-Golgi endosomal membrane domain in Arabidopsis that contributes substantially to the cell plate
    • Chow C., Neto H., Foucart C., and Moore I. Rab-A2 and Rab-A3 GTPases define a trans-Golgi endosomal membrane domain in Arabidopsis that contributes substantially to the cell plate. Plant Cell 20 (2008) 101-123
    • (2008) Plant Cell , vol.20 , pp. 101-123
    • Chow, C.1    Neto, H.2    Foucart, C.3    Moore, I.4
  • 8
    • 37249010561 scopus 로고    scopus 로고
    • Correct targeting of plant ARF GTPases relies on distinct protein domains
    • Matheson L., Suri S., Hanton S., Chatre L., and Brandizzi F. Correct targeting of plant ARF GTPases relies on distinct protein domains. Traffic 9 (2008) 103-120
    • (2008) Traffic , vol.9 , pp. 103-120
    • Matheson, L.1    Suri, S.2    Hanton, S.3    Chatre, L.4    Brandizzi, F.5
  • 9
    • 0034808250 scopus 로고    scopus 로고
    • A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum
    • Tormakangas K., Hadlington J.L., Pimpl P., Hillmer S., Brandizzi F., Teeri T.H., and Denecke J. A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum. Plant Cell 13 (2001) 2021-2032
    • (2001) Plant Cell , vol.13 , pp. 2021-2032
    • Tormakangas, K.1    Hadlington, J.L.2    Pimpl, P.3    Hillmer, S.4    Brandizzi, F.5    Teeri, T.H.6    Denecke, J.7
  • 10
    • 3142706602 scopus 로고    scopus 로고
    • Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells
    • DaSilva L.L.P., Snapp E.L., Denecke J., Lippincott-Schwartz J., Hawes C., and Brandizzi F. Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells. Plant cell 16 (2004) 1753-1771
    • (2004) Plant cell , vol.16 , pp. 1753-1771
    • DaSilva, L.L.P.1    Snapp, E.L.2    Denecke, J.3    Lippincott-Schwartz, J.4    Hawes, C.5    Brandizzi, F.6
  • 12
    • 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., and Nakano A. 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 (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
  • 13
    • 26844472700 scopus 로고    scopus 로고
    • Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites
    • Yang Y.D., Elamawi R., Bubeck J., Pepperkok R., Ritzenthaler C., and Robinson D.G. Dynamics of COPII vesicles and the Golgi apparatus in cultured Nicotiana tabacum BY-2 cells provides evidence for transient association of Golgi stacks with endoplasmic reticulum exit sites. Plant Cell 17 (2005) 1513-1531
    • (2005) Plant Cell , vol.17 , pp. 1513-1531
    • Yang, Y.D.1    Elamawi, R.2    Bubeck, J.3    Pepperkok, R.4    Ritzenthaler, C.5    Robinson, D.G.6
  • 16
    • 34249823659 scopus 로고    scopus 로고
    • Multiple roles of ADP-ribosylation factor 1 in plant cells include spatially regulated recruitment of coatomer and elements of the Golgi matrix
    • Matheson L.A., Hanton S.L., Rossi M., Latijnhouwers M., Stefano G., Renna L., and Brandizzi F. Multiple roles of ADP-ribosylation factor 1 in plant cells include spatially regulated recruitment of coatomer and elements of the Golgi matrix. Plant Physiol. 143 (2007) 1615-1627
    • (2007) Plant Physiol. , vol.143 , pp. 1615-1627
    • Matheson, L.A.1    Hanton, S.L.2    Rossi, M.3    Latijnhouwers, M.4    Stefano, G.5    Renna, L.6    Brandizzi, F.7
  • 17
    • 2542632045 scopus 로고    scopus 로고
    • Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer
    • Contreras I., Ortiz-Zapater E., and Aniento F. 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
  • 18
    • 0027361048 scopus 로고
    • The Arabidopsis endoplasmic-reticulum retention receptor functions in yeast
    • Lee H.I., Gal S., Newman T.C., and Raikhel N.V. The Arabidopsis endoplasmic-reticulum retention receptor functions in yeast. Proc. Natl. Acad. Sci. USA 90 (1993) 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
  • 19
    • 0026752711 scopus 로고
    • Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic reticulum
    • Napier R.M., Fowke L.C., Hawes C., Lewis M., and Pelham H.R. Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic reticulum. J. Cell Sci. 102 Pt 2 (1992) 261-271
    • (1992) J. Cell Sci. , vol.102 , Issue.PART 2 , pp. 261-271
    • Napier, R.M.1    Fowke, L.C.2    Hawes, C.3    Lewis, M.4    Pelham, H.R.5
  • 20
    • 0038029881 scopus 로고    scopus 로고
    • ER quality control can lead to retrograde transport from the ER lumen to the cytosol and the nucleoplasm in plants
    • Brandizzi F., Hanton S., DaSilva L.L., Boevink P., Evans D., Oparka K., Denecke J., and Hawes C. ER quality control can lead to retrograde transport from the ER lumen to the cytosol and the nucleoplasm in plants. Plant J. 34 (2003) 269-281
    • (2003) Plant J. , vol.34 , pp. 269-281
    • Brandizzi, F.1    Hanton, S.2    DaSilva, L.L.3    Boevink, P.4    Evans, D.5    Oparka, K.6    Denecke, J.7    Hawes, C.8
  • 21
    • 0032144201 scopus 로고    scopus 로고
    • Stacks on tracks: the plant Golgi apparatus traffics on an actin/ER network
    • Boevink P., Oparka K., Cruz S.S., Martin B., Betteridge A., and Hawes C. Stacks on tracks: the plant Golgi apparatus traffics on an actin/ER network. Plant J. 15 (1998) 441-447
    • (1998) Plant J. , vol.15 , pp. 441-447
    • Boevink, P.1    Oparka, K.2    Cruz, S.S.3    Martin, B.4    Betteridge, A.5    Hawes, C.6
  • 22
    • 33645968400 scopus 로고    scopus 로고
    • Diacidic motifs influence the export of transmembrane proteins from the endoplasmic reticulum in plant cells
    • Hanton S.L., Renna L., Bortolotti L.E., Chatre L., Stefano G., and Brandizzi F. Diacidic motifs influence the export of transmembrane proteins from the endoplasmic reticulum in plant cells. Plant Cell 17 (2005) 3081-3093
    • (2005) Plant Cell , vol.17 , pp. 3081-3093
    • Hanton, S.L.1    Renna, L.2    Bortolotti, L.E.3    Chatre, L.4    Stefano, G.5    Brandizzi, F.6
  • 23
    • 12744261335 scopus 로고    scopus 로고
    • Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum
    • Yuasa K., Toyooka K., Fukuda H., and Matsuoka K. Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum. Plant J. 41 (2005) 81-94
    • (2005) Plant J. , vol.41 , pp. 81-94
    • Yuasa, K.1    Toyooka, K.2    Fukuda, H.3    Matsuoka, K.4
  • 24
    • 12444339783 scopus 로고    scopus 로고
    • Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat
    • Contreras I., Yang Y., Robinson D., and Aniento F. Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat. Plant Cell Physiol. 45 (2004) 1779-1786
    • (2004) Plant Cell Physiol. , vol.45 , pp. 1779-1786
    • Contreras, I.1    Yang, Y.2    Robinson, D.3    Aniento, F.4
  • 25
    • 33845762779 scopus 로고    scopus 로고
    • Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway
    • Saint-Jore-Dupas C., et al. Plant N-glycan processing enzymes employ different targeting mechanisms for their spatial arrangement along the secretory pathway. Plant Cell 18 (2006) 3182-3200
    • (2006) Plant Cell , vol.18 , pp. 3182-3200
    • Saint-Jore-Dupas, C.1
  • 26
    • 0033883172 scopus 로고    scopus 로고
    • The C-terminal dilysine motif confers endoplasmic reticulum localization to type I membrane proteins in plants
    • Benghezal M., Wasteneys G., and Jones D. The C-terminal dilysine motif confers endoplasmic reticulum localization to type I membrane proteins in plants. Plant Cell 12 (2000) 1179-1201
    • (2000) Plant Cell , vol.12 , pp. 1179-1201
    • Benghezal, M.1    Wasteneys, G.2    Jones, D.3
  • 27
    • 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., and Hawes C. 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
  • 28
  • 31
    • 57249095874 scopus 로고    scopus 로고
    • ER-to-Golgi transport by COPII vesicles in Arabidopsis involves a ribosome-excluding scaffold that is transferred with the vesicles to the Golgi matrix
    • Kang B.H., and Staehelin L.A. ER-to-Golgi transport by COPII vesicles in Arabidopsis involves a ribosome-excluding scaffold that is transferred with the vesicles to the Golgi matrix. Protoplasma 234 (2008) 51-64
    • (2008) Protoplasma , vol.234 , pp. 51-64
    • Kang, B.H.1    Staehelin, L.A.2
  • 33
    • 0037355147 scopus 로고    scopus 로고
    • The relationship between endomembranes and the plant cytoskeleton
    • Brandizzi F., Saint-Jore C., Moore I., and Hawes C. The relationship between endomembranes and the plant cytoskeleton. Cell Biol. Int. 27 (2003) 177-179
    • (2003) Cell Biol. Int. , vol.27 , pp. 177-179
    • Brandizzi, F.1    Saint-Jore, C.2    Moore, I.3    Hawes, C.4
  • 34
    • 29344456761 scopus 로고    scopus 로고
    • Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane
    • Runions J., Brach T., Kuhner S., and Hawes C. Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane. J. Exp. Bot. 57 (2006) 43-50
    • (2006) J. Exp. Bot. , vol.57 , pp. 43-50
    • Runions, J.1    Brach, T.2    Kuhner, S.3    Hawes, C.4
  • 36
    • 62149130111 scopus 로고    scopus 로고
    • Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells
    • Hanton S., Matheson L., Chatre L., and Brandizzi F. Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells. Plant J. 57 (2009) 963-974
    • (2009) Plant J. , vol.57 , pp. 963-974
    • Hanton, S.1    Matheson, L.2    Chatre, L.3    Brandizzi, F.4
  • 37
    • 51849151243 scopus 로고    scopus 로고
    • The syntaxins SYP31 and SYP81 control ER-Golgi trafficking in the plant secretory pathway
    • Bubeck J., et al. The syntaxins SYP31 and SYP81 control ER-Golgi trafficking in the plant secretory pathway. Traffic 9 (2008) 1629-1652
    • (2008) Traffic , vol.9 , pp. 1629-1652
    • Bubeck, J.1
  • 38
    • 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., Nebenfuhr A., Movafeghi A., Stussi-Garaud C., Behnia L., Pimpl P., Staehelin L.A., and Robinson D.G. 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    Nebenfuhr, A.2    Movafeghi, A.3    Stussi-Garaud, C.4    Behnia, L.5    Pimpl, P.6    Staehelin, L.A.7    Robinson, D.G.8
  • 39
    • 33646832927 scopus 로고    scopus 로고
    • In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery
    • Stefano G., Renna L., Chatre L., Hanton S.L., Moreau P., Hawes C., and Brandizzi F. In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery. Plant J. 46 (2006) 95-110
    • (2006) Plant J. , vol.46 , pp. 95-110
    • Stefano, G.1    Renna, L.2    Chatre, L.3    Hanton, S.L.4    Moreau, P.5    Hawes, C.6    Brandizzi, F.7
  • 40
    • 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., and Hawes C. 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
  • 41
    • 34249785671 scopus 로고    scopus 로고
    • De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated
    • Hanton S., Chatre L., Renna L., Matheson L., and Brandizzi F. De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated. Plant Physiol. 143 (2007) 1640-1650
    • (2007) Plant Physiol. , vol.143 , pp. 1640-1650
    • Hanton, S.1    Chatre, L.2    Renna, L.3    Matheson, L.4    Brandizzi, F.5
  • 42
    • 26844533346 scopus 로고    scopus 로고
    • KATAMARI1/MURUS3 is a novel Golgi membrane protein that is required for endomembrane organization in Arabidopsis
    • Tamura K., Shimada T., Kondo M., Nishimura M., and Hara-Nishimura I. KATAMARI1/MURUS3 is a novel Golgi membrane protein that is required for endomembrane organization in Arabidopsis. Plant Cell 17 (2005) 1764-1776
    • (2005) Plant Cell , vol.17 , pp. 1764-1776
    • Tamura, K.1    Shimada, T.2    Kondo, M.3    Nishimura, M.4    Hara-Nishimura, I.5
  • 43
    • 48949107700 scopus 로고    scopus 로고
    • Myosin XI-K Is required for rapid trafficking of Golgi stacks, peroxisomes, and mitochondria in leaf cells of Nicotiana benthamiana
    • Avisar D., Prokhnevsky A., Makarova K., Koonin E., and Dolja V. Myosin XI-K Is required for rapid trafficking of Golgi stacks, peroxisomes, and mitochondria in leaf cells of Nicotiana benthamiana. Plant Physiol. 146 (2008) 1098-1108
    • (2008) Plant Physiol. , vol.146 , pp. 1098-1108
    • Avisar, D.1    Prokhnevsky, A.2    Makarova, K.3    Koonin, E.4    Dolja, V.5
  • 45
    • 48649091493 scopus 로고    scopus 로고
    • Truncated myosin XI tail fusions inhibit peroxisome, Golgi, and mitochondrial movement in tobacco leaf epidermal cells: a genetic tool for the next generation
    • Sparkes I.A., Teanby N.A., and Hawes C. Truncated myosin XI tail fusions inhibit peroxisome, Golgi, and mitochondrial movement in tobacco leaf epidermal cells: a genetic tool for the next generation. J. Exp. Bot. 59 (2008) 2499-2512
    • (2008) J. Exp. Bot. , vol.59 , pp. 2499-2512
    • Sparkes, I.A.1    Teanby, N.A.2    Hawes, C.3
  • 46
    • 12844281650 scopus 로고    scopus 로고
    • An internal motor kinesin is associated with the Golgi apparatus and plays a role in trichome morphogenesis in Arabidopsis
    • Lu L., Lee Y.R.J., Pan R.Q., Maloof J.N., and Liu B. 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
    • Lu, L.1    Lee, Y.R.J.2    Pan, R.Q.3    Maloof, J.N.4    Liu, B.5
  • 49
    • 48949120196 scopus 로고    scopus 로고
    • Two class XI myosins function in organelle trafficking and root hair development in Arabidopsis
    • Peremyslov V.V., Prokhnevsky A.I., Avisar D., and Dolja V.V. Two class XI myosins function in organelle trafficking and root hair development in Arabidopsis. Plant Physiol. 146 (2008) 1109-1116
    • (2008) Plant Physiol. , vol.146 , pp. 1109-1116
    • Peremyslov, V.V.1    Prokhnevsky, A.I.2    Avisar, D.3    Dolja, V.V.4
  • 50
    • 53749093685 scopus 로고    scopus 로고
    • Nanoscale architecture of endoplasmic reticulum export sites and of Golgi membranes as determined by electron tomography
    • Staehelin L.A., and Kang B.H. Nanoscale architecture of endoplasmic reticulum export sites and of Golgi membranes as determined by electron tomography. Plant Physiol. 147 (2008) 1454-1468
    • (2008) Plant Physiol. , vol.147 , pp. 1454-1468
    • Staehelin, L.A.1    Kang, B.H.2
  • 51
    • 0029979493 scopus 로고    scopus 로고
    • Cytokinesis in higher plants
    • Staehelin L.A., and Hepler P.K. Cytokinesis in higher plants. Cell 84 (1996) 821-824
    • (1996) Cell , vol.84 , pp. 821-824
    • Staehelin, L.A.1    Hepler, P.K.2
  • 52
    • 0033829447 scopus 로고    scopus 로고
    • Redistribution of Golgi stacks and other organelles during mitosis and cytokinesis in plant cells
    • Nebenfuhr A., Frohlick J.A., and Staehelin L.A. Redistribution of Golgi stacks and other organelles during mitosis and cytokinesis in plant cells. Plant Physiol. 124 (2000) 135-151
    • (2000) Plant Physiol. , vol.124 , pp. 135-151
    • Nebenfuhr, A.1    Frohlick, J.A.2    Staehelin, L.A.3
  • 53
    • 0000634192 scopus 로고
    • Growth kinetics of the Golgi apparatus during the cell cycle in onion root meristems
    • Garcia-Herdugo G., González-Reyes J.A., Gracia-Navarro F., and Navas P. Growth kinetics of the Golgi apparatus during the cell cycle in onion root meristems. Planta 175 (1988) 305-312
    • (1988) Planta , vol.175 , pp. 305-312
    • Garcia-Herdugo, G.1    González-Reyes, J.A.2    Gracia-Navarro, F.3    Navas, P.4
  • 54
    • 29444448243 scopus 로고    scopus 로고
    • Cell cycle-dependent changes in Golgi stacks, vacuoles, clathrin-coated vesicles and multivesicular bodies in meristematic cells of Arabidopsis thaliana: a quantitative and spatial analysis
    • Segui-Simarro J.M., and Staehelin L.A. Cell cycle-dependent changes in Golgi stacks, vacuoles, clathrin-coated vesicles and multivesicular bodies in meristematic cells of Arabidopsis thaliana: a quantitative and spatial analysis. Planta 223 (2006) 223-236
    • (2006) Planta , vol.223 , pp. 223-236
    • Segui-Simarro, J.M.1    Staehelin, L.A.2
  • 55
    • 34547617323 scopus 로고    scopus 로고
    • Golgi regeneration after brefeldin A treatment in BY-2 cells entails stack enlargement and cisternal growth followed by division
    • Langhans M., Hawes C., Hillmer S., Hummel E., and Robinson D.G. Golgi regeneration after brefeldin A treatment in BY-2 cells entails stack enlargement and cisternal growth followed by division. Plant Physiol. 145 (2007) 527-538
    • (2007) Plant Physiol. , vol.145 , pp. 527-538
    • Langhans, M.1    Hawes, C.2    Hillmer, S.3    Hummel, E.4    Robinson, D.G.5
  • 56
    • 0034718846 scopus 로고    scopus 로고
    • Matrix proteins can generate the higher order architecture of the Golgi apparatus
    • Seemann J., Jokitalo E., Pypaert M., and Warren G. Matrix proteins can generate the higher order architecture of the Golgi apparatus. Nature 407 (2000) 1022-1026
    • (2000) Nature , vol.407 , pp. 1022-1026
    • Seemann, J.1    Jokitalo, E.2    Pypaert, M.3    Warren, G.4
  • 57
    • 0013085340 scopus 로고    scopus 로고
    • Golgins in the structure and dynamics of the Golgi apparatus
    • Barr F.A., and Short B. Golgins in the structure and dynamics of the Golgi apparatus. Curr. Opin. Cell Biol. 15 (2003) 405-413
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 405-413
    • Barr, F.A.1    Short, B.2
  • 58
    • 0028855261 scopus 로고
    • The plant Golgi apparatus: Structure, functional organization and trafficking mechanisms
    • Staehelin, L. and Moore, I. (1995). The plant Golgi apparatus: structure, functional organization and trafficking mechanisms. Ann. Rev. Plant Physiol. Plant Mol. Biol., 46.
    • (1995) Ann. Rev. Plant Physiol. Plant Mol. Biol , vol.46
    • Staehelin, L.1    Moore, I.2
  • 60
    • 33644838123 scopus 로고    scopus 로고
    • An Arabidopsis GRIP domain protein locates to the trans-Golgi and binds the small GTPase ARL1
    • Latijnhouwers M., Hawes C., Carvalho C., Oparka K., Gillingham A.K., and Boevink P. An Arabidopsis GRIP domain protein locates to the trans-Golgi and binds the small GTPase ARL1. Plant J. 44 (2005) 459-470
    • (2005) Plant J. , vol.44 , pp. 459-470
    • Latijnhouwers, M.1    Hawes, C.2    Carvalho, C.3    Oparka, K.4    Gillingham, A.K.5    Boevink, P.6
  • 62
    • 0033535585 scopus 로고    scopus 로고
    • The GRIP domain - a novel Golgi-targeting domain found in several coiled-coil proteins
    • Munro S., and Nichols B.J. The GRIP domain - a novel Golgi-targeting domain found in several coiled-coil proteins. Curr. Biol. 9 (1999) 377-380
    • (1999) Curr. Biol. , vol.9 , pp. 377-380
    • Munro, S.1    Nichols, B.J.2
  • 63
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • Barr F.A., Puype M., Vandekerckhove J., and Warren G. GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91 (1997) 253-262
    • (1997) Cell , vol.91 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 64
    • 0035842897 scopus 로고    scopus 로고
    • Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus
    • Barr F.A., Preisinger C., Kopajtich R., and Korner R. Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus. J. Cell Biol. 155 (2001) 885-891
    • (2001) J. Cell Biol. , vol.155 , pp. 885-891
    • Barr, F.A.1    Preisinger, C.2    Kopajtich, R.3    Korner, R.4
  • 65
    • 51349095514 scopus 로고    scopus 로고
    • GRASP55 regulates Golgi ribbon formation
    • Feinstein T.N., and Linstedt A.D. GRASP55 regulates Golgi ribbon formation. Mol. Biol. Cell 19 (2008) 2696-2707
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2696-2707
    • Feinstein, T.N.1    Linstedt, A.D.2
  • 67
    • 44449096760 scopus 로고    scopus 로고
    • EMBRYO YELLOW gene, encoding a subunit of the conserved oligomeric Golgi complex, is required for appropriate cell expansion and meristem organization in Arabidopsis thaliana
    • Ishikawa T., Machida C., Yoshioka Y., Ueda T., Nakano A., and Machida Y. EMBRYO YELLOW gene, encoding a subunit of the conserved oligomeric Golgi complex, is required for appropriate cell expansion and meristem organization in Arabidopsis thaliana. Genes Cells 13 (2008) 521-535
    • (2008) Genes Cells , vol.13 , pp. 521-535
    • Ishikawa, T.1    Machida, C.2    Yoshioka, Y.3    Ueda, T.4    Nakano, A.5    Machida, Y.6
  • 68
    • 51849142293 scopus 로고    scopus 로고
    • Deciphering the Golgi apparatus: from imaging to genes
    • Boulaflous A., Faso C., and Brandizzi F. Deciphering the Golgi apparatus: from imaging to genes. Traffic 9 (2008) 1613-1617
    • (2008) Traffic , vol.9 , pp. 1613-1617
    • Boulaflous, A.1    Faso, C.2    Brandizzi, F.3
  • 69
    • 34548487513 scopus 로고    scopus 로고
    • A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants
    • Nelson B., Cai X., and Nebenführ A. A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants. Plant J. 51 (2007) 1126-1136
    • (2007) Plant J. , vol.51 , pp. 1126-1136
    • Nelson, B.1    Cai, X.2    Nebenführ, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.