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Volumn 77, Issue 6, 2014, Pages 863-879

A model for transport of a viral membrane protein through the early secretory pathway: Minimal sequence and endoplasmic reticulum lateral mobility requirements

Author keywords

cargo concentration; Cucumis melo; endoplasmic reticulum sorting signal; lateral diffusion; movement proteins; secretory pathway; transmembrane protein; virus movement

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; PHOTOBLEACHING; VIRUSES;

EID: 84895920142     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/tpj.12435     Document Type: Article
Times cited : (16)

References (71)
  • 2
    • 0027383316 scopus 로고
    • Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor
    • Aroeti, B., Kosen, P.A., Kuntz, I.D., Cohen, F.E., and, Mostov, K.E., (1993) Mutational and secondary structural analysis of the basolateral sorting signal of the polymeric immunoglobulin receptor. J. Cell Biol. 123, 1149-1160.
    • (1993) J. Cell Biol. , vol.123 , pp. 1149-1160
    • Aroeti, B.1    Kosen, P.A.2    Kuntz, I.D.3    Cohen, F.E.4    Mostov, K.E.5
  • 3
    • 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.I., Makarova, K.S., Koonin, E.V., and, Dolja, V.V., (2008) Myosin XI-K is required for rapid trafficking of Golgi stacks, peroxisomes, and mitochondria in leaf cells of Nicotiana benthamiana. Plant Physiol. 146, 1098-1108.
    • (2008) Plant Physiol. , vol.146 , pp. 1098-1108
    • Avisar, D.1    Prokhnevsky, A.I.2    Makarova, K.S.3    Koonin, E.V.4    Dolja, V.V.5
  • 4
    • 66649113058 scopus 로고    scopus 로고
    • A comparative study of the involvement of 17 Arabidopsis myosin family members on the motility of Golgi and other organelles
    • Avisar, D., Abu-Abied, M., Belausov, E., Sadot, E., Hawes, C., and, Sparkes, I.A., (2009) A comparative study of the involvement of 17 Arabidopsis myosin family members on the motility of Golgi and other organelles. Plant Physiol. 150, 700-709.
    • (2009) Plant Physiol. , vol.150 , pp. 700-709
    • Avisar, D.1    Abu-Abied, M.2    Belausov, E.3    Sadot, E.4    Hawes, C.5    Sparkes, I.A.6
  • 5
    • 0026315047 scopus 로고
    • The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation
    • Bansal, A., and, Gierasch, L.M., (1991) The NPXY internalization signal of the LDL receptor adopts a reverse-turn conformation. Cell, 67, 1195-1201.
    • (1991) Cell , vol.67 , pp. 1195-1201
    • Bansal, A.1    Gierasch, L.M.2
  • 6
    • 49749152452 scopus 로고    scopus 로고
    • The luminal domain of p23 (Tmp21) plays a critical role in p23 cell surface trafficking
    • Blum, R., and, Lepier, A., (2008) The luminal domain of p23 (Tmp21) plays a critical role in p23 cell surface trafficking. Traffic, 9, 1530-1550.
    • (2008) Traffic , vol.9 , pp. 1530-1550
    • Blum, R.1    Lepier, A.2
  • 7
    • 0032144201 scopus 로고    scopus 로고
    • Stacks on tracks: The plant Golgi apparatus traffics on an actin/ER network
    • Boevink, P., Oparka, K., Santa Cruz, S., Martin, B., Betteridge, A., and, Hawes, C., (1998) Stacks on tracks: the plant Golgi apparatus traffics on an actin/ER network. Plant J. 15, 441-447.
    • (1998) Plant J. , vol.15 , pp. 441-447
    • Boevink, P.1    Oparka, K.2    Santa Cruz, S.3    Martin, B.4    Betteridge, A.5    Hawes, C.6
  • 8
    • 84878253184 scopus 로고    scopus 로고
    • Organization of the ER-Golgi interface for membrane traffic control
    • Brandizzi, F., and, Barlowe, C., (2013) Organization of the ER-Golgi interface for membrane traffic control. Nat. Rev. Mol. Cell Biol. 14, 382-392.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 382-392
    • Brandizzi, F.1    Barlowe, C.2
  • 9
    • 0036016439 scopus 로고    scopus 로고
    • The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain
    • Brandizzi, F., Frangne, N., Marc-Martin, S., Hawes, C., Neuhaus, J.M., and, Paris, N., (2002a) The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain. Plant Cell, 14, 1077-1092.
    • (2002) Plant Cell , vol.14 , pp. 1077-1092
    • Brandizzi, F.1    Frangne, N.2    Marc-Martin, S.3    Hawes, C.4    Neuhaus, J.M.5    Paris, N.6
  • 10
    • 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., (2002b) Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching. Plant Cell, 14, 1293-1309.
    • (2002) Plant Cell , vol.14 , pp. 1293-1309
    • Brandizzi, F.1    Snapp, E.L.2    Roberts, A.G.3    Lippincott-Schwartz, J.4    Hawes, C.5
  • 11
    • 69949146218 scopus 로고    scopus 로고
    • Molecular dissection of Erv26p identifies separable cargo binding and coat protein sorting activities
    • Bue, C.A., and, Barlowe, C., (2009) Molecular dissection of Erv26p identifies separable cargo binding and coat protein sorting activities. J. Biol. Chem. 284, 24049-24060.
    • (2009) J. Biol. Chem. , vol.284 , pp. 24049-24060
    • Bue, C.A.1    Barlowe, C.2
  • 12
    • 67649954766 scopus 로고    scopus 로고
    • Erv26p-dependent export of alkaline phosphatase from the ER requires lumenal domain recognition
    • Dancourt, J., and, Barlowe, C., (2009) Erv26p-dependent export of alkaline phosphatase from the ER requires lumenal domain recognition. Traffic, 10, 1006-1018.
    • (2009) Traffic , vol.10 , pp. 1006-1018
    • Dancourt, J.1    Barlowe, C.2
  • 13
    • 77953642000 scopus 로고    scopus 로고
    • Protein sorting receptors in the early secretory pathway
    • Dancourt, J., and, Barlowe, C., (2010) Protein sorting receptors in the early secretory pathway. Annu. Rev. Biochem. 79, 777-802.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 777-802
    • Dancourt, J.1    Barlowe, C.2
  • 14
    • 0027536798 scopus 로고
    • The internalization signal and the phosphorylation site of transferrin receptor are distinct from the main basolateral sorting information
    • Dargemont, C., Le Bivic, A., Rothenberger, S., Iacopetta, B., and, Kuhn, L.C., (1993) The internalization signal and the phosphorylation site of transferrin receptor are distinct from the main basolateral sorting information. EMBO J. 12, 1713-1721.
    • (1993) EMBO J. , vol.12 , pp. 1713-1721
    • Dargemont, C.1    Le Bivic, A.2    Rothenberger, S.3    Iacopetta, B.4    Kuhn, L.C.5
  • 15
    • 69449102282 scopus 로고    scopus 로고
    • The length of cargo-protein transmembrane segments drives secretory transport by facilitating cargo concentration in export domains
    • Dukhovny, A., Yaffe, Y., Shepshelovitch, J., and, Hirschberg, K., (2009) The length of cargo-protein transmembrane segments drives secretory transport by facilitating cargo concentration in export domains. J. Cell Sci. 122, 1759-1767.
    • (2009) J. Cell Sci. , vol.122 , pp. 1759-1767
    • Dukhovny, A.1    Yaffe, Y.2    Shepshelovitch, J.3    Hirschberg, K.4
  • 16
    • 0026342565 scopus 로고
    • The essential tyrosine of the internalization signal in lysosomal acid phosphatase is part of a beta turn
    • Eberle, W., Sander, C., Klaus, W., Schmidt, B., von Figura, K., and, Peters, C., (1991) The essential tyrosine of the internalization signal in lysosomal acid phosphatase is part of a beta turn. Cell, 67, 1203-1209.
    • (1991) Cell , vol.67 , pp. 1203-1209
    • Eberle, W.1    Sander, C.2    Klaus, W.3    Schmidt, B.4    Von Figura, K.5    Peters, C.6
  • 17
    • 33746817825 scopus 로고    scopus 로고
    • Functional analysis of the five Melon necrotic spot virus genome-encoded proteins
    • Genoves, A., Navarro, J.A., and, Pallas, V., (2006) Functional analysis of the five Melon necrotic spot virus genome-encoded proteins. J. Gen. Virol. 87, 2371-2380.
    • (2006) J. Gen. Virol. , vol.87 , pp. 2371-2380
    • Genoves, A.1    Navarro, J.A.2    Pallas, V.3
  • 18
    • 77449085407 scopus 로고    scopus 로고
    • The intra- and intercellular movement of Melon necrotic spot virus (MNSV) depends on an active secretory pathway
    • Genoves, A., Navarro, J.A., and, Pallas, V., (2010) The intra- and intercellular movement of Melon necrotic spot virus (MNSV) depends on an active secretory pathway. Mol. Plant Microbe Interact. 23, 263-272.
    • (2010) Mol. Plant Microbe Interact. , vol.23 , pp. 263-272
    • Genoves, A.1    Navarro, J.A.2    Pallas, V.3
  • 19
    • 79960397172 scopus 로고    scopus 로고
    • Contribution of topology determinants of a viral movement protein to its membrane association, intracellular traffic, and viral cell-to-cell movement
    • Genoves, A., Pallas, V., and, Navarro, J.A., (2011) Contribution of topology determinants of a viral movement protein to its membrane association, intracellular traffic, and viral cell-to-cell movement. J. Virol. 85, 7797-7809.
    • (2011) J. Virol. , vol.85 , pp. 7797-7809
    • Genoves, A.1    Pallas, V.2    Navarro, J.A.3
  • 20
    • 34249785671 scopus 로고    scopus 로고
    • De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated
    • Hanton, S.L., Chatre, L., Renna, L., Matheson, L.A., and, Brandizzi, F., (2007a) De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated. Plant Physiol. 143, 1640-1650.
    • (2007) Plant Physiol. , vol.143 , pp. 1640-1650
    • Hanton, S.L.1    Chatre, L.2    Renna, L.3    Matheson, L.A.4    Brandizzi, F.5
  • 22
    • 62149130111 scopus 로고    scopus 로고
    • Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells
    • Hanton, S.L., Matheson, L.A., Chatre, L., and, Brandizzi, F., (2009) Dynamic organization of COPII coat proteins at endoplasmic reticulum export sites in plant cells. Plant J. 57, 963-974.
    • (2009) Plant J. , vol.57 , pp. 963-974
    • Hanton, S.L.1    Matheson, L.A.2    Chatre, L.3    Brandizzi, F.4
  • 23
    • 78149305216 scopus 로고    scopus 로고
    • Intracellular transport of viruses and their components: Utilizing the cytoskeleton and membrane highways
    • Harries, P.A., Schoelz, J.E., and, Nelson, R.S., (2010) Intracellular transport of viruses and their components: utilizing the cytoskeleton and membrane highways. Mol. Plant Microbe Interact. 23, 1381-1393.
    • (2010) Mol. Plant Microbe Interact. , vol.23 , pp. 1381-1393
    • Harries, P.A.1    Schoelz, J.E.2    Nelson, R.S.3
  • 24
    • 84877655719 scopus 로고    scopus 로고
    • The ER/Golgi interface - Is there anything in-between?
    • Hawes, C., (2012) The ER/Golgi interface-is there anything in-between? Front. Plant Sci. 3, 73.
    • (2012) Front. Plant Sci. , vol.3 , pp. 73
    • Hawes, C.1
  • 25
    • 20444386846 scopus 로고    scopus 로고
    • The plant Golgi apparatus - Going with the flow
    • Hawes, C., and, Satiat-Jeunemaitre, B., (2005) The plant Golgi apparatus-going with the flow. Biochim. Biophys. Acta, 1744, 93-107.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 93-107
    • Hawes, C.1    Satiat-Jeunemaitre, B.2
  • 27
    • 84862823001 scopus 로고    scopus 로고
    • Actin-binding proteins and actin dynamics in plant cells
    • In (Liu, B. ed.). New York: Springer
    • Huang, S., Xiang, Y., and, Ren, H., (2011) Actin-binding proteins and actin dynamics in plant cells. In The Plant Cytoskeleton. Advances in Plant Biology, Volume 2 (, Liu, B., ed.). New York: Springer, pp. 57-80.
    • (2011) The Plant Cytoskeleton. Advances in Plant Biology, Volume 2 , pp. 57-80
    • Huang, S.1    Xiang, Y.2    Ren, H.3
  • 28
    • 0028566270 scopus 로고
    • A revised set of potentials for β-turn formation in proteins
    • Hutchinson, E.G., and, Thornton, J.M., (1994) A revised set of potentials for β-turn formation in proteins. Protein Sci. 3, 2207-2216.
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 29
    • 78651075537 scopus 로고    scopus 로고
    • Localization and trafficking of an isoform of the AtPRA1 family to the Golgi apparatus depend on both N- and C-terminal sequence motifs
    • Jung, C.J., Lee, M.H., Min, M.K., and, Hwang, I., (2011) Localization and trafficking of an isoform of the AtPRA1 family to the Golgi apparatus depend on both N- and C-terminal sequence motifs. Traffic, 12, 185-200.
    • (2011) Traffic , vol.12 , pp. 185-200
    • Jung, C.J.1    Lee, M.H.2    Min, M.K.3    Hwang, I.4
  • 30
    • 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., (2008) 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, 51-64.
    • (2008) Protoplasma , vol.234 , pp. 51-64
    • Kang, B.H.1    Staehelin, L.A.2
  • 31
    • 8844252295 scopus 로고    scopus 로고
    • A neural network method for prediction of β-turn types in proteins using evolutionary information
    • Kaur, H., and, Raghava, G.P., (2004) A neural network method for prediction of β-turn types in proteins using evolutionary information. Bioinformatics, 20, 2751-2758.
    • (2004) Bioinformatics , vol.20 , pp. 2751-2758
    • Kaur, H.1    Raghava, G.P.2
  • 32
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: A case study using the Phyre server
    • Kelley, L.A., and, Sternberg, M.J.E., (2009) Protein structure prediction on the web: a case study using the Phyre server. Nat. Protoc., 4, 363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 33
    • 79955707349 scopus 로고    scopus 로고
    • High cleavage efficiency of a 2A peptide derived from porcine teschovirus-1 in human cell lines, zebrafish and mice
    • Kim, J.H., Lee, S.R., Li, L.H., Park, H.J., Park, J.H., Lee, K.Y., Kim, M.K., Shin, B.A., and, Choi, S.Y., (2011) High cleavage efficiency of a 2A peptide derived from porcine teschovirus-1 in human cell lines, zebrafish and mice. PLoS ONE, 6, e18556.
    • (2011) PLoS ONE , vol.6
    • Kim, J.H.1    Lee, S.R.2    Li, L.H.3    Park, H.J.4    Park, J.H.5    Lee, K.Y.6    Kim, M.K.7    Shin, B.A.8    Choi, S.Y.9
  • 36
    • 0141675998 scopus 로고    scopus 로고
    • Involvement of the secretory pathway and the cytoskeleton in intracellular targeting and tubule assembly of Grapevine fanleaf virus movement protein in tobacco BY-2 cells
    • Laporte, C., Vetter, G., Loudes, A.M., Robinson, D.G., Hillmer, S., Stussi-Garaud, C., and, Ritzenthaler, C., (2003) Involvement of the secretory pathway and the cytoskeleton in intracellular targeting and tubule assembly of Grapevine fanleaf virus movement protein in tobacco BY-2 cells. Plant Cell, 15, 2058-2075.
    • (2003) Plant Cell , vol.15 , pp. 2058-2075
    • Laporte, C.1    Vetter, G.2    Loudes, A.M.3    Robinson, D.G.4    Hillmer, S.5    Stussi-Garaud, C.6    Ritzenthaler, C.7
  • 37
    • 34548411897 scopus 로고    scopus 로고
    • Molecular mechanisms of COPII vesicle formation
    • Lee, M.C., and, Miller, E.A., (2007) Molecular mechanisms of COPII vesicle formation. Semin. Cell Dev. Biol. 18, 424-434.
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 424-434
    • Lee, M.C.1    Miller, E.A.2
  • 38
    • 84871340049 scopus 로고    scopus 로고
    • ER import sites and their relationship to ER exit sites: A new model for bidirectional ER-Golgi transport in higher plants
    • Lerich, A., Hillmer, S., Langhans, M., Scheuring, D., van Bentum, P., and, Robinson, D.G., (2012) ER import sites and their relationship to ER exit sites: a new model for bidirectional ER-Golgi transport in higher plants. Front. Plant Sci. 3, 143.
    • (2012) Front. Plant Sci. , vol.3 , pp. 143
    • Lerich, A.1    Hillmer, S.2    Langhans, M.3    Scheuring, D.4    Van Bentum, P.5    Robinson, D.G.6
  • 40
    • 84886750395 scopus 로고    scopus 로고
    • The cell biology of tobacco mosaic virus replication and movement
    • Liu, C., and, Nelson, R.S., (2013) The cell biology of tobacco mosaic virus replication and movement. Front. Plant Sci. 4, 12.
    • (2013) Front. Plant Sci. , vol.4 , pp. 12
    • Liu, C.1    Nelson, R.S.2
  • 41
    • 34848883056 scopus 로고    scopus 로고
    • Membrane insertion and topology of the p7B movement protein of Melon necrotic spot virus (MNSV)
    • Martinez-Gil, L., Sauri, A., Vilar, M., Pallas, V., and, Mingarro, I., (2007) Membrane insertion and topology of the p7B movement protein of Melon necrotic spot virus (MNSV). Virology, 367, 348-357.
    • (2007) Virology , vol.367 , pp. 348-357
    • Martinez-Gil, L.1    Sauri, A.2    Vilar, M.3    Pallas, V.4    Mingarro, I.5
  • 42
    • 33751007823 scopus 로고    scopus 로고
    • RNA-binding properties and membrane insertion of Melon necrotic spot virus (MNSV) double gene block movement proteins
    • Navarro, J.A., Genoves, A., Climent, J., Sauri, A., Martinez-Gil, L., Mingarro, I., and, Pallas, V., (2006) RNA-binding properties and membrane insertion of Melon necrotic spot virus (MNSV) double gene block movement proteins. Virology, 356, 57-67.
    • (2006) Virology , vol.356 , pp. 57-67
    • Navarro, J.A.1    Genoves, A.2    Climent, J.3    Sauri, A.4    Martinez-Gil, L.5    Mingarro, I.6    Pallas, V.7
  • 43
    • 78751647617 scopus 로고    scopus 로고
    • Cellular pathways for viral transport through plasmodesmata
    • Niehl, A., and, Heinlein, M., (2011) Cellular pathways for viral transport through plasmodesmata. Protoplasma, 248, 75-99.
    • (2011) Protoplasma , vol.248 , pp. 75-99
    • Niehl, A.1    Heinlein, M.2
  • 44
    • 81255143126 scopus 로고    scopus 로고
    • How do plant viruses induce disease? Interactions and interference with host components
    • Pallás, V., and, Garcia, J.A., (2011) How do plant viruses induce disease? Interactions and interference with host components. J. Gen. Virol. 92, 2691-2705.
    • (2011) J. Gen. Virol. , vol.92 , pp. 2691-2705
    • Pallás, V.1    Garcia, J.A.2
  • 45
    • 3042603709 scopus 로고    scopus 로고
    • The Golgi apparatus in mammalian and higher plant cells: A comparison
    • In (Robinson, D.G. ed.). Oxford: Blackwell Publishing
    • Pavelka, M., and, Robinson, D.G., (2003) The Golgi apparatus in mammalian and higher plant cells: a comparison. In The Golgi Apparatus and the Plant Secretory Pathway (, Robinson, D.G., ed.). Oxford: Blackwell Publishing, pp. 16-35.
    • (2003) The Golgi Apparatus and the Plant Secretory Pathway , pp. 16-35
    • Pavelka, M.1    Robinson, D.G.2
  • 46
    • 1842457749 scopus 로고    scopus 로고
    • Movement protein of a closterovirus is a type III integral transmembrane protein localized to the endoplasmic reticulum
    • Peremyslov, V.V., Pan, Y.W., and, Dolja, V.V., (2004) Movement protein of a closterovirus is a type III integral transmembrane protein localized to the endoplasmic reticulum. J. Virol. 78, 3704-3709.
    • (2004) J. Virol. , vol.78 , pp. 3704-3709
    • Peremyslov, V.V.1    Pan, Y.W.2    Dolja, V.V.3
  • 47
    • 1642377367 scopus 로고    scopus 로고
    • Measurement of dynamic protein binding to chromatin in vivo, using photobleaching microscopy
    • Phair, R.D., Gorski, S.A., and, Misteli, T., (2004) Measurement of dynamic protein binding to chromatin in vivo, using photobleaching microscopy. Methods Enzymol. 375, 393-414.
    • (2004) Methods Enzymol. , vol.375 , pp. 393-414
    • Phair, R.D.1    Gorski, S.A.2    Misteli, T.3
  • 48
    • 55049136297 scopus 로고    scopus 로고
    • FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transport and VAPB-mediated ER aggregation
    • Prosser, D.C., Tran, D., Gougeon, P.Y., Verly, C., and, Ngsee, J.K., (2008) FFAT rescues VAPA-mediated inhibition of ER-to-Golgi transport and VAPB-mediated ER aggregation. J. Cell Sci. 121, 3052-3061.
    • (2008) J. Cell Sci. , vol.121 , pp. 3052-3061
    • Prosser, D.C.1    Tran, D.2    Gougeon, P.Y.3    Verly, C.4    Ngsee, J.K.5
  • 49
    • 77956918456 scopus 로고    scopus 로고
    • Identification of a site in Sar1 involved in the interaction with the cytoplasmic tail of glycolipid glycosyltransferases
    • Quintero, C.A., Giraudo, C.G., Villarreal, M., Montich, G., and, Maccioni, H.J., (2010) Identification of a site in Sar1 involved in the interaction with the cytoplasmic tail of glycolipid glycosyltransferases. J. Biol. Chem. 285, 30340-30346.
    • (2010) J. Biol. Chem. , vol.285 , pp. 30340-30346
    • Quintero, C.A.1    Giraudo, C.G.2    Villarreal, M.3    Montich, G.4    Maccioni, H.J.5
  • 50
    • 84886533018 scopus 로고    scopus 로고
    • The cytosolic nucleoprotein of the plant-infecting bunyavirus Tomato spotted wilt recruits endoplasmic reticulum-resident proteins to endoplasmic reticulum export sites
    • Ribeiro, D., Jung, M., Moling, S., Borst, J.W., Goldbach, R., and, Kormelink, R., (2013) The cytosolic nucleoprotein of the plant-infecting bunyavirus Tomato spotted wilt recruits endoplasmic reticulum-resident proteins to endoplasmic reticulum export sites. Plant Cell, 25, 3602-3614.
    • (2013) Plant Cell , vol.25 , pp. 3602-3614
    • Ribeiro, D.1    Jung, M.2    Moling, S.3    Borst, J.W.4    Goldbach, R.5    Kormelink, R.6
  • 53
    • 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., (2006) Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane. J. Exp. Bot. 57, 43-50.
    • (2006) J. Exp. Bot. , vol.57 , pp. 43-50
    • Runions, J.1    Brach, T.2    Kuhner, S.3    Hawes, C.4
  • 54
    • 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., (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
  • 55
    • 58149185093 scopus 로고    scopus 로고
    • Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes
    • Schoberer, J., Vavra, U., Stadlmann, J., Hawes, C., Mach, L., Steinkellner, H., and, Strasser, R., (2009) Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes. Traffic, 10, 101-115.
    • (2009) Traffic , vol.10 , pp. 101-115
    • Schoberer, J.1    Vavra, U.2    Stadlmann, J.3    Hawes, C.4    Mach, L.5    Steinkellner, H.6    Strasser, R.7
  • 56
    • 80053463385 scopus 로고    scopus 로고
    • Intracellular transport of plant viruses: Finding the door out of the cell
    • Schoelz, J.E., Harries, P.A., and, Nelson, R.S., (2011) Intracellular transport of plant viruses: finding the door out of the cell. Mol. Plant, 4, 813-831.
    • (2011) Mol. Plant , vol.4 , pp. 813-831
    • Schoelz, J.E.1    Harries, P.A.2    Nelson, R.S.3
  • 57
    • 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., and, 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
  • 58
    • 75649083805 scopus 로고    scopus 로고
    • Movement and remodeling of the endoplasmic reticulum in nondividing cells of tobacco leaves
    • Sparkes, I., Runions, J., Hawes, C., and, Griffing, L., (2009a) Movement and remodeling of the endoplasmic reticulum in nondividing cells of tobacco leaves. Plant Cell, 21, 3937-3949.
    • (2009) Plant Cell , vol.21 , pp. 3937-3949
    • Sparkes, I.1    Runions, J.2    Hawes, C.3    Griffing, L.4
  • 59
    • 64849095076 scopus 로고    scopus 로고
    • Grab a Golgi: Laser trapping of Golgi bodies reveals in vivo interactions with the endoplasmic reticulum
    • Sparkes, I.A., Ketelaar, T., de Ruijter, N.C., and, Hawes, C., (2009b) Grab a Golgi: laser trapping of Golgi bodies reveals in vivo interactions with the endoplasmic reticulum. Traffic, 10, 567-571.
    • (2009) Traffic , vol.10 , pp. 567-571
    • Sparkes, I.A.1    Ketelaar, T.2    De Ruijter, N.C.3    Hawes, C.4
  • 60
    • 0028855261 scopus 로고
    • The plant Golgi apparatus: Structure, functional organization and trafficking mechanisms
    • Staehelin, L.A., and, Moore, I., (1995) The plant Golgi apparatus: structure, functional organization and trafficking mechanisms. Annu. Rev. Plant Physiol. Plant Mol. Biol. 46, 261-288.
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 261-288
    • Staehelin, L.A.1    Moore, I.2
  • 61
    • 0037423182 scopus 로고    scopus 로고
    • A 14-amino acid sequence with a β-turn structure is required for apical membrane sorting of the rat ileal bile acid transporter
    • Sun, A.Q., Salkar, R., Sachchidanand, S., Xu, S., Zeng, L., Zhou, M.M., and, Suchy, F.J., (2003) A 14-amino acid sequence with a β-turn structure is required for apical membrane sorting of the rat ileal bile acid transporter. J. Biol. Chem. 278, 4000-4009.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4000-4009
    • Sun, A.Q.1    Salkar, R.2    Sachchidanand, S.3    Xu, S.4    Zeng, L.5    Zhou, M.M.6    Suchy, F.J.7
  • 62
    • 70350446986 scopus 로고    scopus 로고
    • A novel endoplasmic reticulum export signal: Proline at the +2-position from the signal peptide cleavage site
    • Tsukumo, Y., Tsukahara, S., Saito, S., Tsuruo, T., and, Tomida, A., (2009) A novel endoplasmic reticulum export signal: proline at the +2-position from the signal peptide cleavage site. J. Biol. Chem. 284, 27500-27510.
    • (2009) J. Biol. Chem. , vol.284 , pp. 27500-27510
    • Tsukumo, Y.1    Tsukahara, S.2    Saito, S.3    Tsuruo, T.4    Tomida, A.5
  • 64
    • 84861210660 scopus 로고    scopus 로고
    • Interaction of the trans-frame potyvirus protein P3N-PIPO with host protein PCaP1 facilitates potyvirus movement
    • Vijayapalani, P., Maeshima, M., Nagasaki-Takekuchi, N., and, Miller, W.A., (2012) Interaction of the trans-frame potyvirus protein P3N-PIPO with host protein PCaP1 facilitates potyvirus movement. PLoS Pathog. 8, e1002639.
    • (2012) PLoS Pathog. , vol.8
    • Vijayapalani, P.1    Maeshima, M.2    Nagasaki-Takekuchi, N.3    Miller, W.A.4
  • 65
    • 34547866723 scopus 로고    scopus 로고
    • Intracellular trafficking of Potato leafroll virus movement protein in transgenic Arabidopsis
    • Vogel, F., Hofius, D., and, Sonnewald, U., (2007) Intracellular trafficking of Potato leafroll virus movement protein in transgenic Arabidopsis. Traffic, 8, 1205-1214.
    • (2007) Traffic , vol.8 , pp. 1205-1214
    • Vogel, F.1    Hofius, D.2    Sonnewald, U.3
  • 66
    • 3042581415 scopus 로고    scopus 로고
    • The ins and outs of non-destructive cell-to-cell and systemic movement of plant viruses
    • Waigmann, E., Ueki, S., Trutnyeva, K., and, Citovsky, V., (2004) The ins and outs of non-destructive cell-to-cell and systemic movement of plant viruses. Crit. Rev. Plant Sci. 23, 195-250.
    • (2004) Crit. Rev. Plant Sci. , vol.23 , pp. 195-250
    • Waigmann, E.1    Ueki, S.2    Trutnyeva, K.3    Citovsky, V.4
  • 67
    • 77954687469 scopus 로고    scopus 로고
    • Formation of complexes at plasmodesmata for potyvirus intercellular movement is mediated by the viral protein P3N-PIPO
    • Wei, T.Y., Zhang, C.W., Hong, J.A., Xiong, R.Y., Kasschau, K.D., Zhou, X.P., Carrington, J.C., and, Wang, A.M., (2010) Formation of complexes at plasmodesmata for potyvirus intercellular movement is mediated by the viral protein P3N-PIPO. PLoS Pathog. 6, e1000962.
    • (2010) PLoS Pathog. , vol.6
    • Wei, T.Y.1    Zhang, C.W.2    Hong, J.A.3    Xiong, R.Y.4    Kasschau, K.D.5    Zhou, X.P.6    Carrington, J.C.7    Wang, A.M.8
  • 68
    • 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., (2005) 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, 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
  • 69
    • 79957618532 scopus 로고    scopus 로고
    • The early secretory pathway and an actin-myosin VIII motility system are required for plasmodesmatal localization of the NSvc4 protein of Rice stripe virus
    • Yuan, Z.J., Chen, H.Y., Chen, Q., Omura, T., Xie, L.H., Wu, Z.J., and, Wei, T.Y., (2011) The early secretory pathway and an actin-myosin VIII motility system are required for plasmodesmatal localization of the NSvc4 protein of Rice stripe virus. Virus Res. 159, 62-68.
    • (2011) Virus Res. , vol.159 , pp. 62-68
    • Yuan, Z.J.1    Chen, H.Y.2    Chen, Q.3    Omura, T.4    Xie, L.H.5    Wu, Z.J.6    Wei, T.Y.7
  • 71
    • 78650169719 scopus 로고    scopus 로고
    • SPIKE1 signals originate from and assemble specialized domains of the endoplasmic reticulum
    • Zhang, C., Kotchoni, S.O., Samuels, A.L., and, Szymanski, D.B., (2010) SPIKE1 signals originate from and assemble specialized domains of the endoplasmic reticulum. Curr. Biol. 20, 2144-2149.
    • (2010) Curr. Biol. , vol.20 , pp. 2144-2149
    • Zhang, C.1    Kotchoni, S.O.2    Samuels, A.L.3    Szymanski, D.B.4


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