메뉴 건너뛰기




Volumn 109, Issue 10, 1996, Pages 2539-2550

Transport of storage proteins to the vacuole is mediated by vesicles without a clathrin coat

Author keywords

TIP; Clathrin coated vesicle; Complex glycan; Pea cotyledon; Protein storage vacuole; Storage polypeptide

Indexed keywords

ACID HYDROLASE; AVENIN; CELL PROTEIN; CLATHRIN; GLYCOPROTEIN;

EID: 0029860460     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (141)

References (66)
  • 1
    • 0029119236 scopus 로고
    • An Arabidopsis syntaxin homolog isolated by functional complementation of a yeast pep 12 mutant
    • Bassham, D. C., Gal, S., Conceicao, A. D. and Raikhel, N. V. (1995). An Arabidopsis syntaxin homolog isolated by functional complementation of a yeast pep 12 mutant. Proc. Nat. Acad. Sci. USA 92, 7262-7266.
    • (1995) Proc. Nat. Acad. Sci. USA , vol.92 , pp. 7262-7266
    • Bassham, D.C.1    Gal, S.2    Conceicao, A.D.3    Raikhel, N.V.4
  • 2
    • 0002678814 scopus 로고    scopus 로고
    • Transport proteins in the plama membrane and the secretory system
    • Bassham, D. C. and Raikhel, N. V. (1996). Transport proteins in the plama membrane and the secretory system. Trends Plant Sci. 1, 15-20.
    • (1996) Trends Plant Sci. , vol.1 , pp. 15-20
    • Bassham, D.C.1    Raikhel, N.V.2
  • 3
    • 0012466866 scopus 로고
    • The presence of protease digestible material in Golgi vesicles during endosperm development of selected cereals
    • Bechtel, D. B. and Gaines, R. L. (1982). The presence of protease digestible material in Golgi vesicles during endosperm development of selected cereals. Am. J. Bot. 69, 880-884.
    • (1982) Am. J. Bot. , vol.69 , pp. 880-884
    • Bechtel, D.B.1    Gaines, R.L.2
  • 4
    • 0000122262 scopus 로고
    • Anterograde transport of algal scales through the Golgi complex is not mediated by vesicles
    • Becker, B., Böllinger, B. and Melkonian, M. (1995). Anterograde transport of algal scales through the Golgi complex is not mediated by vesicles. Trends Cell Biol. 5, 305-306.
    • (1995) Trends Cell Biol. , vol.5 , pp. 305-306
    • Becker, B.1    Böllinger, B.2    Melkonian, M.3
  • 5
    • 0028814446 scopus 로고
    • Intra-Golgi transport mediated by vesicles?
    • Becker, B. and Melkonian, M. (1995). Intra-Golgi transport mediated by vesicles? Botanica Acta 108, 172-173.
    • (1995) Botanica Acta , vol.108 , pp. 172-173
    • Becker, B.1    Melkonian, M.2
  • 6
    • 0029848444 scopus 로고    scopus 로고
    • Clathrin-coated vesicles in plants
    • Beevers, L. (1996). Clathrin-coated vesicles in plants. Int. Rev. Cytol. 167, 1-35.
    • (1996) Int. Rev. Cytol. , vol.167 , pp. 1-35
    • Beevers, L.1
  • 7
    • 0030345815 scopus 로고    scopus 로고
    • Origin of lysosomal proteins
    • ed. J. B. Lloyd and R. W. Mason. Plenum Press, New York (in press)
    • Braulke, T. (1996). Origin of lysosomal proteins. In Biology of the Lysosome. Subcellular Biochemistry; vol. 27 (ed. J. B. Lloyd and R. W. Mason). Plenum Press, New York (in press).
    • (1996) Biology of the Lysosome. Subcellular Biochemistry , vol.27
    • Braulke, T.1
  • 8
    • 0018436334 scopus 로고
    • Immunoaffinity chromatography as a means of purifying legumin from Pisum (pea) seeds
    • Casey, R. D. (1979). Immunoaffinity chromatography as a means of purifying legumin from Pisum (pea) seeds. Biochem. J. 177, 509-520.
    • (1979) Biochem. J. , vol.177 , pp. 509-520
    • Casey, R.D.1
  • 9
    • 0020132174 scopus 로고
    • Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons
    • Chrispeels, M. J., Higgins, T. J. V. and Spencer, D. (1982). Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons. J. Cell Biol. 93, 306-313.
    • (1982) J. Cell Biol. , vol.93 , pp. 306-313
    • Chrispeels, M.J.1    Higgins, T.J.V.2    Spencer, D.3
  • 10
    • 0000018342 scopus 로고
    • The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons
    • Chrispeels, M. J. (1983). The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons. Planta 158, 140-151.
    • (1983) Planta , vol.158 , pp. 140-151
    • Chrispeels, M.J.1
  • 12
    • 0026532891 scopus 로고
    • Short peptide domains target proteins to plant vacuoles
    • Chrispeels, M. J. and Raikhel, N. V. (1992). Short peptide domains target proteins to plant vacuoles. Cell 68, 613-616.
    • (1992) Cell , vol.68 , pp. 613-616
    • Chrispeels, M.J.1    Raikhel, N.V.2
  • 13
    • 0002649127 scopus 로고
    • Periodate-acid treatment of sections permits on-grid immunogold localization of pea seed vicilin in ER and Golgi
    • Craig, S. and Goodchild, D. J. (1984). Periodate-acid treatment of sections permits on-grid immunogold localization of pea seed vicilin in ER and Golgi. Protoplasma 122, 35-44.
    • (1984) Protoplasma , vol.122 , pp. 35-44
    • Craig, S.1    Goodchild, D.J.2
  • 14
    • 0000009035 scopus 로고
    • Structural aspects of protein accumulation in developing legume seeds
    • Craig, S. (1988). Structural aspects of protein accumulation in developing legume seeds. Biochem. Physiol. Pflanzen 183, 159-171.
    • (1988) Biochem. Physiol. Pflanzen , vol.183 , pp. 159-171
    • Craig, S.1
  • 15
    • 0344583446 scopus 로고
    • Improved coated vesicle isolation allows better characterization of clathrin polypeptides
    • Demmer, A., Holstein, S. E. H., Hinz, G., Schauermann, G. and Robinson, D. G. (1993). Improved coated vesicle isolation allows better characterization of clathrin polypeptides. J. Exp. Bot. 44, 23-33.
    • (1993) J. Exp. Bot. , vol.44 , pp. 23-33
    • Demmer, A.1    Holstein, S.E.H.2    Hinz, G.3    Schauermann, G.4    Robinson, D.G.5
  • 17
    • 0007391753 scopus 로고
    • The isolation and enrichment of coated vesicles from suspension-cultured carrot cells
    • Depta, H. and Robinson, D. G. (1986). The isolation and enrichment of coated vesicles from suspension-cultured carrot cells. Protoplasma 130, 162-170.
    • (1986) Protoplasma , vol.130 , pp. 162-170
    • Depta, H.1    Robinson, D.G.2
  • 18
    • 4243531386 scopus 로고
    • The deposition of vacuolar proteins in oilseeds
    • ed. G. E. Inglett, Avi. Publ. Comp. Inc., Westport
    • Dieckert, J. W. and Dieckert, M. C. (1972). The deposition of vacuolar proteins in oilseeds. In: Symposium Seed Proteins (ed. G. E. Inglett), pp. 52-85. Avi. Publ. Comp. Inc., Westport.
    • (1972) Symposium Seed Proteins , pp. 52-85
    • Dieckert, J.W.1    Dieckert, M.C.2
  • 19
    • 0030051441 scopus 로고    scopus 로고
    • The AP-1 adaptor complex binds to immature secretory granules from PC12 cells and is regulated by ADP-ribosylation factor
    • Dittié, A. S., Hajibagheri, N. and Tooze, S. A. (1996). The AP-1 adaptor complex binds to immature secretory granules from PC12 cells and is regulated by ADP-ribosylation factor. J. Cell Biol. 132, 523-536.
    • (1996) J. Cell Biol. , vol.132 , pp. 523-536
    • Dittié, A.S.1    Hajibagheri, N.2    Tooze, S.A.3
  • 20
    • 0028988844 scopus 로고
    • Demonstration of a β-type adaptin at the plant plasma membrane
    • Drucker, M., Herkt, B. and Robinson, D. G. (1995). Demonstration of a β-type adaptin at the plant plasma membrane. Cell Biol. Intern. 3, 191-201.
    • (1995) Cell Biol. Intern. , vol.3 , pp. 191-201
    • Drucker, M.1    Herkt, B.2    Robinson, D.G.3
  • 21
    • 0028248853 scopus 로고
    • Two structural domains mediate two sequential events in γ-zein targeting: Protein endoplasmic reticulum retention and protein body formation
    • Geli, M. I., Torrent, M. and Ludevid, D. (1994). Two structural domains mediate two sequential events in γ-zein targeting: protein endoplasmic reticulum retention and protein body formation. Plant Cell 6, 1911-1922.
    • (1994) Plant Cell , vol.6 , pp. 1911-1922
    • Geli, M.I.1    Torrent, M.2    Ludevid, D.3
  • 22
    • 0001069047 scopus 로고
    • Tonoplast and soluble vacuolar proteins are targeted by different mechanisms
    • Gomez, L. and Chrispeels, M. J. (1993). Tonoplast and soluble vacuolar proteins are targeted by different mechanisms. The Plant Cell 5, 1113-1124.
    • (1993) The Plant Cell , vol.5 , pp. 1113-1124
    • Gomez, L.1    Chrispeels, M.J.2
  • 23
    • 0001571108 scopus 로고
    • Immunocytochemical localization of phaesolin and phytohemagglutinin in the endoplasmic reticulum and Golgi complex of developing bean cotyledons
    • Greenwood, J. S. and Chrispeels, M. J. (1985). Immunocytochemical localization of phaesolin and phytohemagglutinin in the endoplasmic reticulum and Golgi complex of developing bean cotyledons. Planta 164, 295-302.
    • (1985) Planta , vol.164 , pp. 295-302
    • Greenwood, J.S.1    Chrispeels, M.J.2
  • 24
    • 0026100686 scopus 로고
    • Comparisons of Golgi structure and dynamics in plant and animal cells
    • Griffing, L. R. (1991). Comparisons of Golgi structure and dynamics in plant and animal cells. J. Electron Microsc. Tech. 17, 179-199.
    • (1991) J. Electron Microsc. Tech. , vol.17 , pp. 179-199
    • Griffing, L.R.1
  • 25
    • 0000651011 scopus 로고
    • Coated vesicles are involved in the transport of storage proteins during seed development in Pisum sativum L
    • Harley, S. M. and Beevers, L. (1989). Coated vesicles are involved in the transport of storage proteins during seed development in Pisum sativum L. Plant Physiol. 91, 674-678.
    • (1989) Plant Physiol. , vol.91 , pp. 674-678
    • Harley, S.M.1    Beevers, L.2
  • 26
    • 38249026010 scopus 로고
    • Correlated in situ hybridisation and immunochemical studies of legumin storage protein deposition in pea (Pisum sativum L.)
    • Harris, N., Grindley, H., Mulchrone, J. and Croy, R. D. (1989). Correlated in situ hybridisation and immunochemical studies of legumin storage protein deposition in pea (Pisum sativum L.). Cell Biol. Int. Rep. 13, 23-35.
    • (1989) Cell Biol. Int. Rep. , vol.13 , pp. 23-35
    • Harris, N.1    Grindley, H.2    Mulchrone, J.3    Croy, R.D.4
  • 27
    • 0000680069 scopus 로고
    • Multiple origins of intravacuolar protein accumulation of plant cells
    • Herman, E. M. (1994). Multiple origins of intravacuolar protein accumulation of plant cells. Advan. Struct. Biol. 3, 243-283.
    • (1994) Advan. Struct. Biol. , vol.3 , pp. 243-283
    • Herman, E.M.1
  • 28
    • 0344611479 scopus 로고
    • Strategies in the isolation of storage protein receptors
    • Hinz, G., Hoh, B. and Robinson, D. G. (1993). Strategies in the isolation of storage protein receptors. J. Exp. Bot. 44 (Suppl.), 351-357.
    • (1993) J. Exp. Bot. , vol.44 , Issue.SUPPL. , pp. 351-357
    • Hinz, G.1    Hoh, B.2    Robinson, D.G.3
  • 29
    • 8244222779 scopus 로고
    • Vegetative and seed-specific forms of tonoplast intrinsic protein in the vacuolar membrane of Arabidopsis thaliana
    • Höfte, H., Hubbard, L., Reizer, J., Ludevid, D., Herman, E. M., Chrispeels, M. J. (1992). Vegetative and seed-specific forms of tonoplast intrinsic protein in the vacuolar membrane of Arabidopsis thaliana. Plant Physiol. 99, 561-570.
    • (1992) Plant Physiol. , vol.99 , pp. 561-570
    • Höfte, H.1    Hubbard, L.2    Reizer, J.3    Ludevid, D.4    Herman, E.M.5    Chrispeels, M.J.6
  • 30
    • 85014251402 scopus 로고
    • Storage protein polypeptides in clathrin coated vesicle fractions from developing pea cotyledons are not due to endomembrane contamination
    • Hoh, B., Schauermann, G. and Robinson, D. G. (1991). Storage protein polypeptides in clathrin coated vesicle fractions from developing pea cotyledons are not due to endomembrane contamination. J. Plant Physiol. 138, 309-316.
    • (1991) J. Plant Physiol. , vol.138 , pp. 309-316
    • Hoh, B.1    Schauermann, G.2    Robinson, D.G.3
  • 31
    • 0028893601 scopus 로고
    • Protein storage vacuoles form de novo during pea cotyledon development
    • Hoh, B., Hinz, G., Jeong, B.-K. and Robinson, D. G. (1995). Protein storage vacuoles form de novo during pea cotyledon development. J. Cell Sci. 108, 299-310.
    • (1995) J. Cell Sci. , vol.108 , pp. 299-310
    • Hoh, B.1    Hinz, G.2    Jeong, B.-K.3    Robinson, D.G.4
  • 32
    • 0028178629 scopus 로고
    • Identification of a β-type adaptin in plant clathrin-coated vesicles
    • Holstein, S. E. H., Drucker, M. and Robinson, D. G. (1994). Identification of a β-type adaptin in plant clathrin-coated vesicles. J. Cell Sci. 107, 945-953.
    • (1994) J. Cell Sci. , vol.107 , pp. 945-953
    • Holstein, S.E.H.1    Drucker, M.2    Robinson, D.G.3
  • 33
    • 0001438180 scopus 로고
    • An abundant, highly conserved tonoplast protein in seeds
    • Johnson, K. D., Herman, E. M. and Chrispeels, M. J. (1989). An abundant, highly conserved tonoplast protein in seeds. Plant Physiol. 91, 1006-1013.
    • (1989) Plant Physiol. , vol.91 , pp. 1006-1013
    • Johnson, K.D.1    Herman, E.M.2    Chrispeels, M.J.3
  • 34
    • 0001150043 scopus 로고
    • Formation of wheat protein bodies: Involvement of the Golgi apparatus in gliadin transport
    • Kim, W. T., Franceschi, V. R., Krishnan, H. B. and Okita, T. W. (1988). Formation of wheat protein bodies: involvement of the Golgi apparatus in gliadin transport. Planta 176, 173-182.
    • (1988) Planta , vol.176 , pp. 173-182
    • Kim, W.T.1    Franceschi, V.R.2    Krishnan, H.B.3    Okita, T.W.4
  • 35
    • 0028201318 scopus 로고
    • Purification and initial characterization of a potential plant vacuolar targeting receptor
    • Kirsch, T., Paris, N., Bulter, J. M., Beevers, L. and Rogers, J. C. (1994). Purification and initial characterization of a potential plant vacuolar targeting receptor. Proc. Nat. Acad. Sci. USA 91, 3403-3407.
    • (1994) Proc. Nat. Acad. Sci. USA , vol.91 , pp. 3403-3407
    • Kirsch, T.1    Paris, N.2    Bulter, J.M.3    Beevers, L.4    Rogers, J.C.5
  • 36
    • 0030162062 scopus 로고    scopus 로고
    • Interaction of a potential vacuolar targeting receptor with amino- and carboxy-terminal targeting determinants
    • Kirsch, T., Saalbach, G., Raikhel, N. V. and Beevers, L. (1996). Interaction of a potential vacuolar targeting receptor with amino- and carboxy-terminal targeting determinants. Plant Physiol. 111, 469-474.
    • (1996) Plant Physiol. , vol.111 , pp. 469-474
    • Kirsch, T.1    Saalbach, G.2    Raikhel, N.V.3    Beevers, L.4
  • 38
    • 0000178962 scopus 로고
    • Immunochemical studies on the role of the Golgi complex in protein-body formation in rice seeds
    • Krishnan, H. B., Franceschi, V. R. and Okita, T. W. (1986). Immunochemical studies on the role of the Golgi complex in protein-body formation in rice seeds. Planta 169, 471-480.
    • (1986) Planta , vol.169 , pp. 471-480
    • Krishnan, H.B.1    Franceschi, V.R.2    Okita, T.W.3
  • 39
    • 0028241106 scopus 로고
    • Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic β-cells
    • Kuliawat, R. and Arvan, P. (1994). Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic β-cells. J. Cell Biol. 126, 77-86.
    • (1994) J. Cell Biol. , vol.126 , pp. 77-86
    • Kuliawat, R.1    Arvan, P.2
  • 40
    • 0024067066 scopus 로고
    • Characterization of a lectin-binding storage protein from pea (Pisum sativum)
    • Kummer, H. and Rüdiger, H. (1988). Characterization of a lectin-binding storage protein from pea (Pisum sativum). Biol. Chem. Hoppe-Seyler 369, 639-646.
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 639-646
    • Kummer, H.1    Rüdiger, H.2
  • 41
    • 0000406542 scopus 로고
    • Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins
    • Laurière, M., Laurière, C., Chrispeels, M. J., Johnson, K. D. and Sturm, A. (1989). Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins. Plant Physiol. 90, 1182-1188.
    • (1989) Plant Physiol. , vol.90 , pp. 1182-1188
    • Laurière, M.1    Laurière, C.2    Chrispeels, M.J.3    Johnson, K.D.4    Sturm, A.5
  • 42
    • 0026478698 scopus 로고
    • Evidence for a novel route of wheat storage proteins to vacuoles
    • Levanony, H., Rubin, R., Altschuler, Y. and Galili, G. (1992). Evidence for a novel route of wheat storage proteins to vacuoles. J. Cell Biol. 119, 1117-1128.
    • (1992) J. Cell Biol. , vol.119 , pp. 1117-1128
    • Levanony, H.1    Rubin, R.2    Altschuler, Y.3    Galili, G.4
  • 43
    • 0021111891 scopus 로고
    • The vicilin gene family of pea (Pisum sativum L.): A complete cDNA coding sequence for provicilin
    • Lycett, G. W., Delauney, A. J., Gatehouse, J. A., Gilroy, J., Croy, R. R. D. and Boulter, D. (1983). The vicilin gene family of pea (Pisum sativum L.): a complete cDNA coding sequence for provicilin. Nucl. Acids Res. 11, 2367-2380.
    • (1983) Nucl. Acids Res. , vol.11 , pp. 2367-2380
    • Lycett, G.W.1    Delauney, A.J.2    Gatehouse, J.A.3    Gilroy, J.4    Croy, R.R.D.5    Boulter, D.6
  • 44
    • 0021760486 scopus 로고
    • The complete nucleotide sequence of a legumin gene from pea (Pisum sativum L.)
    • Lycett, G. W., Croy, R. R. D., Shirsat, A. H. and Boulter, D. (1984). The complete nucleotide sequence of a legumin gene from pea (Pisum sativum L.). Nucl. Acids Res. 12, 4493-4506.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 4493-4506
    • Lycett, G.W.1    Croy, R.R.D.2    Shirsat, A.H.3    Boulter, D.4
  • 45
    • 0000280810 scopus 로고
    • Synthesis of an integral protein of the protein body membrane in Phaseolus vulgaris cotyledons
    • Mäder, M. and Chrispeels, M. J. (1984). Synthesis of an integral protein of the protein body membrane in Phaseolus vulgaris cotyledons. Planta 160, 330-340.
    • (1984) Planta , vol.160 , pp. 330-340
    • Mäder, M.1    Chrispeels, M.J.2
  • 46
    • 0028842134 scopus 로고
    • Antibodies to the tonoplast from the storage parenchyma cells of beetroot recognize a major intrinsic protein related to TIPs
    • Marty-Mazars, D., Clémencet, M.-C., Dozolme, P. and Marty, F. (1995). Antibodies to the tonoplast from the storage parenchyma cells of beetroot recognize a major intrinsic protein related to TIPs. Eur. J. Cell Biol. 66, 106-118.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 106-118
    • Marty-Mazars, D.1    Clémencet, M.-C.2    Dozolme, P.3    Marty, F.4
  • 47
    • 0028981718 scopus 로고
    • Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells
    • Matsuoka, K., Bassham, D. C., Raikhel, N. V. and Kakamura, K. (1995). Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells. J. Cell Biol. 130, 1307-1318.
    • (1995) J. Cell Biol. , vol.130 , pp. 1307-1318
    • Matsuoka, K.1    Bassham, D.C.2    Raikhel, N.V.3    Kakamura, K.4
  • 48
    • 0026078287 scopus 로고
    • Spatial orgniaztion of the assembly pathways of glycoproteins and complex polysaccharides in the Golgi apparatus of plants
    • Moore, P. J., Swords, K. M. M., Lynch, M. A. and Staehelin, L. A. (1991). Spatial orgniaztion of the assembly pathways of glycoproteins and complex polysaccharides in the Golgi apparatus of plants. J. Cell Biol. 112, 589-602.
    • (1991) J. Cell Biol. , vol.112 , pp. 589-602
    • Moore, P.J.1    Swords, K.M.M.2    Lynch, M.A.3    Staehelin, L.A.4
  • 49
    • 0001064980 scopus 로고    scopus 로고
    • Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds
    • Müntz, K. (1996). Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds. J. Exp. Bot. 47, 605-622.
    • (1996) J. Exp. Bot. , vol.47 , pp. 605-622
    • Müntz, K.1
  • 50
    • 0030019101 scopus 로고    scopus 로고
    • Protein targeting to the plant vacuole
    • Neuhaus, J.-M. (1996). Protein targeting to the plant vacuole. Plant Physiol. Biochem. 34, 217-221.
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 217-221
    • Neuhaus, J.-M.1
  • 51
    • 0001009574 scopus 로고    scopus 로고
    • Compartmentation of proteins in the endomembrane system of plant cells
    • Okita, T. W. and Rogers, J. C. (1996). Compartmentation of proteins in the endomembrane system of plant cells. Annu. Rev. Plant Physiol. Plant Mol. Biol. 47, 327-350.
    • (1996) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.47 , pp. 327-350
    • Okita, T.W.1    Rogers, J.C.2
  • 52
    • 0030060549 scopus 로고    scopus 로고
    • The role of receptors in targeting soluble proteins from the secretory pathway to the vacuole
    • Paris, N. and Rogers, J. (1996). The role of receptors in targeting soluble proteins from the secretory pathway to the vacuole. Plant Physiol. Biochem. 34, 223-228.
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 223-228
    • Paris, N.1    Rogers, J.2
  • 53
    • 0030014157 scopus 로고    scopus 로고
    • Plant cells contain two functionally distinct vacuolar compartments
    • Paris, N., Stanley, C. M., Jones, R. L. and Rogers, J. C. (1996). Plant cells contain two functionally distinct vacuolar compartments. Cell 85, 563-572.
    • (1996) Cell , vol.85 , pp. 563-572
    • Paris, N.1    Stanley, C.M.2    Jones, R.L.3    Rogers, J.C.4
  • 54
    • 0029294115 scopus 로고
    • Plasma membrane intrinsic proteins of Beta vulgaris L
    • Qi, X., Tai, C.-Y. and Wasserman, B. P. (1995). Plasma membrane intrinsic proteins of Beta vulgaris L. Plant Physiol. 108, 387-392.
    • (1995) Plant Physiol. , vol.108 , pp. 387-392
    • Qi, X.1    Tai, C.-Y.2    Wasserman, B.P.3
  • 55
    • 0009282840 scopus 로고
    • Convergence of the endocytic and lysosomal pathways in soybean protoplasts
    • Record, R. D. and Griffing, L. R. (1988). Convergence of the endocytic and lysosomal pathways in soybean protoplasts. Planta 176, 425-432.
    • (1988) Planta , vol.176 , pp. 425-432
    • Record, R.D.1    Griffing, L.R.2
  • 56
    • 84968620640 scopus 로고
    • Membrane flow via the Golgi apparatus of higher plant cells
    • Robinson, D. G. and Kristen, U. (1982). Membrane flow via the Golgi apparatus of higher plant cells. Int. Rev. Cytol. 77, 89-127.
    • (1982) Int. Rev. Cytol. , vol.77 , pp. 89-127
    • Robinson, D.G.1    Kristen, U.2
  • 57
    • 1842361211 scopus 로고
    • Legumin antibodies recognize polypeptides in coated vesicles from developing pea cotyledons
    • Robinson, D. G., Balusek, K. and Freundt, H. (1989). Legumin antibodies recognize polypeptides in coated vesicles from developing pea cotyledons. Protoplasma 150, 79-82.
    • (1989) Protoplasma , vol.150 , pp. 79-82
    • Robinson, D.G.1    Balusek, K.2    Freundt, H.3
  • 58
    • 0008959963 scopus 로고
    • Coated pits
    • ed. C. Larsson and I. M. Møller, Springer Verlag
    • Robinson, D. G. and Hillmer, S. (1990). Coated pits. In The Plant Plasma Membrane (ed. C. Larsson and I. M. Møller), pp. 233-255. Springer Verlag.
    • (1990) The Plant Plasma Membrane , pp. 233-255
    • Robinson, D.G.1    Hillmer, S.2
  • 59
    • 0000367861 scopus 로고
    • One vacuole or two vacuoles: Do protein storage vacuoles arise de novo during pea cotyledon development?
    • Robinson, D. G., Hoh, B., Hinz, G. and Jeong, B.-K. (1995). One vacuole or two vacuoles: do protein storage vacuoles arise de novo during pea cotyledon development? J. Plant Physiol. 145, 654-664.
    • (1995) J. Plant Physiol. , vol.145 , pp. 654-664
    • Robinson, D.G.1    Hoh, B.2    Hinz, G.3    Jeong, B.-K.4
  • 60
    • 0028026793 scopus 로고
    • The role of clathrin, adaptors and dynamin in endocytosis
    • Robinson, M. S. (1994). The role of clathrin, adaptors and dynamin in endocytosis. Curr. Opin. Cell Biol. 6, 538-544.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 538-544
    • Robinson, M.S.1
  • 61
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. (1994). Mechanisms of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 62
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R. and Orci, L. (1996). Coat proteins and vesicle budding. Science 271, 1526-1533.
    • (1996) Science , vol.271 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 63
    • 0028823381 scopus 로고
    • Coated vesicles: A diversity of form and function
    • Schmid, S. L. and Damke, H. (1995). Coated vesicles: a diversity of form and function. FASEB J. 9, 1445-1453.
    • (1995) FASEB J. , vol.9 , pp. 1445-1453
    • Schmid, S.L.1    Damke, H.2
  • 64
    • 0001455921 scopus 로고
    • Subcellular localization of glycosidases and glycosyl-transferases involved in the processing of N-linked oligosaccharides
    • Sturm, A., Johnson, K. D., Szumilo, T., Elbein, A. D. and Chrispeels, M. J. (1987). Subcellular localization of glycosidases and glycosyl-transferases involved in the processing of N-linked oligosaccharides. Plant Physiol. 85, 741-745.
    • (1987) Plant Physiol. , vol.85 , pp. 741-745
    • Sturm, A.1    Johnson, K.D.2    Szumilo, T.3    Elbein, A.D.4    Chrispeels, M.J.5
  • 66
    • 0021433360 scopus 로고
    • Dictyosomes participate in the intracellular pathway of storage proteins in developing Vicia faba cotyledons
    • zur Nieden, U., Manteuffel, R., Weber, E. and Neumann, D. (1984). Dictyosomes participate in the intracellular pathway of storage proteins in developing Vicia faba cotyledons. Eur. J. Cell Biol. 34, 9-17.
    • (1984) Eur. J. Cell Biol. , vol.34 , pp. 9-17
    • Zur Nieden, U.1    Manteuffel, R.2    Weber, E.3    Neumann, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.