메뉴 건너뛰기




Volumn 8, Issue 8, 2013, Pages

Unconventional pathways of secretory plant proteins from the endoplasmic reticulum to the vacuole bypassing the Golgi complex

Author keywords

Endoplasmic reticulum; Golgi; Plant; Secretory pathway; Unconventional transport; Vacuole

Indexed keywords

VEGETABLE PROTEIN;

EID: 84881050636     PISSN: 15592316     EISSN: 15592324     Source Type: Journal    
DOI: 10.4161/psb.25129     Document Type: Review
Times cited : (20)

References (41)
  • 1
    • 21444434554 scopus 로고    scopus 로고
    • Sorting of proteins to storage vacuoles: How many mechanisms?
    • PMID:15950520
    • Vitale A, Hinz G. Sorting of proteins to storage vacuoles: how many mechanisms? Trends Plant Sci 2005; 10:316-23. PMID:15950520; http://dx.doi.org/10.1016/j.tplants.2005.05.001
    • (2005) Trends Plant Sci , vol.10 , pp. 316-323
    • Vitale, A.1    Hinz, G.2
  • 2
    • 57749091611 scopus 로고    scopus 로고
    • Sorting and anterograde trafficking at the Golgi apparatus
    • PMID:18838501
    • Hwang I. Sorting and anterograde trafficking at the Golgi apparatus. Plant Physiol 2008; 148:673-83. PMID:18838501; http://dx.doi.org/10.1104/pp.108.124925
    • (2008) Plant Physiol , vol.148 , pp. 673-683
    • Hwang, I.1
  • 3
    • 78650452484 scopus 로고    scopus 로고
    • Plant RMR proteins: Unique vacuolar sorting receptors that couple ligand sorting with membrane internalization
    • PMID:21078125
    • Wang H, Rogers JC, Jiang L. Plant RMR proteins: unique vacuolar sorting receptors that couple ligand sorting with membrane internalization. FEBS J 2011; 278:59-68. PMID:21078125; http://dx.doi.org/10.1111/j.1742-4658.2010.07923.x
    • (2011) FEBS J , vol.278 , pp. 59-68
    • Wang, H.1    Rogers, J.C.2    Jiang, L.3
  • 4
    • 84874106315 scopus 로고    scopus 로고
    • Vacuolar protein sorting mechanisms in plants
    • PMID:23241209
    • Xiang L, Etxeberria E, Van den Ende W. Vacuolar protein sorting mechanisms in plants. FEBS J 2013; 280:979-93. PMID:23241209; http://dx.doi.org/10.1111/febs.12092.
    • (2013) FEBS J , vol.280 , pp. 979-993
    • Xiang, L.1    Etxeberria, E.2    Van den Ende, W.3
  • 5
    • 56349091771 scopus 로고    scopus 로고
    • Endoplasmic reticulum bodies: Solving the insoluble
    • PMID:18824401
    • Herman EM. Endoplasmic reticulum bodies: solving the insoluble. Curr Opin Plant Biol 2008; 11:672-9. PMID:18824401; http://dx.doi.org/10.1016/j. pbi.2008.08.004.
    • (2008) Curr Opin Plant Biol , vol.11 , pp. 672-679
    • Herman, E.M.1
  • 6
    • 16544372267 scopus 로고    scopus 로고
    • Endoplasmic reticulum to vacuole trafficking of endoplasmic reticulum bodies provides an alternate pathway for protein transfer to the vacuole
    • PMID:15542498
    • Herman EM, Schmidt M. Endoplasmic reticulum to vacuole trafficking of endoplasmic reticulum bodies provides an alternate pathway for protein transfer to the vacuole. Plant Physiol 2004; 136:3440-6. PMID:15542498; http://dx.doi.org/10.1104/pp.104.051722
    • (2004) Plant Physiol , vol.136 , pp. 3440-3446
    • Herman, E.M.1    Schmidt, M.2
  • 7
    • 84857758872 scopus 로고    scopus 로고
    • A new type of compartment, defined by plant-specific Atg8-interacting proteins, is induced upon exposure of Arabidopsis plants to carbon starvation
    • PMID:22253227
    • Honig A, Avin-Wittenberg T, Ufaz S, Galili G. A new type of compartment, defined by plant-specific Atg8-interacting proteins, is induced upon exposure of Arabidopsis plants to carbon starvation. Plant Cell 2012; 24:288-303. PMID:22253227; http://dx.doi.org/10.1105/tpc.111.093112
    • (2012) Plant Cell , vol.24 , pp. 288-303
    • Honig, A.1    Avin-Wittenberg, T.2    Ufaz, S.3    Galili, G.4
  • 8
    • 84875696506 scopus 로고    scopus 로고
    • Traffic of human α-mannosidase in plant cells suggests the presence of a new endoplasmic reticulum-to-vacuole pathway without involving the Golgi complex
    • PMID:234496462
    • De Marchis F, Bellucci M, Pompa A. Traffic of human α-mannosidase in plant cells suggests the presence of a new endoplasmic reticulum-to-vacuole pathway without involving the Golgi complex. Plant Physiol 2013; 161:1769-8. PMID:234496462; http://dx.doi.org/10.1104/pp.113.214536
    • (2013) Plant Physiol , vol.161 , pp. 1768-1769
    • de Marchis, F.1    Bellucci, M.2    Pompa, A.3
  • 9
    • 0002284514 scopus 로고
    • Sorting of proteins in the secretory system. Annual Review of Plant Physiology and lant
    • Chrispeels MJ. Sorting of proteins in the secretory system. Annual Review of Plant Physiology and lant. Mol Biol 1991; 42:21-53;
    • (1991) Mol Biol , vol.42 , pp. 21-53
    • Chrispeels, M.J.1
  • 10
    • 84878129672 scopus 로고    scopus 로고
    • Traffic routes and signals for the tonoplast
    • PMID:23356396
    • Pedrazzini E, Komarova NY, Rentsch D, Vitale A. Traffic routes and signals for the tonoplast. Traffic 2013; 14:622-8.http://dx.doi.org/10.1111/tra.12051. PMID:23356396
    • (2013) Traffic , vol.14 , pp. 622-628
    • Pedrazzini, E.1    Komarova, N.Y.2    Rentsch, D.3    Vitale, A.4
  • 11
    • 0030014157 scopus 로고    scopus 로고
    • Plant cells contain two functionally distinct vacuolar compartments
    • PMID:8653791
    • Paris N, Stanley CM, Jones RL, Rogers JC. Plant cells contain two functionally distinct vacuolar compartments. Cell 1996; 85:563-72. PMID:8653791; http://dx.doi.org/10.1016/S0092-8674(00)81256-8
    • (1996) Cell , vol.85 , pp. 563-572
    • Paris, N.1    Stanley, C.M.2    Jones, R.L.3    Rogers, J.C.4
  • 12
    • 0001069047 scopus 로고
    • Tonoplast and soluble vacuolar proteins are targeted by different mechanisms
    • PMID:12271099
    • Gomez L, Chrispeels MJ. Tonoplast and soluble vacuolar proteins are targeted by different mechanisms. Plant Cell 1993; 5:1113-24. PMID:12271099
    • (1993) Plant Cell , vol.5 , pp. 1113-1124
    • Gomez, L.1    Chrispeels, M.J.2
  • 14
    • 0032583163 scopus 로고    scopus 로고
    • Integral membrane protein sorting to vacuoles in plant cells: Evidence for two pathways
    • PMID:9832548
    • Jiang L, Rogers JC. Integral membrane protein sorting to vacuoles in plant cells: evidence for two pathways. J Cell Biol 1998; 143:1183-99. PMID:9832548; http://dx.doi.org/10.1083/jcb.143.5.1183
    • (1998) J Cell Biol , vol.143 , pp. 1183-1199
    • Jiang, L.1    Rogers, J.C.2
  • 15
    • 84866026793 scopus 로고    scopus 로고
    • A small molecule inhibitor partitions two distinct pathways for trafficking of tonoplast intrinsic proteins in Arabidopsis
    • PMID:22957103;
    • Rivera-Serrano EE, Rodriguez-Welsh MF, Hicks GR, Rojas-Pierce M. A small molecule inhibitor partitions two distinct pathways for trafficking of tonoplast intrinsic proteins in Arabidopsis. PLoS ONE 2012; 7:e44735. PMID:22957103; http://dx.doi.org/10.1371/journal.pone.0044735
    • (2012) PLoS ONE , vol.7
    • Rivera-Serrano, E.E.1    Rodriguez-Welsh, M.F.2    Hicks, G.R.3    Rojas-Pierce, M.4
  • 16
    • 79953090330 scopus 로고    scopus 로고
    • Rice two-pore K channels are expressed in different types of vacuoles
    • PMID:21224427
    • Isayenkov S, Isner JC, Maathuis FJ. Rice two-pore K channels are expressed in different types of vacuoles. Plant Cell 2011; 23:756-68. PMID:21224427; http://dx.doi.org/10.1105/tpc.110.081463
    • (2011) Plant Cell , vol.23 , pp. 756-768
    • Isayenkov, S.1    Isner, J.C.2    Maathuis, F.J.3
  • 17
    • 73849141867 scopus 로고    scopus 로고
    • CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores
    • PMID:19832944
    • Batistic O, Waadt R, Steinhorst L, Held K, Kudla J. CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores. Plant J 2010; 61:211-22. PMID:19832944; http://dx.doi.org/10.1111/j.1365-313X.2009.04045.x
    • (2010) Plant J , vol.61 , pp. 211-222
    • Batistic, O.1    Waadt, R.2    Steinhorst, L.3    Held, K.4    Kudla, J.5
  • 18
    • 80053199138 scopus 로고    scopus 로고
    • Vacuolar transport in tobacco leaf epidermis cells involves a single route for soluble cargo and multiple routes for membrane cargo
    • PMID:21856792
    • Bottanelli F, Foresti O, Hanton S, Denecke J. Vacuolar transport in tobacco leaf epidermis cells involves a single route for soluble cargo and multiple routes for membrane cargo. Plant Cell 2011; 23:3007-25. PMID:21856792; http://dx.doi.org/10.1105/tpc.111.085480.
    • (2011) Plant Cell , vol.23 , pp. 3007-3025
    • Bottanelli, F.1    Foresti, O.2    Hanton, S.3    Denecke, J.4
  • 19
    • 0033840913 scopus 로고    scopus 로고
    • Endoplasmic reticulum-derived compartments function in storage and as mediators of vacuolar remodeling via a new type of organelle, precursor protease vesicles
    • PMID:10938342
    • Chrispeels MJ, Herman EM. Endoplasmic reticulum-derived compartments function in storage and as mediators of vacuolar remodeling via a new type of organelle, precursor protease vesicles. Plant Physiol 2000; 123:1227-34. PMID:10938342; http://dx.doi. org/10.1104/pp.123.4.1227
    • (2000) Plant Physiol , vol.123 , pp. 1227-1234
    • Chrispeels, M.J.1    Herman, E.M.2
  • 20
    • 0026478698 scopus 로고
    • Evidence for a novel route of wheat storage proteins to vacuoles
    • PMID:1447291
    • Levanony H, Rubin R, Altschuler Y, Galili G. Evidence for a novel route of wheat storage proteins to vacuoles. J Cell Biol 1992; 119:1117-28. PMID:1447291; http://dx.doi.org/10.1083/jcb.119.5.1117
    • (1992) J Cell Biol , vol.119 , pp. 1117-1128
    • Levanony, H.1    Rubin, R.2    Altschuler, Y.3    Galili, G.4
  • 21
    • 14644429029 scopus 로고    scopus 로고
    • A novel vesicle derived directly from endoplasmic reticulum is involved in the transport of vacuolar storage proteins in rice endosperm
    • PMID:15659439
    • Takahashi H, Saito Y, Kitagawa T, Morita S, Masumura T, Tanaka K. A novel vesicle derived directly from endoplasmic reticulum is involved in the transport of vacuolar storage proteins in rice endosperm. Plant Cell Physiol 2005; 46:245-9. PMID:15659439; http://dx.doi.org/10.1093/pcp/pci019
    • (2005) Plant Cell Physiol , vol.46 , pp. 245-249
    • Takahashi, H.1    Saito, Y.2    Kitagawa, T.3    Morita, S.4    Masumura, T.5    Tanaka, K.6
  • 22
    • 6444239665 scopus 로고    scopus 로고
    • The composition of newly synthesized proteins in the endoplasmic reticulum determines the transport pathways of soybean seed storage proteins
    • PMID:15447650
    • Mori T, Maruyama N, Nishizawa K, Higasa T, Yagasaki K, Ishimoto M, et al. The composition of newly synthesized proteins in the endoplasmic reticulum determines the transport pathways of soybean seed storage proteins. Plant J 2004; 40:238-49. PMID:15447650; http://dx.doi.org/10.1111/j.1365-313X.2004.02204.x
    • (2004) Plant J , vol.40 , pp. 238-249
    • Mori, T.1    Maruyama, N.2    Nishizawa, K.3    Higasa, T.4    Yagasaki, K.5    Ishimoto, M.6
  • 23
    • 79953088489 scopus 로고    scopus 로고
    • Delivery of prolamins to the protein storage vacuole in maize aleurone cells
    • PMID:21343414;
    • Reyes FC, Chung T, Holding D, Jung R, Vierstra R, Otegui MS. Delivery of prolamins to the protein storage vacuole in maize aleurone cells. Plant Cell 2011; 23:769-84. PMID:21343414; http://dx.doi.org/10.1105/tpc.110.082156
    • (2011) Plant Cell , vol.23 , pp. 769-784
    • Reyes, F.C.1    Chung, T.2    Holding, D.3    Jung, R.4    Vierstra, R.5    Otegui, M.S.6
  • 24
    • 0031795695 scopus 로고    scopus 로고
    • Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles
    • PMID:9596640
    • Hara-Nishimura I, Shimada T, Hatano K, Takeuchi Y, Nishimura M. Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles. Plant Cell 1998; 10:825-36. PMID:9596640
    • (1998) Plant Cell , vol.10 , pp. 825-836
    • Hara-Nishimura, I.1    Shimada, T.2    Hatano, K.3    Takeuchi, Y.4    Nishimura, M.5
  • 25
    • 0034797989 scopus 로고    scopus 로고
    • A proteinase-storing body that prepares for cell death or stresses in the epidermal cells of Arabidopsis
    • PMID:11577182
    • Hayashi Y, Yamada K, Shimada T, Matsushima R, Nishizawa NK, Nishimura M, et al. A proteinase-storing body that prepares for cell death or stresses in the epidermal cells of Arabidopsis. Plant Cell Physiol 2001; 42:894-9. PMID:11577182; http://dx.doi.org/10.1093/pcp/pce144
    • (2001) Plant Cell Physiol , vol.42 , pp. 894-899
    • Hayashi, Y.1    Yamada, K.2    Shimada, T.3    Matsushima, R.4    Nishizawa, N.K.5    Nishimura, M.6
  • 26
    • 0038808989 scopus 로고    scopus 로고
    • A unique mechanism for protein processing and degradation in Arabidopsis thaliana
    • PMID:12773619
    • Rojo E, Zouhar J, Carter C, Kovaleva V, Raikhel NV. A unique mechanism for protein processing and degradation in Arabidopsis thaliana. Proc Natl Acad Sci USA 2003; 100:7389-94. PMID:12773619; http://dx.doi.org/10.1073/pnas.1230987100
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7389-7394
    • Rojo, E.1    Zouhar, J.2    Carter, C.3    Kovaleva, V.4    Raikhel, N.V.5
  • 27
    • 0034614933 scopus 로고    scopus 로고
    • Mass transport of proform of a KDEL-tailed cysteine proteinase (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds
    • PMID:10662772
    • Toyooka K, Okamoto T, Minamikawa T. Mass transport of proform of a KDEL-tailed cysteine proteinase (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds. J Cell Biol 2000; 148:453-64. PMID:10662772; http://dx.doi.org/10.1083/jcb.148.3.453
    • (2000) J Cell Biol , vol.148 , pp. 453-464
    • Toyooka, K.1    Okamoto, T.2    Minamikawa, T.3
  • 28
    • 0035942237 scopus 로고    scopus 로고
    • The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum
    • PMID:11296243
    • Schmid M, Simpson DJ, Sarioglu H, Lottspeich F, Gietl C. The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum. Proc Natl Acad Sci USA 2001; 98:5353-8. PMID:11296243; http://dx.doi.org/10.1073/pnas.061038298
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5353-5358
    • Schmid, M.1    Simpson, D.J.2    Sarioglu, H.3    Lottspeich, F.4    Gietl, C.5
  • 29
    • 83255189504 scopus 로고    scopus 로고
    • Unique defense strategy by the endoplasmic reticulum body in plants
    • PMID:22102697
    • Yamada K, Hara-Nishimura I, Nishimura M. Unique defense strategy by the endoplasmic reticulum body in plants. Plant Cell Physiol 2011; 52:2039-49. PMID:22102697; http://dx.doi.org/10.1093/pcp/pcr156.
    • (2011) Plant Cell Physiol , vol.52 , pp. 2039-2049
    • Yamada, K.1    Hara-Nishimura, I.2    Nishimura, M.3
  • 30
    • 16544378458 scopus 로고    scopus 로고
    • Diversity and formation of endoplasmic reticulum-derived compartments in plants. Are these compartments specific to plant cells?
    • PMID:15542497
    • Hara-Nishimura I, Matsushima R, Shimada T, Nishimura M. Diversity and formation of endoplasmic reticulum-derived compartments in plants. Are these compartments specific to plant cells? Plant Physiol 2004; 136:3435-9. PMID:15542497; http://dx.doi.org/10.1104/pp.104.053876
    • (2004) Plant Physiol , vol.136 , pp. 3435-3439
    • Hara-Nishimura, I.1    Matsushima, R.2    Shimada, T.3    Nishimura, M.4
  • 31
    • 84871814088 scopus 로고    scopus 로고
    • Identification of two novel endoplasmic reticulum body-specific integral membrane proteins
    • PMID:23166355
    • Yamada K, Nagano AJ, Nishina M, Hara-Nishimura I, Nishimura M. Identification of two novel endoplasmic reticulum body-specific integral membrane proteins. Plant Physiol 2013; 161:108-20. PMID:23166355; http://dx.doi.org/10.1104/pp.112.207654
    • (2013) Plant Physiol , vol.161 , pp. 108-120
    • Yamada, K.1    Nagano, A.J.2    Nishina, M.3    Hara-Nishimura, I.4    Nishimura, M.5
  • 32
    • 0031080071 scopus 로고    scopus 로고
    • The C-terminal HDEL sequence is sufficient for retention of secretory proteins in the endoplasmic reticulum (ER) but promotes vacuolar targeting of proteins that escape the ER
    • PMID:9076996
    • Gomord V, Denmat LA, Fitchette-Lainé AC, Satiat-Jeunemaitre B, Hawes C, Faye L. The C-terminal HDEL sequence is sufficient for retention of secretory proteins in the endoplasmic reticulum (ER) but promotes vacuolar targeting of proteins that escape the ER. Plant J 1997; 11:313-25. PMID:9076996; http://dx.doi.org/10.1046/j.1365-313X.1997.11020313.x
    • (1997) Plant J , vol.11 , pp. 313-325
    • Gomord, V.1    Denmat, L.A.2    Fitchette-Lainé, A.C.3    Satiat-Jeunemaitre, B.4    Hawes, C.5    Faye, L.6
  • 33
    • 0034997285 scopus 로고    scopus 로고
    • Influence of KDEL on the fate of trimeric or assembly-defective phaseolin: Selective use of an alternative route to vacuoles
    • PMID:11340185
    • Frigerio L, Pastres A, Prada A, Vitale A. Influence of KDEL on the fate of trimeric or assembly-defective phaseolin: selective use of an alternative route to vacuoles. Plant Cell 2001; 13:1109-26. PMID:11340185
    • (2001) Plant Cell , vol.13 , pp. 1109-1126
    • Frigerio, L.1    Pastres, A.2    Prada, A.3    Vitale, A.4
  • 34
    • 3843103539 scopus 로고    scopus 로고
    • Endoplasmic reticulum-resident proteins are constitutively transported to vacuoles for degradation
    • PMID:15255868
    • Tamura K, Yamada K, Shimada T, Hara-Nishimura I. Endoplasmic reticulum-resident proteins are constitutively transported to vacuoles for degradation. Plant J 2004; 39:393-402. PMID:15255868; http://dx.doi.org/10.1111/j.1365-313X.2004.02141.x
    • (2004) Plant J , vol.39 , pp. 393-402
    • Tamura, K.1    Yamada, K.2    Shimada, T.3    Hara-Nishimura, I.4
  • 35
    • 33645737420 scopus 로고    scopus 로고
    • Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway
    • PMID:16339854
    • Pimpl P, Taylor JP, Snowden C, Hillmer S, Robinson DG, Denecke J. Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway. Plant Cell 2006; 18:198-211. PMID:16339854; http://dx.doi.org/10.1105/tpc.105.036665
    • (2006) Plant Cell , vol.18 , pp. 198-211
    • Pimpl, P.1    Taylor, J.P.2    Snowden, C.3    Hillmer, S.4    Robinson, D.G.5    Denecke, J.6
  • 36
    • 34248356819 scopus 로고    scopus 로고
    • EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites
    • PMID:17360537
    • Zuber C, Cormier JH, Guhl B, Santimaria R, Hebert DN, Roth J. EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites. Proc Natl Acad Sci USA 2007; 104:4407-12. PMID:17360537; http://dx.doi.org/10.1073/pnas.0700154104
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4407-4412
    • Zuber, C.1    Cormier, J.H.2    Guhl, B.3    Santimaria, R.4    Hebert, D.N.5    Roth, J.6
  • 37
    • 43549087339 scopus 로고    scopus 로고
    • Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities
    • PMID:18452703
    • Calì T, Galli C, Olivari S, Molinari M. Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities. Biochem Biophys Res Commun 2008; 371:405-10. PMID:18452703; http://dx.doi.org/10.1016/j.bbrc.2008.04.098
    • (2008) Biochem Biophys Res Commun , vol.371 , pp. 405-410
    • Calì, T.1    Galli, C.2    Olivari, S.3    Molinari, M.4
  • 38
    • 84863866336 scopus 로고    scopus 로고
    • Golgi bypass: Skirting around the heart of classical secretion
    • PMID:21441587
    • Grieve AG, Rabouille C. Golgi bypass: skirting around the heart of classical secretion. Cold Spring Harb Perspect Biol 2011; 3:a005298. PMID:21441587; http://dx.doi.org/10.1101/cshperspect.a005298
    • (2011) Cold Spring Harb Perspect Biol , vol.3
    • Grieve, A.G.1    Rabouille, C.2
  • 39
    • 77950179262 scopus 로고    scopus 로고
    • An engineered C-terminal disulfide bond can partially replace the phaseolin vacuolar sorting signal
    • PMID:20030752
    • Pompa A, De Marchis F, Vitale A, Arcioni S, Bellucci M. An engineered C-terminal disulfide bond can partially replace the phaseolin vacuolar sorting signal. Plant J 2010; 61:782-91. PMID:20030752
    • (2010) Plant J , vol.61 , pp. 782-791
    • Pompa, A.1    de Marchis, F.2    Vitale, A.3    Arcioni, S.4    Bellucci, M.5
  • 40
    • 77952175947 scopus 로고    scopus 로고
    • Sorting of plant vacuolar proteins is initiated in the ER
    • PMID:20149141
    • Niemes S, Labs M, Scheuring D, Krueger F, Langhans M, Jesenofsky B, et al. Sorting of plant vacuolar proteins is initiated in the ER. Plant J 2010; 62:601-14. PMID:20149141; http://dx.doi.org/10.1111/j.1365-313X.2010.04171.x
    • (2010) Plant J , vol.62 , pp. 601-614
    • Niemes, S.1    Labs, M.2    Scheuring, D.3    Krueger, F.4    Langhans, M.5    Jesenofsky, B.6
  • 41
    • 0031439665 scopus 로고    scopus 로고
    • A pumpkin 72-kDa membrane protein of precursor-accumulating vesicles has characteristics of a vacuolar sorting receptor
    • PMID:9522472
    • Shimada T, Kuroyanagi M, Nishimura M, Hara-Nishimura I. A pumpkin 72-kDa membrane protein of precursor-accumulating vesicles has characteristics of a vacuolar sorting receptor. Plant Cell Physiol 1997; 38:1414-20. PMID:9522472; http://dx.doi.org/10.1093/oxfordjournals.pcp.a029138
    • (1997) Plant Cell Physiol , vol.38 , pp. 1414-1420
    • Shimada, T.1    Kuroyanagi, M.2    Nishimura, M.3    Hara-Nishimura, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.