메뉴 건너뛰기




Volumn 9, Issue 10, 2008, Pages 1629-1652

The syntaxins SYP31 and SYP81 control ER-Golgi trafficking in the plant secretory pathway

Author keywords

BFA resistance; ER; Golgi; SNARE overexpression; SYP31; SYP81

Indexed keywords

AMYLASE; HYBRID PROTEIN; PROTEIN SYP31; PROTEIN SYP81; SNARE PROTEIN; SYNTAXIN; UNCLASSIFIED DRUG;

EID: 51849151243     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2008.00803.x     Document Type: Article
Times cited : (70)

References (109)
  • 2
    • 3042689728 scopus 로고    scopus 로고
    • The role of ADP-ribosylation factor and SAR1 in vesicular trafficking in plants
    • Memon AR. The role of ADP-ribosylation factor and SAR1 in vesicular trafficking in plants. Biochim Biophys Acta 2004;1664: 9-30.
    • (2004) Biochim Biophys Acta , vol.1664 , pp. 9-30
    • Memon, A.R.1
  • 3
    • 33749015997 scopus 로고    scopus 로고
    • Microtubule motors at the intersection of trafficking and transport
    • Caviston JP, Holzbaur EL. Microtubule motors at the intersection of trafficking and transport. Trends Cell Biol 2006;16:530-537.
    • (2006) Trends Cell Biol , vol.16 , pp. 530-537
    • Caviston, J.P.1    Holzbaur, E.L.2
  • 4
    • 16644375282 scopus 로고    scopus 로고
    • Cytoskeletal motors in Arabidopsis. Sixty-one kinesins and seventeen myosins
    • Lee YR, Liu B. Cytoskeletal motors in Arabidopsis. Sixty-one kinesins and seventeen myosins. Plant Physiol 2004;136:3877-3883.
    • (2004) Plant Physiol , vol.136 , pp. 3877-3883
    • Lee, Y.R.1    Liu, B.2
  • 5
    • 0032522377 scopus 로고    scopus 로고
    • Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
    • Cao X, Ballew N, Barlowe C. Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J 1998;17:2156-2165.
    • (1998) EMBO J , vol.17 , pp. 2156-2165
    • Cao, X.1    Ballew, N.2    Barlowe, C.3
  • 7
    • 23844556932 scopus 로고    scopus 로고
    • SNAREs and traffic
    • Hong W. SNAREs and traffic. Biochim Biophys Acta 2005;1744:493-517.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 493-517
    • Hong, W.1
  • 9
    • 35649028253 scopus 로고    scopus 로고
    • SNARE-ware: The role of SNARE-domain proteins in plant biology
    • Lipka V, Kwon C, Panstruga R. SNARE-ware: The role of SNARE-domain proteins in plant biology. Annu Rev Cell Dev Biol 2007;23:147-174.
    • (2007) Annu Rev Cell Dev Biol , vol.23 , pp. 147-174
    • Lipka, V.1    Kwon, C.2    Panstruga, R.3
  • 10
    • 33747066132 scopus 로고    scopus 로고
    • Rabs and their effectors: Achieving specificity in membrane traffic
    • Grosshans BL, Ortiz D, Novick P. Rabs and their effectors: Achieving specificity in membrane traffic. Proc Natl Acad Sci U S A 2006;103:11821-11827.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11821-11827
    • Grosshans, B.L.1    Ortiz, D.2    Novick, P.3
  • 11
    • 33644816187 scopus 로고    scopus 로고
    • Role of tethering factors in secretory membrane traffic
    • Sztul E, Lupashin V. Role of tethering factors in secretory membrane traffic. Am J Physiol Cell Physiol 2006;290:C11-C26.
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Sztul, E.1    Lupashin, V.2
  • 12
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • Rothman JE, Warren G. Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr Biol 1994;4:220-233.
    • (1994) Curr Biol , vol.4 , pp. 220-233
    • Rothman, J.E.1    Warren, G.2
  • 13
    • 0027404604 scopus 로고
    • The molecular machinery for secretion is conserved from yeast to neurons
    • Bennett MK, Scheller RH. The molecular machinery for secretion is conserved from yeast to neurons. Proc Natl Acad Sci U S A 1993;90:2559-2563.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2559-2563
    • Bennett, M.K.1    Scheller, R.H.2
  • 16
    • 0034631955 scopus 로고    scopus 로고
    • Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors
    • McNew JA, Weber T, Parlati F, Johnston RJ, Melia TJ, Sollner TH, Rothman JE. Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors. J Cell Biol 2000;150:105-117.
    • (2000) J Cell Biol , vol.150 , pp. 105-117
    • McNew, J.A.1    Weber, T.2    Parlati, F.3    Johnston, R.J.4    Melia, T.J.5    Sollner, T.H.6    Rothman, J.E.7
  • 18
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer D, Sutton RB, Brunger AT, Jahn R. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc Natl Acad Sci U S A 1998;95:15781-15786.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 19
    • 0035279058 scopus 로고    scopus 로고
    • SNAREs and the specificity of membrane fusion
    • Pelham HR. SNAREs and the specificity of membrane fusion. Trends Cell Biol 2001;11:99-101.
    • (2001) Trends Cell Biol , vol.11 , pp. 99-101
    • Pelham, H.R.1
  • 20
    • 0033985393 scopus 로고    scopus 로고
    • Yeast Golgi SNARE interactions are promiscuous
    • Tsui MM, Banfield DK. Yeast Golgi SNARE interactions are promiscuous. J Cell Sci 2000;113:145-152.
    • (2000) J Cell Sci , vol.113 , pp. 145-152
    • Tsui, M.M.1    Banfield, D.K.2
  • 21
    • 0035158866 scopus 로고    scopus 로고
    • Selective formation of Sed5p-containing SNARE complexes is mediated by combinatorial binding interactions
    • Tsui MM, Tai WC, Banfield DK. Selective formation of Sed5p-containing SNARE complexes is mediated by combinatorial binding interactions. Mol Biol Cell 2001;12:521-538.
    • (2001) Mol Biol Cell , vol.12 , pp. 521-538
    • Tsui, M.M.1    Tai, W.C.2    Banfield, D.K.3
  • 22
    • 0026756118 scopus 로고
    • SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex
    • Hardwick KG, Pelham HR. SED5 encodes a 39-kD integral membrane protein required for vesicular transport between the ER and the Golgi complex. J Cell Biol 1992;119:513-521.
    • (1992) J Cell Biol , vol.119 , pp. 513-521
    • Hardwick, K.G.1    Pelham, H.R.2
  • 23
    • 0030863058 scopus 로고    scopus 로고
    • An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal
    • Hui N, Nakamura N, Sonnichsen B, Shima DT, Nilsson T, Warren G. An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal. Mol Biol Cell 1997;8:1777-1787.
    • (1997) Mol Biol Cell , vol.8 , pp. 1777-1787
    • Hui, N.1    Nakamura, N.2    Sonnichsen, B.3    Shima, D.T.4    Nilsson, T.5    Warren, G.6
  • 24
    • 0025282485 scopus 로고
    • BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex
    • Newman AP, Shim J, Ferro-Novick S. BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex. Mol Cell Biol 1990;10:3405-3414.
    • (1990) Mol Cell Biol , vol.10 , pp. 3405-3414
    • Newman, A.P.1    Shim, J.2    Ferro-Novick, S.3
  • 25
    • 0032516856 scopus 로고    scopus 로고
    • SNAREs and membrane fusion in the Golgi apparatus
    • Nichols BJ, Pelham HR. SNAREs and membrane fusion in the Golgi apparatus. Biochim Biophys Acta 1998;1404:9-31.
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 9-31
    • Nichols, B.J.1    Pelham, H.R.2
  • 28
    • 0030858498 scopus 로고    scopus 로고
    • The synaptobrevin-related domains of Bos1p and Sec22p bind to the syntaxin-like region of Sed5p
    • Sacher M, Stone S, Ferro-Novick S. The synaptobrevin-related domains of Bos1p and Sec22p bind to the syntaxin-like region of Sed5p. J Biol Chem 1997;272:17134-17138.
    • (1997) J Biol Chem , vol.272 , pp. 17134-17138
    • Sacher, M.1    Stone, S.2    Ferro-Novick, S.3
  • 30
    • 0030911653 scopus 로고    scopus 로고
    • A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum
    • Lewis MJ, Rayner JC, Pelham HR. A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum. EMBO J 1997;16:3017-3024.
    • (1997) EMBO J , vol.16 , pp. 3017-3024
    • Lewis, M.J.1    Rayner, J.C.2    Pelham, H.R.3
  • 31
    • 0032489507 scopus 로고    scopus 로고
    • Organelle membrane fusion: A novel function for the syntaxin homolog Ufe1p in ER membrane fusion
    • Patel SK, Indig FE, Olivieri N, Levine ND, Latterich M. Organelle membrane fusion: A novel function for the syntaxin homolog Ufe1p in ER membrane fusion. Cell 1998;92:611-620.
    • (1998) Cell , vol.92 , pp. 611-620
    • Patel, S.K.1    Indig, F.E.2    Olivieri, N.3    Levine, N.D.4    Latterich, M.5
  • 32
    • 0031665836 scopus 로고    scopus 로고
    • The dynamics of Golgi protein traffic visualized in living yeast cells
    • Wooding S, Pelham HR. The dynamics of Golgi protein traffic visualized in living yeast cells. Mol Biol Cell 1998;9:2667-2680.
    • (1998) Mol Biol Cell , vol.9 , pp. 2667-2680
    • Wooding, S.1    Pelham, H.R.2
  • 33
    • 0031808667 scopus 로고    scopus 로고
    • Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p
    • Ballensiefen W, Ossipov D, Schmitt HD. Recycling of the yeast v-SNARE Sec22p involves COPI-proteins and the ER transmembrane proteins Ufe1p and Sec20p. J Cell Sci 1998;111:1507-1520.
    • (1998) J Cell Sci , vol.111 , pp. 1507-1520
    • Ballensiefen, W.1    Ossipov, D.2    Schmitt, H.D.3
  • 34
    • 0742272120 scopus 로고    scopus 로고
    • A complete set of SNAREs in yeast
    • Burri L, Lithgow T. A complete set of SNAREs in yeast. Traffic 2004;5:45-52.
    • (2004) Traffic , vol.5 , pp. 45-52
    • Burri, L.1    Lithgow, T.2
  • 35
    • 0028837490 scopus 로고
    • Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane
    • Kutay U, Ahnert-Hilger G, Hartmann E, Wiedenmann B, Rapoport TA. Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane. EMBO J 1995;14:217-223.
    • (1995) EMBO J , vol.14 , pp. 217-223
    • Kutay, U.1    Ahnert-Hilger, G.2    Hartmann, E.3    Wiedenmann, B.4    Rapoport, T.A.5
  • 36
    • 0032577974 scopus 로고    scopus 로고
    • Localization, dynamics, and protein interactions reveal distinct roles for ER and Golgi SNAREs
    • Hay JC, Klumperman J, Oorschot V, Steegmaier M, Kuo CS, Scheller RH. Localization, dynamics, and protein interactions reveal distinct roles for ER and Golgi SNAREs. J Cell Biol 1998;141:1489-1502.
    • (1998) J Cell Biol , vol.141 , pp. 1489-1502
    • Hay, J.C.1    Klumperman, J.2    Oorschot, V.3    Steegmaier, M.4    Kuo, C.S.5    Scheller, R.H.6
  • 37
    • 0036736095 scopus 로고    scopus 로고
    • Analysis of Sec22p in endoplasmic reticulum/Golgi transport reveals cellular redundancy in SNARE protein function
    • Liu Y, Barlowe C. Analysis of Sec22p in endoplasmic reticulum/Golgi transport reveals cellular redundancy in SNARE protein function. Mol Biol Cell 2002;13:3314-3324.
    • (2002) Mol Biol Cell , vol.13 , pp. 3314-3324
    • Liu, Y.1    Barlowe, C.2
  • 38
    • 0342470378 scopus 로고    scopus 로고
    • Yeast ER-Golgi v-SNAREs Bos1p and Bet1p differ in steady-state localization and targeting
    • Ossipov D, Schroder-Kohne S, Schmitt HD. Yeast ER-Golgi v-SNAREs Bos1p and Bet1p differ in steady-state localization and targeting. J Cell Sci 1999;112:4135-4142.
    • (1999) J Cell Sci , vol.112 , pp. 4135-4142
    • Ossipov, D.1    Schroder-Kohne, S.2    Schmitt, H.D.3
  • 39
    • 0033602030 scopus 로고    scopus 로고
    • SNAREs and the secretory pathway-lessons from yeast
    • Pelham HR. SNAREs and the secretory pathway-lessons from yeast. Exp Cell Res 1999;247:1-8.
    • (1999) Exp Cell Res , vol.247 , pp. 1-8
    • Pelham, H.R.1
  • 40
    • 0032476574 scopus 로고    scopus 로고
    • Reconstitution of retrograde transport from the Golgi to the ER in vitro
    • Spang A, Schekman R. Reconstitution of retrograde transport from the Golgi to the ER in vitro. J Cell Biol 1998;143:589-599.
    • (1998) J Cell Biol , vol.143 , pp. 589-599
    • Spang, A.1    Schekman, R.2
  • 41
    • 26244449794 scopus 로고    scopus 로고
    • Control of Golgi morphology and function by Sed5 t-SNARE phosphorylation
    • Weinberger A, Kamena F, Kama R, Spang A, Gerst JE. Control of Golgi morphology and function by Sed5 t-SNARE phosphorylation. Mol Biol Cell 2005;16:4918-4930.
    • (2005) Mol Biol Cell , vol.16 , pp. 4918-4930
    • Weinberger, A.1    Kamena, F.2    Kama, R.3    Spang, A.4    Gerst, J.E.5
  • 42
    • 0026703234 scopus 로고
    • Genes that allow yeast cells to grow in the absence of the HDEL receptor
    • Hardwick KG, Boothroyd JC, Rudner AD, Pelham HR. Genes that allow yeast cells to grow in the absence of the HDEL receptor. EMBO J 1992;11:4187-4195.
    • (1992) EMBO J , vol.11 , pp. 4187-4195
    • Hardwick, K.G.1    Boothroyd, J.C.2    Rudner, A.D.3    Pelham, H.R.4
  • 43
    • 0025362445 scopus 로고
    • ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway
    • Semenza JC, Hardwick KG, Dean N, Pelham HR. ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 1990;61:1349-1357.
    • (1990) Cell , vol.61 , pp. 1349-1357
    • Semenza, J.C.1    Hardwick, K.G.2    Dean, N.3    Pelham, H.R.4
  • 44
    • 33749262307 scopus 로고    scopus 로고
    • Overexpression of the Arabidopsis syntaxin PEP12/SYP21 inhibits transport from the prevacuolar compartment to the lytic vacuole in vivo
    • Foresti O, daSilva LL, Denecke J. Overexpression of the Arabidopsis syntaxin PEP12/SYP21 inhibits transport from the prevacuolar compartment to the lytic vacuole in vivo. Plant Cell 2006;18:2275-2293.
    • (2006) Plant Cell , vol.18 , pp. 2275-2293
    • Foresti, O.1    daSilva, L.L.2    Denecke, J.3
  • 46
    • 0034525357 scopus 로고    scopus 로고
    • The Arabidopsis genome. An abundance of soluble N-ethylmaleimide-sensitive factor adaptor protein receptors
    • Sanderfoot AA, Assaad FF, Raikhel NV. The Arabidopsis genome. An abundance of soluble N-ethylmaleimide-sensitive factor adaptor protein receptors. Plant Physiol 2000;124:1558-1569.
    • (2000) Plant Physiol , vol.124 , pp. 1558-1569
    • Sanderfoot, A.A.1    Assaad, F.F.2    Raikhel, N.V.3
  • 47
    • 0742323556 scopus 로고    scopus 로고
    • Traffic jams affect plant development and signal transduction
    • Surpin M, Raikhel N. Traffic jams affect plant development and signal transduction. Nat Rev Mol Cell Biol 2004;5:100-109.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 100-109
    • Surpin, M.1    Raikhel, N.2
  • 48
    • 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 RL, Nakano A, Takeyasu K, Sato MH. Systematic analysis of SNARE molecules in Arabidopsis: Dissection of the post-Golgi network in plant cells. Cell Struct Funct 2004;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
  • 50
    • 33644847629 scopus 로고    scopus 로고
    • Sec22 and Memb11 are v-SNAREs of the anterograde endoplasmic reticulum-Golgi pathway in tobacco leaf epidermal cells
    • Chatre L, Brandizzi F, Hocquellet A, Hawes C, Moreau P. Sec22 and Memb11 are v-SNAREs of the anterograde endoplasmic reticulum-Golgi pathway in tobacco leaf epidermal cells. Plant Physiol 2005;139:1244-1254.
    • (2005) Plant Physiol , vol.139 , pp. 1244-1254
    • Chatre, L.1    Brandizzi, F.2    Hocquellet, A.3    Hawes, C.4    Moreau, P.5
  • 52
    • 0036009778 scopus 로고    scopus 로고
    • The abscisic acid-related SNARE homolog NtSyr1 contributes to secretion and growth: Evidence from competition with its cytosolic domain
    • Geelen D, Leyman B, Batoko H, Di Sansabastiano GP, Moore I, Blatt MR. The abscisic acid-related SNARE homolog NtSyr1 contributes to secretion and growth: Evidence from competition with its cytosolic domain. Plant Cell 2002;14:387-406.
    • (2002) Plant Cell , vol.14 , pp. 387-406
    • Geelen, D.1    Leyman, B.2    Batoko, H.3    Di Sansabastiano, G.P.4    Moore, I.5    Blatt, M.R.6
  • 53
    • 34548504555 scopus 로고    scopus 로고
    • Selective targeting of plasma membrane and tonoplast traffic by inhibitory (dominant-negative) SNARE fragments
    • Tyrrell M, Campanoni P, Sutter JU, Pratelli R, Paneque M, Sokolovski S, Blatt MR. Selective targeting of plasma membrane and tonoplast traffic by inhibitory (dominant-negative) SNARE fragments. Plant J 2007;51:1099-1115.
    • (2007) Plant J , vol.51 , pp. 1099-1115
    • Tyrrell, M.1    Campanoni, P.2    Sutter, J.U.3    Pratelli, R.4    Paneque, M.5    Sokolovski, S.6    Blatt, M.R.7
  • 54
    • 0036193747 scopus 로고    scopus 로고
    • Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
    • Yamaguchi T, Dulubova I, Min SW, Chen X, Rizo J, Sudhof TC. Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev Cell 2002;2:295-305.
    • (2002) Dev Cell , vol.2 , pp. 295-305
    • Yamaguchi, T.1    Dulubova, I.2    Min, S.W.3    Chen, X.4    Rizo, J.5    Sudhof, T.C.6
  • 55
    • 33745456532 scopus 로고    scopus 로고
    • Targeting of the plant vacuolar sorting receptor BP80 is dependent on multiple sorting signals in the cytosolic tail
    • daSilva LL, Foresti O, Denecke J. Targeting of the plant vacuolar sorting receptor BP80 is dependent on multiple sorting signals in the cytosolic tail. Plant Cell 2006;18:1477-1497.
    • (2006) Plant Cell , vol.18 , pp. 1477-1497
    • daSilva, L.L.1    Foresti, O.2    Denecke, J.3
  • 56
    • 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 YD, Elamawi R, Bubeck J, Pepperkok R, Ritzenthaler C, Robinson DG. 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 2005;17:1513-1531.
    • (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
  • 57
    • 11244292123 scopus 로고    scopus 로고
    • Arabidopsis thaliana expresses multiple Golgi-localized nucleotide-sugar transporters related to GONST1
    • Handford MG, Sicilia F, Brandizzi F, Chung JH, Dupree P. Arabidopsis thaliana expresses multiple Golgi-localized nucleotide-sugar transporters related to GONST1. Mol Genet Genomics 2004;272:397-410.
    • (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
  • 58
    • 0036851186 scopus 로고    scopus 로고
    • Brefeldin A: Deciphering an enigmatic inhibitor of secretion
    • Nebenfuhr A, Ritzenthaler C, Robinson DG. Brefeldin A: Deciphering an enigmatic inhibitor of secretion. Plant Physiol 2002;130:1102-1108.
    • (2002) Plant Physiol , vol.130 , pp. 1102-1108
    • Nebenfuhr, A.1    Ritzenthaler, C.2    Robinson, D.G.3
  • 62
    • 34248653184 scopus 로고    scopus 로고
    • Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants
    • Sparkes IA, Runions J, Kearns A, Hawes C. Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants. Nat Protoc 2006;1:2019-2025.
    • (2006) Nat Protoc , vol.1 , pp. 2019-2025
    • Sparkes, I.A.1    Runions, J.2    Kearns, A.3    Hawes, C.4
  • 63
    • 29344456761 scopus 로고    scopus 로고
    • Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane
    • Runions J, Brach T, Kuhner S, Hawes C. Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane. J Exp Bot 2006;57:43-50.
    • (2006) J Exp Bot , vol.57 , pp. 43-50
    • Runions, J.1    Brach, T.2    Kuhner, S.3    Hawes, C.4
  • 64
    • 18044367582 scopus 로고    scopus 로고
    • Plant cytokinesis: Fission by fusion
    • Jurgens G. Plant cytokinesis: Fission by fusion. Trends Cell Biol 2005;15:277-283.
    • (2005) Trends Cell Biol , vol.15 , pp. 277-283
    • Jurgens, G.1
  • 66
    • 0029843491 scopus 로고    scopus 로고
    • Molecular analysis of UFE1, a Saccharomyces cerevisiae gene essential for spore formation and vegetative growth
    • Downing TA, Storms RK. Molecular analysis of UFE1, a Saccharomyces cerevisiae gene essential for spore formation and vegetative growth. Curr Genet 1996;30:396-403.
    • (1996) Curr Genet , vol.30 , pp. 396-403
    • Downing, T.A.1    Storms, R.K.2
  • 67
    • 0029932226 scopus 로고    scopus 로고
    • SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum
    • Lewis MJ, Pelham HR. SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell 1996;85:205-215.
    • (1996) Cell , vol.85 , pp. 205-215
    • Lewis, M.J.1    Pelham, H.R.2
  • 69
    • 0029024860 scopus 로고
    • A SNARE-like protein required for traffic through the Golgi complex
    • Banfield DK, Lewis MJ, Pelham HR. A SNARE-like protein required for traffic through the Golgi complex. Nature 1995;375:806-809.
    • (1995) Nature , vol.375 , pp. 806-809
    • Banfield, D.K.1    Lewis, M.J.2    Pelham, H.R.3
  • 70
    • 8144231395 scopus 로고    scopus 로고
    • Multiple SNARE interactions of an SM protein: Sed5p/Sly1p binding is dispensable for transport
    • Peng R, Gallwitz D. Multiple SNARE interactions of an SM protein: Sed5p/ Sly1p binding is dispensable for transport. EMBO J 2004;23:3939-3949.
    • (2004) EMBO J , vol.23 , pp. 3939-3949
    • Peng, R.1    Gallwitz, D.2
  • 72
    • 0030054915 scopus 로고    scopus 로고
    • Mammalian Sly1 regulates syntaxin 5 function in endoplasmic reticulum to Golgi transport
    • Dascher C, Balch WE. Mammalian Sly1 regulates syntaxin 5 function in endoplasmic reticulum to Golgi transport. J Biol Chem 1996;271:15866-15869.
    • (1996) J Biol Chem , vol.271 , pp. 15866-15869
    • Dascher, C.1    Balch, W.E.2
  • 74
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner JC, Pelham HR. Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO J 1997:16:1832-1841.
    • (1997) EMBO J , vol.16 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.2
  • 75
  • 76
    • 36749104219 scopus 로고    scopus 로고
    • SM-protein-controlled ER-associated degradation discriminates between different SNAREs
    • Braun S, Jentsch S. SM-protein-controlled ER-associated degradation discriminates between different SNAREs. EMBO Rep 2007;8:1176-1182.
    • (2007) EMBO Rep , vol.8 , pp. 1176-1182
    • Braun, S.1    Jentsch, S.2
  • 77
    • 0034607967 scopus 로고    scopus 로고
    • Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking
    • Hatsuzawa K, Hirose H, Tani K, Yamamoto A, Scheller RH, Tagaya M. Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking. J Biol Chem 2000;275:13713-13720.
    • (2000) J Biol Chem , vol.275 , pp. 13713-13720
    • Hatsuzawa, K.1    Hirose, H.2    Tani, K.3    Yamamoto, A.4    Scheller, R.H.5    Tagaya, M.6
  • 78
    • 0034718846 scopus 로고    scopus 로고
    • Matrix proteins can generate the higher order architecture of the Golgi apparatus
    • Seemann J, Jokitalo E, Pypaert M, Warren G. Matrix proteins can generate the higher order architecture of the Golgi apparatus. Nature 2000;407:1022-1026.
    • (2000) Nature , vol.407 , pp. 1022-1026
    • Seemann, J.1    Jokitalo, E.2    Pypaert, M.3    Warren, G.4
  • 79
    • 0036468386 scopus 로고    scopus 로고
    • Partitioning of the matrix fraction of the Golgi apparatus during mitosis in animal cells
    • Seemann J, Pypaert M, Taguchi T, Malsam J, Warren G. Partitioning of the matrix fraction of the Golgi apparatus during mitosis in animal cells. Science 2002;295:848-851.
    • (2002) Science , vol.295 , pp. 848-851
    • Seemann, J.1    Pypaert, M.2    Taguchi, T.3    Malsam, J.4    Warren, G.5
  • 81
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: The Sec7 family of guanine-nucleotide-exchange factors
    • Jackson CL, Casanova JE. Turning on ARF: The Sec7 family of guanine-nucleotide-exchange factors. Trends Cell Biol 2000;10:60-67.
    • (2000) Trends Cell Biol , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 83
    • 26844526297 scopus 로고    scopus 로고
    • Holding it all together?. Candidate proteins for the plant Golgi matrix
    • Latijnhouwers M, Hawes C, Carvalho C. Holding it all together?. Candidate proteins for the plant Golgi matrix. Curr Opin Plant Biol 2005;8:632-639.
    • (2005) Curr Opin Plant Biol , vol.8 , pp. 632-639
    • Latijnhouwers, M.1    Hawes, C.2    Carvalho, C.3
  • 85
    • 36549042931 scopus 로고    scopus 로고
    • A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles
    • Miller SE, Collins BM, McCoy AJ, Robinson MS, Owen DJ. A SNARE-adaptor interaction is a new mode of cargo recognition in clathrin-coated vesicles. Nature 2007;450:570-574.
    • (2007) Nature , vol.450 , pp. 570-574
    • Miller, S.E.1    Collins, B.M.2    McCoy, A.J.3    Robinson, M.S.4    Owen, D.J.5
  • 87
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • Mossessova E, Bickford LC, Goldberg J. SNARE selectivity of the COPII coat. Cell 2003;114:483-495.
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 90
    • 3142706602 scopus 로고    scopus 로고
    • Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells
    • daSilva LL, Snapp EL, Denecke J, Lippincott-Schwartz J, Hawes C, Brandizzi F. Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells. Plant Cell 2004;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
  • 91
    • 0000882190 scopus 로고
    • Ultrastructure of freeze-substituted pollen tubes of Lilium longiflorum
    • Lancelle SA, Hepler PK. Ultrastructure of freeze-substituted pollen tubes of Lilium longiflorum. Protoplasma 1992;167:215-230.
    • (1992) Protoplasma , vol.167 , pp. 215-230
    • Lancelle, S.A.1    Hepler, P.K.2
  • 92
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban MJ, Cohen SN. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J Mol Biol 1980;138:179-207.
    • (1980) J Mol Biol , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 94
    • 0036016439 scopus 로고    scopus 로고
    • The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain
    • Brandizzi F, Frangne N, Marc-Martin S, Hawes C, Neuhaus JM, Paris N. The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain. Plant Cell 2002;14:1077-1092.
    • (2002) Plant Cell , vol.14 , pp. 1077-1092
    • Brandizzi, F.1    Frangne, N.2    Marc-Martin, S.3    Hawes, C.4    Neuhaus, J.M.5    Paris, N.6
  • 97
    • 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 LL, Boevink P, Evans D, Oparka K, Denecke J, Hawes C. ER quality control can lead to retrograde transport from the ER lumen to the cytosol and the nucleoplasm in plants. Plant J 2003;34:269-281.
    • (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
  • 98
    • 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. Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope. EMBO J 1992;11:2345-2355.
    • (1992) EMBO J , vol.11 , pp. 2345-2355
    • Denecke, J.1    De Rycke, R.2    Botterman, J.3
  • 100
    • 0030989517 scopus 로고    scopus 로고
    • Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly
    • Haseloff J, Siemering KR, Prasher DC, Hodge S. Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly. Proc Natl Acad Sci U S A 1997:94:2122-2127.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2122-2127
    • Haseloff, J.1    Siemering, K.R.2    Prasher, D.C.3    Hodge, S.4
  • 101
    • 0015914077 scopus 로고
    • Streptomycin-resistant plants from callus culture of haploid tobacco
    • Maliga P, Sz-Breznovits A, Marton L. Streptomycin-resistant plants from callus culture of haploid tobacco. Nat New Biol 1973;244:29-30.
    • (1973) Nat New Biol , vol.244 , pp. 29-30
    • Maliga, P.1    Sz-Breznovits, A.2    Marton, L.3
  • 102
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige R, Skoog F. A revised medium for rapid growth and bioassays with tobacco tissue cultures. Plant Physiol 1962;15:473-497.
    • (1962) Plant Physiol , vol.15 , pp. 473-497
    • Murashige, R.1    Skoog, F.2
  • 103
    • 0024982237 scopus 로고
    • Protein secretion in plant cells can occur via a default pathway
    • Denecke J, Botterman J, Deblaere R. Protein secretion in plant cells can occur via a default pathway. Plant Cell 1990;2:51-59.
    • (1990) Plant Cell , vol.2 , pp. 51-59
    • Denecke, J.1    Botterman, J.2    Deblaere, R.3
  • 104
    • 0141621588 scopus 로고    scopus 로고
    • The green fluorescent protein (GFP) as a reporter in plant cells
    • In: Hawes C and Satiat-Jeunemaitre B, editors. Oxford, UK: Oxford University Press
    • Neuhaus JM, Boevink P. The green fluorescent protein (GFP) as a reporter in plant cells. In: Hawes C and Satiat-Jeunemaitre B, editors. Plant Cell Biology. Oxford, UK: Oxford University Press; 2001, pp. 127-142.
    • (2001) Plant Cell Biology , pp. 127-142
    • Neuhaus, J.M.1    Boevink, P.2
  • 105
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • Frangioni JV, Neel BG. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal Biochem 1993;210:179-187.
    • (1993) Anal Biochem , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 106
    • 33645737420 scopus 로고    scopus 로고
    • Golgi-mediated vacuolar sorting of the ER chaperone BiP may play an active role in quality control within the secretory pathway
    • Pimpl P, Taylor JP, Snowden CJ, Hillmer S, Robinson DG, Denecke J. Golgi-mediated vacuolar sorting of the ER chaperone BiP may play an active role in quality control within the secretory pathway. Plant Cell 2006;18:198-211.
    • (2006) Plant Cell , vol.18 , pp. 198-211
    • Pimpl, P.1    Taylor, J.P.2    Snowden, C.J.3    Hillmer, S.4    Robinson, D.G.5    Denecke, J.6
  • 107
    • 34247278153 scopus 로고    scopus 로고
    • Rapid freeze-substitution preserves membranes in high-pressure frozen tissue culture cells
    • Hawes P, Netherton CL, Mueller M, Wileman T, Monaghan P. Rapid freeze-substitution preserves membranes in high-pressure frozen tissue culture cells. J Microsc 2007;226:182-189.
    • (2007) J Microsc , vol.226 , pp. 182-189
    • Hawes, P.1    Netherton, C.L.2    Mueller, M.3    Wileman, T.4    Monaghan, P.5
  • 108
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • Elble R. A simple and efficient procedure for transformation of yeasts. Biotechniques 1992;13:18-20.
    • (1992) Biotechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 109
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall TA. BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nul Acids Symp Ser 1999;41:95-98.
    • (1999) Nul Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.