메뉴 건너뛰기




Volumn 197, Issue 1-2, 1997, Pages 1-25

Vacuole biogenesis and protein transport to the plant vacuole: A comparison with the yeast vacuole and the mammalian lysosome: Review article

Author keywords

Clathrin coated vesicles; Endosome; Golgi apparatus; Protein trafficking; Vacuole

Indexed keywords

ANIMALIA; MAMMALIA;

EID: 0030980068     PISSN: 0033183X     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF01279880     Document Type: Review
Times cited : (55)

References (244)
  • 1
    • 0000812569 scopus 로고
    • Origin and development of protein bodies in cotyledons of Vicia faba
    • Adler K, Müntz K (1983) Origin and development of protein bodies in cotyledons of Vicia faba. Planta 157: 401-410
    • (1983) Planta , vol.157 , pp. 401-410
    • Adler, K.1    Müntz, K.2
  • 2
    • 0141603396 scopus 로고
    • Zur Entwicklung der Vakuole in Testa-Zellen des Leinsamens
    • Amelunxen F, Heinze U (1984) Zur Entwicklung der Vakuole in Testa-Zellen des Leinsamens. Eur J Cell Biol 35: 343-354
    • (1984) Eur J Cell Biol , vol.35 , pp. 343-354
    • Amelunxen, F.1    Heinze, U.2
  • 3
    • 0030003893 scopus 로고    scopus 로고
    • Ultrastructural and biochemical characterization of autophagy in higher plant cells subjected to carbon deprivation: Control by the supply of mitochondria with respiratory substrates
    • Aubert S, Gout E, Bligny R, Marty-Mazars D, Barrieu F, Alabouvette J, Marty F, Douce R (1996) Ultrastructural and biochemical characterization of autophagy in higher plant cells subjected to carbon deprivation: control by the supply of mitochondria with respiratory substrates. J Cell Biol 133: 1251-1263
    • (1996) J Cell Biol , vol.133 , pp. 1251-1263
    • Aubert, S.1    Gout, E.2    Bligny, R.3    Marty-Mazars, D.4    Barrieu, F.5    Alabouvette, J.6    Marty, F.7    Douce, R.8
  • 4
    • 0000677403 scopus 로고    scopus 로고
    • Physiology of ion transport across the tonoplast of higher plants
    • Barkla BJ, Pantoja O (1996) Physiology of ion transport across the tonoplast of higher plants. Annu Rev Plant Physiol Plant Mol Biol 47: 159-184
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 159-184
    • Barkla, B.J.1    Pantoja, O.2
  • 5
    • 0029119236 scopus 로고
    • An Arabidopsis syntaxin homologue isolated by functional complementation of a yeast pep 12 mutant
    • Bassham DC, Gal S, da Silva Conceicao A, Raikhel NV (1995) An Arabidopsis syntaxin homologue isolated by functional complementation of a yeast pep 12 mutant. Proc Natl Acad Sci USA 92: 7262-7266
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7262-7266
    • Bassham, D.C.1    Gal, S.2    Da Silva Conceicao, A.3    Raikhel, N.V.4
  • 6
    • 0028814446 scopus 로고
    • Intra-Golgi transport mediated by vesicles?
    • Becker B, Melkonian M (1995) Intra-Golgi transport mediated by vesicles? Bot Acta 108: 172-173
    • (1995) Bot Acta , vol.108 , pp. 172-173
    • Becker, B.1    Melkonian, M.2
  • 7
    • 0028370601 scopus 로고
    • A small GTP-binding protein from Arabidopsis thaliana functionally complements the yeast YPT6 null mutant
    • Bednarek SY, Reynold TL, Schroeder M, Grabowski L, Gallwitz D, Raikhel NV (1994) A small GTP-binding protein from Arabidopsis thaliana functionally complements the yeast YPT6 null mutant. Plant Physiol 104: 591-596
    • (1994) Plant Physiol , vol.104 , pp. 591-596
    • Bednarek, S.Y.1    Reynold, T.L.2    Schroeder, M.3    Grabowski, L.4    Gallwitz, D.5    Raikhel, N.V.6
  • 8
    • 0025574861 scopus 로고
    • A carboxylterminal propeptide is necessary for proper sorting of barley lectin to vacuoles of tobacco
    • _ Wilkins TA, Dombrowski JE, Raikhel NV (1990) A carboxylterminal propeptide is necessary for proper sorting of barley lectin to vacuoles of tobacco. Plant Cell 2: 1145-1155
    • (1990) Plant Cell , vol.2 , pp. 1145-1155
    • Wilkins, T.A.1    Dombrowski, J.E.2    Raikhel, N.V.3
  • 9
    • 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
  • 10
    • 0024260020 scopus 로고
    • The two mannose 6-phosphatase receptors have almost identical subcellular distributions in U937 monocytes
    • Bleekemolen JE, Stein M, Figura K von, Slot JW, Geuze HJ (1988) The two mannose 6-phosphatase receptors have almost identical subcellular distributions in U937 monocytes. Eur J Cell Biol 47: 366-372
    • (1988) Eur J Cell Biol , vol.47 , pp. 366-372
    • Bleekemolen, J.E.1    Stein, M.2    Von Figura, K.3    Slot, J.W.4    Geuze, H.J.5
  • 11
    • 0000199795 scopus 로고
    • Dynamics of vacuolar compartmentation
    • Boiler T, Wiemken A (1987) Dynamics of vacuolar compartmentation. Annu Rev Plant Physiol 37: 137-164
    • (1987) Annu Rev Plant Physiol , vol.37 , pp. 137-164
    • Boiler, T.1    Wiemken, A.2
  • 13
    • 0028814328 scopus 로고
    • Regulation of protein degradation
    • Callis J (1995) Regulation of protein degradation. Plant Cell 7: 845-857
    • (1995) Plant Cell , vol.7 , pp. 845-857
    • Callis, J.1
  • 14
    • 0021100238 scopus 로고
    • Coated vesicles from rat liver and calf brain contain lysosomal enzymes bound to mannose 6-phosphate receptors
    • Campbell CH, Rome LH (1983) Coated vesicles from rat liver and calf brain contain lysosomal enzymes bound to mannose 6-phosphate receptors. J Biol Chem 258: 13347-13352
    • (1983) J Biol Chem , vol.258 , pp. 13347-13352
    • Campbell, C.H.1    Rome, L.H.2
  • 15
    • 0026478889 scopus 로고
    • Lysosomal enzyme phosphorylation. II. Protein recognition determinants in either lobe of procathepsin D are sufficient for phosphorylation of both the amino and carboxyl lobe oligosaccharides
    • Cantor AB, Baranski TJ, Kornfeld S (1992) Lysosomal enzyme phosphorylation. II. Protein recognition determinants in either lobe of procathepsin D are sufficient for phosphorylation of both the amino and carboxyl lobe oligosaccharides. J Biol Chem 267: 23349-23356
    • (1992) J Biol Chem , vol.267 , pp. 23349-23356
    • Cantor, A.B.1    Baranski, T.J.2    Kornfeld, S.3
  • 16
    • 0018436334 scopus 로고
    • Immunoaffinity chromatography as a means of purifying legumin from Pisum (pea) seeds
    • Casey RD (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
  • 17
    • 0025084076 scopus 로고
    • Mannose 6-phosphate receptor dependent secretion of lysosomal enzymes
    • Chao H-J, Waheed A, Pohlmann R, Hille A, Figura K von (1990) Mannose 6-phosphate receptor dependent secretion of lysosomal enzymes. EMBO J 9: 3507-3513
    • (1990) EMBO J , vol.9 , pp. 3507-3513
    • Chao, H.-J.1    Waheed, A.2    Pohlmann, R.3    Hille, A.4    Von Figura, K.5
  • 18
    • 0027961075 scopus 로고
    • The functioning of the yeast Golgi apparatus requires an ER protein encoded by ANPI, a member of a new family of genes affecting the secretory pathway
    • Chapman R, Munro S (1994) The functioning of the yeast Golgi apparatus requires an ER protein encoded by ANPI, a member of a new family of genes affecting the secretory pathway. EMBO J 13: 4896-4907
    • (1994) EMBO J , vol.13 , pp. 4896-4907
    • Chapman, R.1    Munro, S.2
  • 19
    • 0029816236 scopus 로고    scopus 로고
    • The VPS8 gene is required for localization and trafficking of the CPY sorting reception in Saccharomyces cerevisiae
    • Chen Y-J, Stevens TH (1996) The VPS8 gene is required for localization and trafficking of the CPY sorting reception in Saccharomyces cerevisiae: Eur J Cell Biol 70: 289-297
    • (1996) Eur J Cell Biol , vol.70 , pp. 289-297
    • Chen, Y.-J.1    Stevens, T.H.2
  • 20
    • 0027371136 scopus 로고
    • Roles of plant homologs of Rab1p and Rab7p in the biogenesis of the peribacteroid membrane, a subcellular compartment formed de novo during root nodule symbiosis
    • Cheon C-I, Lee N-G, Siddique A-BM, Bal AK, Verma DPS (1993) Roles of plant homologs of Rab1p and Rab7p in the biogenesis of the peribacteroid membrane, a subcellular compartment formed de novo during root nodule symbiosis. EMBO J 12: 4125-4135
    • (1993) EMBO J , vol.12 , pp. 4125-4135
    • Cheon, C.-I.1    Lee, N.-G.2    Siddique, A.-B.M.3    Bal, A.K.4    Verma, D.P.S.5
  • 21
    • 0025804582 scopus 로고
    • Regulated import and degradation of a cytosolic protein in the yeast vacuole
    • Chiang H-L, Schekman R (1991) Regulated import and degradation of a cytosolic protein in the yeast vacuole. Nature 350: 313-318
    • (1991) Nature , vol.350 , pp. 313-318
    • Chiang, H.-L.1    Schekman, R.2
  • 22
    • 0000018342 scopus 로고
    • The Golgi apparatus mediates the transport of phytohemagglutinin to the protein bodies in bean cotyledons
    • Chrispeels MJ (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
  • 23
    • 0003024778 scopus 로고
    • The role of the Golgi apparatus in the transport and posttranslational modifications of vacuolar (protein body) proteins
    • _ (1985) The role of the Golgi apparatus in the transport and posttranslational modifications of vacuolar (protein body) proteins. Oxford Surv Plant Mol Cell Biol 2: 43-68
    • (1985) Oxford Surv Plant Mol Cell Biol , vol.2 , pp. 43-68
  • 24
    • 0002284514 scopus 로고
    • Sorting of proteins in the secretory system
    • _ (1991) Sorting of proteins in the secretory system. Annu Rev Plant Physiol Plant Mol Biol 42: 21-53
    • (1991) Annu Rev Plant Physiol Plant Mol Biol , vol.42 , pp. 21-53
  • 25
    • 0025718126 scopus 로고
    • Lectins, lectin genes, and their role in plant defense
    • Raikhel N (1991) Lectins, lectin genes, and their role in plant defense. Plant Cell 3: 1-9
    • (1991) Plant Cell , vol.3 , pp. 1-9
    • Raikhel, N.1
  • 26
    • 0020061795 scopus 로고
    • Role of the endoplasmic reticulum in the synthesis of reserve proteins and the kinetics of their transport to protein bodies in developing pea cotyledons
    • _ Higgins TJV, Craig S, Spencer D (1982) Role of the endoplasmic reticulum in the synthesis of reserve proteins and the kinetics of their transport to protein bodies in developing pea cotyledons. J Cell Biol 93: 5-14
    • (1982) J Cell Biol , vol.93 , pp. 5-14
    • Higgins, T.J.V.1    Craig, S.2    Spencer, D.3
  • 27
    • 0020461640 scopus 로고
    • Asparagine-linked carbohydrate does not determine the cellular location of yeast vacuolar nonspecific alkaline phosphatase
    • Clark DW, Tkacz JS, Lampen JO (1982) Asparagine-linked carbohydrate does not determine the cellular location of yeast vacuolar nonspecific alkaline phosphatase. J Bacteriol 152: 865-873
    • (1982) J Bacteriol , vol.152 , pp. 865-873
    • Clark, D.W.1    Tkacz, J.S.2    Lampen, J.O.3
  • 28
    • 0029905298 scopus 로고    scopus 로고
    • VPS10p cycles between the late Golgi and prevacuolar compartments in its function as the sort-ing receptor for multiple yeast vacuolar hydrolases
    • Cooper AA, Stevens TH (1996) VPS10p cycles between the late Golgi and prevacuolar compartments in its function as the sort-ing receptor for multiple yeast vacuolar hydrolases. J Cell Biol 133: 529-541
    • (1996) J Cell Biol , vol.133 , pp. 529-541
    • Cooper, A.A.1    Stevens, T.H.2
  • 29
    • 0023771534 scopus 로고
    • A highly phosphorylated subpopulation of insulin-like growth factor II/mannose-6-phosphate receptors is in a clathrin-enriched plasma membrane fraction
    • Corvera S, Folander K, Clairmont KB, Czech MP (1988) A highly phosphorylated subpopulation of insulin-like growth factor II/mannose-6-phosphate receptors is in a clathrin-enriched plasma membrane fraction. Proc Natl Acad Sci USA 85: 7567-7571
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7567-7571
    • Corvera, S.1    Folander, K.2    Clairmont, K.B.3    Czech, M.P.4
  • 30
    • 0029889808 scopus 로고    scopus 로고
    • Endocytosis in Cucurbita pepo root meristems: Coated vesicles, multivesicular bodies and vacuole relationship
    • Coulomb S, Coulomb S (1996) Endocytosis in Cucurbita pepo root meristems: coated vesicles, multivesicular bodies and vacuole relationship. C R Acad Sci Paris III 319: 377-383
    • (1996) C R Acad Sci Paris III , vol.319 , pp. 377-383
    • Coulomb, S.1    Coulomb, S.2
  • 31
    • 0002649127 scopus 로고
    • Periodate-acid treatment of sections permits on-grids immunogold localization of pea seed vicilin in ER and Golgi
    • Craig S, Goodchild DJ (1984) Periodate-acid treatment of sections permits on-grids 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
  • 32
    • 0002245187 scopus 로고
    • Structural aspects of protein accumulation in developing pea cotyledons. I. Qualitative and quantitative changes in parenchyma cell vacuoles
    • _ _ Hardham AR (1979) Structural aspects of protein accumulation in developing pea cotyledons. I. Qualitative and quantitative changes in parenchyma cell vacuoles. Aust J Plant Physiol 6: 81-98
    • (1979) Aust J Plant Physiol , vol.6 , pp. 81-98
    • Hardham, A.R.1
  • 33
    • 0013580656 scopus 로고
    • Structural aspects of protein accumulation in developing pea cotyledons. II. Three-dimensional reconstructions of vacuoles and protein bodies from serial sections
    • _ _ Miller C (1980) Structural aspects of protein accumulation in developing pea cotyledons. II. Three-dimensional reconstructions of vacuoles and protein bodies from serial sections. Aust J Plant Physiol 7: 329-337
    • (1980) Aust J Plant Physiol , vol.7 , pp. 329-337
    • Miller, C.1
  • 34
    • 0027175829 scopus 로고
    • Trans-acting and cisacting functions required for endocytosis of the yeast pheromone receptors
    • Davis NG, Horecka JL, Sprayve GF (1993) Trans-acting and cisacting functions required for endocytosis of the yeast pheromone receptors. J Cell Biol 122: 53-65
    • (1993) J Cell Biol , vol.122 , pp. 53-65
    • Davis, N.G.1    Horecka, J.L.2    Sprayve, G.F.3
  • 36
    • 0024982237 scopus 로고
    • Protein secretion in plant cells can occur via a default pathway
    • Denecke J, Botterman J, Deblaere R (1990) Protein secretion in plant cells can occur via a default pathway. Plant Cell 2: 51-59
    • (1990) Plant Cell , vol.2 , pp. 51-59
    • Denecke, J.1    Botterman, J.2    Deblaere, R.3
  • 38
    • 8244225454 scopus 로고
    • Ontogeny, structure and breakdown of protein bodies in Linum usitatissimum Linn
    • Dhar U, Vijayaraghavan MR (1979 Ontogeny, structure and breakdown of protein bodies in Linum usitatissimum Linn. Ann Bot 43: 107-111
    • (1979) Ann Bot , vol.43 , pp. 107-111
    • Dhar, U.1    Vijayaraghavan, M.R.2
  • 39
    • 0000031703 scopus 로고
    • Correlation between infection by Rhizobium leguminosarium and lectin on the surface of Pisum sativum L. roots
    • Diaz C, Van Spronsen PC, Bakhuizen R, Logman GJJ, Lugtenberg EJJ, Kyne JW (1986) Correlation between infection by Rhizobium leguminosarium and lectin on the surface of Pisum sativum L. roots. Planta 168: 350-359
    • (1986) Planta , vol.168 , pp. 350-359
    • Diaz, C.1    Van Spronsen, P.C.2    Bakhuizen, R.3    Logman, G.J.J.4    Lugtenberg, E.J.J.5    Kyne, J.W.6
  • 40
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice JF (1990) Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem Sci 15: 305-309
    • (1990) Trends Biochem Sci , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 41
    • 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 AS, Hajibagheri N, Tooze SA (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
  • 42
    • 0027597740 scopus 로고
    • Determination of the functional elements within the vacuolar targeting signal of barley lectin
    • Dombrowski JE, Schroeder MR, Bednarek SY, Raikhel NV (1993) Determination of the functional elements within the vacuolar targeting signal of barley lectin. Plant Cell 5: 587-596
    • (1993) Plant Cell , vol.5 , pp. 587-596
    • Dombrowski, J.E.1    Schroeder, M.R.2    Bednarek, S.Y.3    Raikhel, N.V.4
  • 43
    • 0027989904 scopus 로고
    • Retention of vacuole contents of plant cells during fixation
    • Dong Z, McCully ME, Canny MJ (1994) Retention of vacuole contents of plant cells during fixation. J Microsc 175: 222-228
    • (1994) J Microsc , vol.175 , pp. 222-228
    • Dong, Z.1    McCully, M.E.2    Canny, M.J.3
  • 44
    • 0028881641 scopus 로고
    • A novel mutagenesis strategy identifies distantly spaced amino acid sequences that are required for the phosphorylation of both the oligosaccharides of procathepsin D by N-acetylglucosamine 1-phosphotransferase
    • Dustin ML, Baranski TJ, Sampath D, Kornfeld S (1995) A novel mutagenesis strategy identifies distantly spaced amino acid sequences that are required for the phosphorylation of both the oligosaccharides of procathepsin D by N-acetylglucosamine 1-phosphotransferase. J Biol Chem 270: 170-179
    • (1995) J Biol Chem , vol.270 , pp. 170-179
    • Dustin, M.L.1    Baranski, T.J.2    Sampath, D.3    Kornfeld, S.4
  • 45
    • 0001195242 scopus 로고
    • Structural organization of ultrarapidly frozen barley aleurone cells actively involved in protein secretion
    • Fernandez DE, Staehelin LA (1985) Structural organization of ultrarapidly frozen barley aleurone cells actively involved in protein secretion. Planta 165: 455-468
    • (1985) Planta , vol.165 , pp. 455-468
    • Fernandez, D.E.1    Staehelin, L.A.2
  • 46
    • 0028070987 scopus 로고
    • Vesicle fusion from yeast to man
    • Ferro-Novick S, Jahn R (1994) Vesicle fusion from yeast to man. Nature 370: 191-193
    • (1994) Nature , vol.370 , pp. 191-193
    • Ferro-Novick, S.1    Jahn, R.2
  • 47
    • 0029979181 scopus 로고    scopus 로고
    • Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes
    • Futter CE, Pearse A, Hewlett LJ, Hopkins CR (1996) Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes. J Cell Biol 132: 1011-1023
    • (1996) J Cell Biol , vol.132 , pp. 1011-1023
    • Futter, C.E.1    Pearse, A.2    Hewlett, L.J.3    Hopkins, C.R.4
  • 48
    • 0027640236 scopus 로고
    • Protein sorting in the endomembrane system of plant cells
    • Gal S, Raikhel NV (1993) Protein sorting in the endomembrane system of plant cells. Curr Opin Cell Biol 5: 636-640
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 636-640
    • Gal, S.1    Raikhel, N.V.2
  • 49
    • 0027371488 scopus 로고
    • Ultrastructure of the endocytotic pathway in glutaraldehyde-fixed and high-pressure frozen/freeze-substituted protoplasts of white spruce (Picea glauca)
    • Galway ME, Rennie PJ, Fowke LC (1993) Ultrastructure of the endocytotic pathway in glutaraldehyde-fixed and high-pressure frozen/freeze-substituted protoplasts of white spruce (Picea glauca). J Cell Sci 106: 847-858
    • (1993) J Cell Sci , vol.106 , pp. 847-858
    • Galway, M.E.1    Rennie, P.J.2    Fowke, L.C.3
  • 50
    • 3142638352 scopus 로고
    • Protein bodies and vacuoles as lysosomes. Investigations into the role of mannose-6-phosphate in intracellular transport of glycosidases in pea cotyledons
    • Gaudreault PR, Beevers L (1984) Protein bodies and vacuoles as lysosomes. Investigations into the role of mannose-6-phosphate in intracellular transport of glycosidases in pea cotyledons. Plant Physiol 76: 228-232
    • (1984) Plant Physiol , vol.76 , pp. 228-232
    • Gaudreault, P.R.1    Beevers, L.2
  • 51
    • 0028248853 scopus 로고
    • Two structural domains mediate two sequential events in γ-zein targeting: Protein endoplasmic reticulum retention and protein body formation
    • Geli MI, Torrent M, 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
  • 53
    • 0021040348 scopus 로고
    • The pathway of the asialoglycoprotein-ligand during receptor-mediated endocytosis: A morphological study with colloidal gold/ligands in the human hepatoma cell line Hep G2
    • _ Slot JW, Strous GJ, Lodish HF, Schwartz AL (1983) The pathway of the asialoglycoprotein-ligand during receptor-mediated endocytosis: a morphological study with colloidal gold/ligands in the human hepatoma cell line Hep G2. Eur J Cell Biol 32: 38-44
    • (1983) Eur J Cell Biol , vol.32 , pp. 38-44
    • Slot, J.W.1    Strous, G.J.2    Lodish, H.F.3    Schwartz, A.L.4
  • 54
    • 0022392709 scopus 로고
    • Possible pathways for lysosomal enzyme delivery
    • _ _ Hasilik A, Figura K von (1985) Possible pathways for lysosomal enzyme delivery. J Cell Biol 101: 2253-2262
    • (1985) J Cell Biol , vol.101 , pp. 2253-2262
    • Hasilik, A.1    Von Figura, K.2
  • 55
    • 0024241414 scopus 로고
    • Sorting of mannose 6-phosphate receptors and lysosomal membrane proteins in endocytic vesicles
    • - Stoorvogel W, Strous GJ, Slot JW, Zijderhand-Bleekemolen J, Mellman I (1989) Sorting of mannose 6-phosphate receptors and lysosomal membrane proteins in endocytic vesicles. J Cell Biol 107: 2491-2501
    • (1989) J Cell Biol , vol.107 , pp. 2491-2501
    • Stoorvogel, W.1    Strous, G.J.2    Slot, J.W.3    Zijderhand-Bleekemolen, J.4    Mellman, I.5
  • 57
    • 0001069047 scopus 로고
    • Tonoplast and soluble vacuolar proteins are targeted by different mechanisms
    • Gomez L, Chrispeels MJ (1993) Tonoplast and soluble vacuolar proteins are targeted by different mechanisms. Plant Cell 5: 1113-1124
    • (1993) Plant Cell , vol.5 , pp. 1113-1124
    • Gomez, L.1    Chrispeels, M.J.2
  • 58
    • 0030019126 scopus 로고    scopus 로고
    • Signals and mechanisms involved in intracellular transport of secreted proteins in plants
    • Gomord V, Faye L (1996) Signals and mechanisms involved in intracellular transport of secreted proteins in plants. Plant Physiol Biochem 34: 165-181
    • (1996) Plant Physiol Biochem , vol.34 , pp. 165-181
    • Gomord, V.1    Faye, L.2
  • 59
    • 0028980860 scopus 로고
    • Sorting of yeast a 1,3 mannosyltransferase is mediated by a lumenal domain interaction and a transmembrane signal that can confer clathrin-dependent Golgi localization to a secreted protein
    • Graham TR, Krasnow VA (1995) Sorting of yeast a 1,3 mannosyltransferase is mediated by a lumenal domain interaction and a transmembrane signal that can confer clathrin-dependent Golgi localization to a secreted protein. Mol Biol Cell 6: 809-824
    • (1995) Mol Biol Cell , vol.6 , pp. 809-824
    • Graham, T.R.1    Krasnow, V.A.2
  • 60
    • 0028171094 scopus 로고
    • Clathrin-dependent localization of a 1,3 mannosyltransferase to the Golgi complex of Saccharomyces cerevisiae
    • _ Seeger M, Payne GS, McKay VL, Emr SD (1994) Clathrin-dependent localization of a 1,3 mannosyltransferase to the Golgi complex of Saccharomyces cerevisiae. J Cell Biol 127: 667-678
    • (1994) J Cell Biol , vol.127 , pp. 667-678
    • Seeger, M.1    Payne, G.S.2    McKay, V.L.3    Emr, S.D.4
  • 61
    • 0026100686 scopus 로고
    • Comparisons of Golgi structure and dynamics in plant and animals cells
    • Griffing LR (1991) Comparisons of Golgi structure and dynamics in plant and animals cells. J Electron Microsc Techn 17: 179-199
    • (1991) J Electron Microsc Techn , vol.17 , pp. 179-199
    • Griffing, L.R.1
  • 62
    • 0342866583 scopus 로고
    • Cytochemical localization of peroxidase in soybean suspension cultured cells and protoplasts: Intracellular vacuole differentiation and presence of peroxidase in coated vesicles and multivesicular bodies
    • Fowke LC (1985) Cytochemical localization of peroxidase in soybean suspension cultured cells and protoplasts: intracellular vacuole differentiation and presence of peroxidase in coated vesicles and multivesicular bodies. Protoplasma 128: 22-30
    • (1985) Protoplasma , vol.128 , pp. 22-30
    • Fowke, L.C.1
  • 63
    • 0025817708 scopus 로고
    • The arguments for pre-existing early and late endosomes
    • Griffiths G, Gruenberg J (1991) The arguments for pre-existing early and late endosomes. Trends Cell Biol 1: 5-9
    • (1991) Trends Cell Biol , vol.1 , pp. 5-9
    • Griffiths, G.1    Gruenberg, J.2
  • 64
    • 0028811965 scopus 로고
    • The bulk-flow hypothesis: Not quite the end
    • _ Doms RW, Mayhew T, Lucocq J (1995) The bulk-flow hypothesis: not quite the end. Trends Cell Biol 5: 9-13
    • (1995) Trends Cell Biol , vol.5 , pp. 9-13
    • Doms, R.W.1    Mayhew, T.2    Lucocq, J.3
  • 65
    • 0024449827 scopus 로고
    • Membrane traffic in endocytosis: Insights from cell-free assays
    • Gruenberg J, Howell KE (1989) Membrane traffic in endocytosis: insights from cell-free assays. Annu Rev Cell Biol 5: 453-481
    • (1989) Annu Rev Cell Biol , vol.5 , pp. 453-481
    • Gruenberg, J.1    Howell, K.E.2
  • 66
    • 0028108664 scopus 로고
    • Comparative modelling of barley grain aspartic proteinase: A structural rationale for observed hydrolytic specificity
    • Guruprasad K, Tömäkangas K, Kervinin J, Blundell TL (1994) Comparative modelling of barley grain aspartic proteinase: a structural rationale for observed hydrolytic specificity. FEBS Lett 352: 131-136
    • (1994) FEBS Lett , vol.352 , pp. 131-136
    • Guruprasad, K.1    Tömäkangas, K.2    Kervinin, J.3    Blundell, T.L.4
  • 67
    • 0030015868 scopus 로고    scopus 로고
    • Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF)
    • Haas A, Wickner W (1996) Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF). EMBO J 15: 13
    • (1996) EMBO J , vol.15 , pp. 13
    • Haas, A.1    Wickner, W.2
  • 68
    • 0027692821 scopus 로고
    • Vesicle transport and processing of the precursor to 2S albumin in pumpkin
    • Hara-Nishimura I, Takenchi Y, Inoue K, Nishimura M (1993) Vesicle transport and processing of the precursor to 2S albumin in pumpkin. Plant J 4: 793-800
    • (1993) Plant J , vol.4 , pp. 793-800
    • Hara-Nishimura, I.1    Takenchi, Y.2    Inoue, K.3    Nishimura, M.4
  • 69
    • 0001612653 scopus 로고
    • Vacuolar processing enzyme responsible for maturation of seed proteins
    • _ Shimada T, Hiraiwa N, Nishimura M (1995) Vacuolar processing enzyme responsible for maturation of seed proteins. J Plant Physiol 145: 632-640
    • (1995) J Plant Physiol , vol.145 , pp. 632-640
    • Shimada, T.1    Hiraiwa, N.2    Nishimura, M.3
  • 70
    • 0000651011 scopus 로고
    • Coated vesicles are involved in the transport of storage proteins during seed development in Pisum sativum L
    • Harley SM, 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
  • 71
    • 49549129862 scopus 로고
    • Protein body formation in cotyledons of developing cowpea (Vigna unguiculata) seeds
    • Harris N, Boulter D (1976) Protein body formation in cotyledons of developing cowpea (Vigna unguiculata) seeds. Ann Bot 40: 739-744
    • (1976) Ann Bot , vol.40 , pp. 739-744
    • Harris, N.1    Boulter, D.2
  • 72
    • 38249026010 scopus 로고
    • Correlated in situ hybridisation and immunochemical studies of legumin storage protein deposition in pea (Pisum sativum L.)
    • _ Grindley H, Mulchrone J, Croy JD (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
    • Grindley, H.1    Mulchrone, J.2    Croy, J.D.3
  • 73
    • 0023643158 scopus 로고
    • Processing of a plant vacuolar precursor in vitro
    • Hattori T, Ichihara S, Nakamura K (1987) Processing of a plant vacuolar precursor in vitro. Eur J Biochem 166: 533-538
    • (1987) Eur J Biochem , vol.166 , pp. 533-538
    • Hattori, T.1    Ichihara, S.2    Nakamura, K.3
  • 74
    • 0019770750 scopus 로고
    • The structure of the endoplasmic reticulum revealed by osmium tetroxide-potassium ferricyanide staining
    • Hepler PK (1981) The structure of the endoplasmic reticulum revealed by osmium tetroxide-potassium ferricyanide staining. Eur J Cell Biol 26: 102-110
    • (1981) Eur J Cell Biol , vol.26 , pp. 102-110
    • Hepler, P.K.1
  • 75
    • 0000680069 scopus 로고
    • Multiple origins of intravacuolar protein accumulation of plant cells
    • Herman EM (1994) Multiple origins of intravacuolar protein accumulation of plant cells. Adv Struct Biol 3: 243-283
    • (1994) Adv Struct Biol , vol.3 , pp. 243-283
    • Herman, E.M.1
  • 76
    • 0008164550 scopus 로고
    • Bark and leaf lectins of Sophora japonica are sequestered in protein-storage vacuoles
    • _ Hankins CN, Shannon LM (1988) Bark and leaf lectins of Sophora japonica are sequestered in protein-storage vacuoles. Plant Physiol 86: 1027-1031
    • (1988) Plant Physiol , vol.86 , pp. 1027-1031
    • Hankins, C.N.1    Shannon, L.M.2
  • 77
    • 0028259120 scopus 로고
    • +-ATPases are associated with the endoplasmic reticulum and provacules of root tip cells
    • +-ATPases are associated with the endoplasmic reticulum and provacules of root tip cells. Plant Physiol 106: 1313-1324
    • (1994) Plant Physiol , vol.106 , pp. 1313-1324
    • Li, X.1    Su, R.T.2    Hsu, H.-T.3    Sze, H.4
  • 78
    • 0026086456 scopus 로고
    • A genetic and structural analysis of the yeast Vps15 protein kinase: Evidence for a direct role of VPs15 in vacuolar protein delivery
    • Herman PK, Stack JH, Emr SD (1991) A genetic and structural analysis of the yeast Vps15 protein kinase: evidence for a direct role of VPs15 in vacuolar protein delivery. EMBO J 10: 4049-4060
    • (1991) EMBO J , vol.10 , pp. 4049-4060
    • Herman, P.K.1    Stack, J.H.2    Emr, S.D.3
  • 79
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A, Ciechanover A (1992) The ubiquitin system for protein degradation. Annu Rev Biochem 61: 761-807
    • (1992) Annu Rev Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 80
    • 0028078228 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding a small GTP-binding protein related to mammalian ADP-ribosylation factor from rice
    • Higo H, Kishimoto N, Saito K (1994) Molecular cloning and characterization of a cDNA encoding a small GTP-binding protein related to mammalian ADP-ribosylation factor from rice. Plant Sci 100: 41-49
    • (1994) Plant Sci , vol.100 , pp. 41-49
    • Higo, H.1    Kishimoto, N.2    Saito, K.3
  • 82
    • 0029089823 scopus 로고
    • Mannose 6-phosphate receptors in sorting and transport of lysosomal enzymes
    • Hille-Rehfeld A (1995) Mannose 6-phosphate receptors in sorting and transport of lysosomal enzymes. Biochim Biophys Acta 1241: 177-194
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 177-194
    • Hille-Rehfeld, A.1
  • 83
    • 0021997295 scopus 로고
    • On the development of the vacuole. II. Further evidence for endoplasmic reticulum origin
    • Hilling B, Amelunxen F (1985) On the development of the vacuole. II. Further evidence for endoplasmic reticulum origin. Eur J Cell Biol 38: 195-200
    • (1985) Eur J Cell Biol , vol.38 , pp. 195-200
    • Hilling, B.1    Amelunxen, F.2
  • 84
    • 0013639228 scopus 로고
    • Confirmation of endocytosis in higher plant protoplasts using lectin-gold conjugates
    • Hillmer S, Depta H, Robinson DG (1986) Confirmation of endocytosis in higher plant protoplasts using lectin-gold conjugates. Eur J Cell Biol 42: 142-149
    • (1986) Eur J Cell Biol , vol.42 , pp. 142-149
    • Hillmer, S.1    Depta, H.2    Robinson, D.G.3
  • 85
    • 0025353619 scopus 로고
    • Barley aleurone protoplasts are structurally and functionally similar to the walled cells of aleurone layers
    • _ Bush DS, Robinson DG, Zingen-Sell I, Jones RL (1990) Barley aleurone protoplasts are structurally and functionally similar to the walled cells of aleurone layers. Eur J Cell Biol 52: 169-173
    • (1990) Eur J Cell Biol , vol.52 , pp. 169-173
    • Bush, D.S.1    Robinson, D.G.2    Zingen-Sell, I.3    Jones, R.L.4
  • 86
    • 0344611479 scopus 로고
    • Strategies in the isolation of storage protein receptors
    • Hinz G, Hoh B, Robinson DG (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
  • 87
    • 0029157875 scopus 로고
    • Stratification of storage proteins in the protein storage vacuole of developing cotyledons of Pisum sativum L
    • _ _ Hohl I, Robinson DG (1995) Stratification of storage proteins in the protein storage vacuole of developing cotyledons of Pisum sativum L. J Plant Physiol 145: 437-442
    • (1995) J Plant Physiol , vol.145 , pp. 437-442
    • Hohl, I.1    Robinson, D.G.2
  • 88
    • 0026903856 scopus 로고
    • Protein sorting to the vacuolar membrane
    • Höfte H, Chrispeels MJ (1992) Protein sorting to the vacuolar membrane. Plant Cell 4: 995-1004
    • (1992) Plant Cell , vol.4 , pp. 995-1004
    • Höfte, H.1    Chrispeels, M.J.2
  • 89
    • 0001610227 scopus 로고
    • The protein-body proteins phytohemagglutinin and tonoplast intrinsic protein are targeted to vacuoles in leaves of transgenic tobacco
    • _ Faye L, Dickinson C, Herman EM, Chrispeels MJ (1991) The protein-body proteins phytohemagglutinin and tonoplast intrinsic protein are targeted to vacuoles in leaves of transgenic tobacco. Planta 184: 431-437
    • (1991) Planta , vol.184 , pp. 431-437
    • Faye, L.1    Dickinson, C.2    Herman, E.M.3    Chrispeels, M.J.4
  • 91
    • 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, Robinson DG (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
  • 92
    • 0028893601 scopus 로고
    • Protein storage vacuoles form de novo during pea cotyledon development
    • _ Hinz G, Jeong B-K, Robinson DG (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
    • Hinz, G.1    Jeong, B.-K.2    Robinson, D.G.3
  • 93
    • 0029860460 scopus 로고    scopus 로고
    • Transport of storage proteins to the vacuole is mediated by vesicles without a clathrin coat
    • Hohl I, Robinson DG, Chrispeels MJ, Hinz G (1996) Transport of storage proteins to the vacuole is mediated by vesicles without a clathrin coat. J Cell Sci 19: 2539-2550
    • (1996) J Cell Sci , vol.19 , pp. 2539-2550
    • Hohl, I.1    Robinson, D.G.2    Chrispeels, M.J.3    Hinz, G.4
  • 94
    • 0026828751 scopus 로고
    • Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions
    • Holwerda BC, Padgett HS, Rogers JC (1992) Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions. Plant Cell 4: 307-318
    • (1992) Plant Cell , vol.4 , pp. 307-318
    • Holwerda, B.C.1    Padgett, H.S.2    Rogers, J.C.3
  • 95
    • 0028169625 scopus 로고
    • A phosphatidolinositol 3-kinase is induced during soybean nodule organogenesis and is associated with membrane proliferation
    • Hong A, Verma DPS (1994) A phosphatidolinositol 3-kinase is induced during soybean nodule organogenesis and is associated with membrane proliferation. Proc Natl Acad Sci USA 91: 9617-9621
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9617-9621
    • Hong, A.1    Verma, D.P.S.2
  • 96
    • 0028339264 scopus 로고
    • In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella
    • Hopkins CR, Gibson A, Shipman M, Strickland DK, Trowbridge IS (1994) In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella. J Cell Biol 125: 1265-1274
    • (1994) J Cell Biol , vol.125 , pp. 1265-1274
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Strickland, D.K.4    Trowbridge, I.S.5
  • 97
    • 0001527581 scopus 로고
    • Endocytosis in maize root cap cells. Evidence obtained using heavy metal salt solutions
    • Hübner R, Depta H, Robinson DG (1985) Endocytosis in maize root cap cells. Evidence obtained using heavy metal salt solutions. Protoplasma 129: 214-222
    • (1985) Protoplasma , vol.129 , pp. 214-222
    • Hübner, R.1    Depta, H.2    Robinson, D.G.3
  • 98
    • 0026755982 scopus 로고
    • Characterization of the signal for rapid internalization of the bovine mannose 6-phosphate/insulin-like growth factor-11 receptor
    • Jadot M, Canfield WM, Gregory W, Kornfeld S (1992) Characterization of the signal for rapid internalization of the bovine mannose 6-phosphate/insulin-like growth factor-11 receptor. J Biol Chem 267: 11069-11077
    • (1992) J Biol Chem , vol.267 , pp. 11069-11077
    • Jadot, M.1    Canfield, W.M.2    Gregory, W.3    Kornfeld, S.4
  • 99
    • 0001438180 scopus 로고
    • An abundant, highly conserved tonoplast protein in seeds
    • Johnson KD, Herman EM, Chrispeels MJ (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
  • 100
    • 0025600403 scopus 로고
    • Cation-dependent mannose 6-phosphate receptor contains two internalization signals in its cytoplasmic domain
    • Johnson KF, Chan W, Kornfeld S (1990) Cation-dependent mannose 6-phosphate receptor contains two internalization signals in its cytoplasmic domain. Proc Natl Acad Sci USA 87: 10010-10014
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 10010-10014
    • Johnson, K.F.1    Chan, W.2    Kornfeld, S.3
  • 101
    • 84986927552 scopus 로고
    • Protein secretion in plants
    • Jones RL, Robinson DG (1989) Protein secretion in plants. New Phytol 111: 567-597
    • (1989) New Phytol , vol.111 , pp. 567-597
    • Jones, R.L.1    Robinson, D.G.2
  • 102
    • 0026787085 scopus 로고
    • Subunit composition, biosynthesis, and assembly of the yeast vacuolar protein-locating ATPase
    • Kane PM, Stevens TH (1992) Subunit composition, biosynthesis, and assembly of the yeast vacuolar protein-locating ATPase. J Bioenerg Biomembr. 24: 383-393
    • (1992) J Bioenerg Biomembr. , vol.24 , pp. 383-393
    • Kane, P.M.1    Stevens, T.H.2
  • 103
    • 0029759612 scopus 로고    scopus 로고
    • The mechanics of the grass flower; the extension of the staminal filaments and the locules of maize
    • Keijzer CJ, Reinders MC, Leferink-Ten Klooster HB (1996) The mechanics of the grass flower; the extension of the staminal filaments and the locules of maize: Ann Bot 77: 675-683
    • (1996) Ann Bot , vol.77 , pp. 675-683
    • Keijzer, C.J.1    Reinders, M.C.2    Leferink-Ten Klooster, H.B.3
  • 104
    • 0001150043 scopus 로고
    • Formation of wheat protein bodies: Involvement of the Golgi apparatus in gliadin transport
    • Kim WT, Franceschi VR, Krishnan HB, Okita TW (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
  • 105
    • 0028201318 scopus 로고
    • Purification and initial characterization of a potential plant vacuolar targeting receptor
    • Kirsch T, Paris N, Butler M, Beevers L, Rogers JC (1994) Purification and initial characterization of a potential plant vacuolar targeting receptor. Proc Natl Acad Sci USA 91: 3403-3407
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3403-3407
    • Kirsch, T.1    Paris, N.2    Butler, M.3    Beevers, L.4    Rogers, J.C.5
  • 106
    • 0030162062 scopus 로고    scopus 로고
    • Interaction of a potential vacuolar targeting receptor with amino- and carboxylterminal targeting determinants
    • _ Saalbach G, Raikhel NV, Beevers L (1996) Interaction of a potential vacuolar targeting receptor with amino- and carboxylterminal targeting determinants. Plant Physiol 111: 469-474
    • (1996) Plant Physiol , vol.111 , pp. 469-474
    • Saalbach, G.1    Raikhel, N.V.2    Beevers, L.3
  • 107
    • 0029379616 scopus 로고
    • Targeting and release of phytohemagglutinin from the roots of bean seedlings
    • Kjemtrup S, Borkhsenious O, Raikhel NV, Chrispeels MJ (1995) Targeting and release of phytohemagglutinin from the roots of bean seedlings. Plant Physiol 109: 603-610
    • (1995) Plant Physiol , vol.109 , pp. 603-610
    • Kjemtrup, S.1    Borkhsenious, O.2    Raikhel, N.V.3    Chrispeels, M.J.4
  • 108
    • 0024447838 scopus 로고
    • Membrane protein sorting: Biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase
    • Klionsky DJ, Emr SD (1989) Membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase. EMBO J 8: 2241-2250
    • (1989) EMBO J , vol.8 , pp. 2241-2250
    • Klionsky, D.J.1    Emr, S.D.2
  • 109
    • 0024006019 scopus 로고
    • Intracellular sorting and processing of a yeast vacuolar hydrolase: Proteinase A propeptide contains vacuolar targeting information
    • Banta LM, Emr SD (1988) Intracellular sorting and processing of a yeast vacuolar hydrolase: proteinase A propeptide contains vacuolar targeting information. Mol Cell Biol 8: 2105-2116
    • (1988) Mol Cell Biol , vol.8 , pp. 2105-2116
    • Banta, L.M.1    Emr, S.D.2
  • 112
    • 0008618938 scopus 로고
    • Ultrastructure, origin, and composition of the protein bodies in the ligule of Isoetes lacustris L
    • Kristen U, Biedermann M (1981) Ultrastructure, origin, and composition of the protein bodies in the ligule of Isoetes lacustris L. Ann Bot 48: 655-663
    • (1981) Ann Bot , vol.48 , pp. 655-663
    • Kristen, U.1    Biedermann, M.2
  • 113
    • 0002601119 scopus 로고
    • Development of aleurone and sub-aleurone layers in maize
    • Kyle DJ, Styles ED (1977) Development of aleurone and sub-aleurone layers in maize. Planta 137: 185-193
    • (1977) Planta , vol.137 , pp. 185-193
    • Kyle, D.J.1    Styles, E.D.2
  • 114
    • 0029187289 scopus 로고
    • Subcellular volumes and metabolite concentrations in potato (Solanum tuberosum cv. Desiree) leaves
    • Leidreiter K, Kruse A, Heinecke D, Robinson DG, Heldt H-W (1995) Subcellular volumes and metabolite concentrations in potato (Solanum tuberosum cv. Desiree) leaves. Bot Acta 108: 439-444
    • (1995) Bot Acta , vol.108 , pp. 439-444
    • Leidreiter, K.1    Kruse, A.2    Heinecke, D.3    Robinson, D.G.4    Heldt, H.-W.5
  • 115
    • 0023221575 scopus 로고
    • Lysosomal enzyme precursors in coated vesicles derived from the exocytic and endocytic pathways
    • Lemansky P, Hasilik A, Figura K von, Helmy S, Fishman J (1987) Lysosomal enzyme precursors in coated vesicles derived from the exocytic and endocytic pathways. J Cell Biol 104: 1743-1748
    • (1987) J Cell Biol , vol.104 , pp. 1743-1748
    • Lemansky, P.1    Hasilik, A.2    Von Figura, K.3    Helmy, S.4    Fishman, J.5
  • 116
    • 0023986504 scopus 로고
    • Characterization of yeast clathrin and anticlathrin heavy-chain monoclonal antibodies
    • Lemmon SK, Lemmon VP, Jones EW (1988) Characterization of yeast clathrin and anticlathrin heavy-chain monoclonal antibodies. J Cell Biochem 36: 329-340
    • (1988) J Cell Biochem , vol.36 , pp. 329-340
    • Lemmon, S.K.1    Lemmon, V.P.2    Jones, E.W.3
  • 117
    • 0026478698 scopus 로고
    • Evidence for a novel route of wheat storage proteins to vacuoles
    • Levanony H, Rubin R, Altschuler Y, 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
  • 118
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y encoded by the VPS10 gene
    • Marcusson EG, Horazdorsky BF, Cereghino JL, Garakhuniun E, Emr SD (1994) The sorting receptor for yeast vacuolar carboxypeptidase Y encoded by the VPS10 gene. Cell 77: 579-586
    • (1994) Cell , vol.77 , pp. 579-586
    • Marcusson, E.G.1    Horazdorsky, B.F.2    Cereghino, J.L.3    Garakhuniun, E.4    Emr, S.D.5
  • 119
    • 0023432307 scopus 로고
    • Association of the precursor of cathepsin D with coated membranes. Kinetics and carbohydrate processing
    • Marquardt T, Braulke T, Hasilik A, Figura K von (1987) Association of the precursor of cathepsin D with coated membranes. Kinetics and carbohydrate processing. Eur J Biochem 168: 37-42
    • (1987) Eur J Biochem , vol.168 , pp. 37-42
    • Marquardt, T.1    Braulke, T.2    Hasilik, A.3    Von Figura, K.4
  • 120
    • 0000677401 scopus 로고    scopus 로고
    • The functions and regulation of glutathione S-transferases in plants
    • Marrs KA (1996) The functions and regulation of glutathione S-transferases in plants. Annu Rev Plant Physiol Plant Mol Biol 47: 127-158
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 127-158
    • Marrs, K.A.1
  • 121
    • 0029825193 scopus 로고    scopus 로고
    • A barley (Hordeum vulgar L.) LEA3 protein. HVA1. is abundant in protein storage vacuoles
    • Marttila S, Tenbola T, Mikkonen A (1996) A barley (Hordeum vulgar L.) LEA3 protein. HVA1. is abundant in protein storage vacuoles. Planta 199: 602-611
    • (1996) Planta , vol.199 , pp. 602-611
    • Marttila, S.1    Tenbola, T.2    Mikkonen, A.3
  • 122
    • 8244234121 scopus 로고
    • Mise en évidence d'un appareil provacuolaire et de son role dans l'autophagie cellulaire et l'origine des vacuoles
    • Marty F (1973a) Mise en évidence d'un appareil provacuolaire et de son role dans l'autophagie cellulaire et l'origine des vacuoles. C R Acad Sci Paris D 276: 1549-1552
    • (1973) C R Acad Sci Paris D , vol.276 , pp. 1549-1552
    • Marty, F.1
  • 123
    • 8244249078 scopus 로고
    • Dissemblance des faces golgiennes et activité des dictyosomes dans les cellules en cours de vacuolisation de la racine d'Euphorbia characias L
    • (1973b) Dissemblance des faces golgiennes et activité des dictyosomes dans les cellules en cours de vacuolisation de la racine d'Euphorbia characias L. C R Acad Sci D 277: 1749-1752
    • (1973) C R Acad Sci D , vol.277 , pp. 1749-1752
  • 124
    • 8244257646 scopus 로고
    • Sites reactifs a l'iodure de zinc-tetroxyde d'osmium dans les cellules de la racine d'Euphorbia characias L
    • _ (1973c) Sites reactifs a l'iodure de zinc-tetroxyde d'osmium dans les cellules de la racine d'Euphorbia characias L. C R Acad Sci D 277: 1317-1320
    • (1973) C R Acad Sci D , vol.277 , pp. 1317-1320
  • 125
    • 0017804308 scopus 로고
    • Cytochemical studies on GERL, provacuoles and vacuoles in root meristematic cells of Euphorbia
    • _ (1978) Cytochemical studies on GERL, provacuoles and vacuoles in root meristematic cells of Euphorbia. Proc Natl Acad Sci USA 75: 852-856
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 852-856
  • 126
    • 0018860611 scopus 로고
    • High voltage electron microscopy of membrane interac-tions in wheat
    • _ (1980) High voltage electron microscopy of membrane interac-tions in wheat. J Histochem Cytochem 28: 1129-1132
    • (1980) J Histochem Cytochem , vol.28 , pp. 1129-1132
  • 127
    • 8244220630 scopus 로고
    • Microscopic électronique à haute tension de l'appareil provacuolaire dans les cellules méristématiques des racines de rais (Raphanus sativus L.)
    • _ (1983) Microscopic électronique à haute tension de l'appareil provacuolaire dans les cellules méristématiques des racines de rais (Raphanus sativus L.). Ann Sci Nat Bot 13: 245-260
    • (1983) Ann Sci Nat Bot , vol.13 , pp. 245-260
  • 129
    • 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, Clemencet MC, Dozolme P, 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    Clemencet, M.C.2    Dozolme, P.3    Marty, F.4
  • 130
    • 0002490298 scopus 로고
    • Autophagy, microautophagy, and crinophagy as mechanisms for protein degradation
    • Glaumann H, Ballard FJ (eds) Academic Press, New York
    • Marzella L, Glaumann H (1987) Autophagy, microautophagy, and crinophagy as mechanisms for protein degradation. In: Glaumann H, Ballard FJ (eds) Lysosomes: their role in protein breakdown. Academic Press, New York, pp 319-367
    • (1987) Lysosomes: Their Role in Protein Breakdown , pp. 319-367
    • Marzella, L.1    Glaumann, H.2
  • 131
    • 0003238559 scopus 로고
    • The lytic compartment of plant cells
    • Springer, Wien New York Alfert M et al (eds)
    • Matile P (1975) The lytic compartment of plant cells. Springer, Wien New York [Alfert M et al (eds) Cell biology monographs, vol 1 ]
    • (1975) Cell Biology Monographs , vol.1
    • Matile, P.1
  • 132
    • 0007581180 scopus 로고
    • Transport of a sweet potato storage protein sporamin to the vacuole in yeast cells
    • Matsuoka K, Nakamura K (1992) Transport of a sweet potato storage protein sporamin to the vacuole in yeast cells. Plant Cell Physiol 33: 453-462
    • (1992) Plant Cell Physiol , vol.33 , pp. 453-462
    • Matsuoka, K.1    Nakamura, K.2
  • 133
    • 0028981718 scopus 로고
    • Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells
    • _ Bassham DC, Raikhel NV, Nakamura 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
    • Bassham, D.C.1    Raikhel, N.V.2    Nakamura, K.3
  • 134
    • 0001008022 scopus 로고
    • Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves
    • Mauch F, Staehelin LA (1989) Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves. Plant Cell 1: 447-457
    • (1989) Plant Cell , vol.1 , pp. 447-457
    • Mauch, F.1    Staehelin, L.A.2
  • 135
    • 0030022935 scopus 로고    scopus 로고
    • A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes
    • Mauxion F, Le Borgne R, Munier-Lehmann H, Hoflack B (1996) A casein kinase II phosphorylation site in the cytoplasmic domain of the cation-dependent mannose 6-phosphate receptor determines the high affinity interaction of the AP-1 Golgi assembly proteins with membranes. J Biol Chem 271: 2171-2178
    • (1996) J Biol Chem , vol.271 , pp. 2171-2178
    • Mauxion, F.1    Le Borgne, R.2    Munier-Lehmann, H.3    Hoflack, B.4
  • 136
    • 0000101132 scopus 로고
    • TIP, an integral membrane protein of the protein-storage vacuoles of the soybean cotyledon undergoes developmentally regulated membrane accumulation and removal
    • Melroy DL, Herman EM (1991) TIP, an integral membrane protein of the protein-storage vacuoles of the soybean cotyledon undergoes developmentally regulated membrane accumulation and removal. Planta 184: 113-122
    • (1991) Planta , vol.184 , pp. 113-122
    • Melroy, D.L.1    Herman, E.M.2
  • 137
    • 12044250881 scopus 로고
    • Nucleotide sequence of a cDNA clone encoding β-amylase from Arabidopsis thaliana
    • Monroe JD, Salminen MD, Press J (1991) Nucleotide sequence of a cDNA clone encoding β-amylase from Arabidopsis thaliana. Plant Physiol 97: 1599-1601
    • (1991) Plant Physiol , vol.97 , pp. 1599-1601
    • Monroe, J.D.1    Salminen, M.D.2    Press, J.3
  • 138
    • 0029798980 scopus 로고    scopus 로고
    • Autophagy in tobacco suspensioncultured cells in response to sucrose starvation
    • Moriyasu Y, Ohsumi Y (1996) Autophagy in tobacco suspensioncultured cells in response to sucrose starvation. Plant Physiol 111: 1233-1241
    • (1996) Plant Physiol , vol.111 , pp. 1233-1241
    • Moriyasu, Y.1    Ohsumi, Y.2
  • 139
    • 0001273124 scopus 로고
    • Histochemistry and fine structure of developing wheat aleurone cells
    • Morrison IN, Kuo J, O'Brian TP (1975) Histochemistry and fine structure of developing wheat aleurone cells. Planta 123: 105-116
    • (1975) Planta , vol.123 , pp. 105-116
    • Morrison, I.N.1    Kuo, J.2    O'Brian, T.P.3
  • 140
    • 0000446039 scopus 로고
    • Intracellular protein sorting and the formation of protein reserves in storage tissue cells of plant seeds
    • Müntz K (1989) Intracellular protein sorting and the formation of protein reserves in storage tissue cells of plant seeds. Biochem Physiol Pflanzen 185: 315-335
    • (1989) Biochem Physiol Pflanzen , vol.185 , pp. 315-335
    • Müntz, K.1
  • 141
    • 0001064980 scopus 로고    scopus 로고
    • Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds
    • _ (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
  • 142
    • 0028017706 scopus 로고
    • Lysosomes can fuse with a late endosomal compartment in a cell-free system from rat liver
    • Mullock BM, Perez JH, Kuwana T, Gray SR, Luzio JP (1994) Lysosomes can fuse with a late endosomal compartment in a cell-free system from rat liver. J Cell Biol 126: 1173-1182
    • (1994) J Cell Biol , vol.126 , pp. 1173-1182
    • Mullock, B.M.1    Perez, J.H.2    Kuwana, T.3    Gray, S.R.4    Luzio, J.P.5
  • 143
    • 0025808286 scopus 로고
    • Maturation models for endosome and lysosome biogenesis
    • Murphy RF (1991) Maturation models for endosome and lysosome biogenesis. Trends Cell Biol 1: 77-82
    • (1991) Trends Cell Biol , vol.1 , pp. 77-82
    • Murphy, R.F.1
  • 144
    • 0027255716 scopus 로고
    • +)-ATPase associates with and is phosphorylated by the 50-kDa polypeptide of clathrin assembly protein ATP-2
    • +)-ATPase associates with and is phosphorylated by the 50-kDa polypeptide of clathrin assembly protein ATP-2. J Biol Chem 268: 9184-9186
    • (1993) J Biol Chem , vol.268 , pp. 9184-9186
    • Myers, M.1    Forgac, M.2
  • 145
    • 0001356880 scopus 로고
    • Proteinase-inhibitor synthesis in tomato plants: Evidence for extracellular deposition in roots through the secretory pathway
    • Narváez-Vàesquez J, Franceschi VR, Ryan CA (1993) Proteinase-inhibitor synthesis in tomato plants: evidence for extracellular deposition in roots through the secretory pathway. Planta 189: 257-266
    • (1993) Planta , vol.189 , pp. 257-266
    • Narváez-Vàesquez, J.1    Franceschi, V.R.2    Ryan, C.A.3
  • 146
    • 0026950884 scopus 로고
    • +-ATPase: One of the most fundamental pumps in nature
    • +-ATPase: one of the most fundamental pumps in nature. J Exp Biol 172: 19-27
    • (1992) J Exp Biol , vol.172 , pp. 19-27
    • Nelson, N.1
  • 147
    • 0026950641 scopus 로고
    • Structure and function of V-ATPase in endocytic and secretory organelles
    • _ (1992b) Structure and function of V-ATPase in endocytic and secretory organelles. J Exp Biol 172: 149-153
    • (1992) J Exp Biol , vol.172 , pp. 149-153
  • 148
    • 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
  • 149
    • 0028002143 scopus 로고
    • Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: Low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space
    • Pietrzak M, Boller T (1994) Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space. Plant J 5: 45-54
    • (1994) Plant J , vol.5 , pp. 45-54
    • Pietrzak, M.1    Boller, T.2
  • 150
    • 0028283489 scopus 로고
    • Sorting of membrane proteins in the yeast secretory pathway
    • Nothwehr SF, Stevens TH (1994) Sorting of membrane proteins in the yeast secretory pathway. J Biol Chem 269: 10185-10188
    • (1994) J Biol Chem , vol.269 , pp. 10185-10188
    • Nothwehr, S.F.1    Stevens, T.H.2
  • 151
    • 0027204816 scopus 로고
    • Membrane protein retention in the yeast Golgi apparatus: Dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues
    • Robert CJ, Stevens TH (1993) Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues. J Cell Biol 121: 1197-1209
    • (1993) J Cell Biol , vol.121 , pp. 1197-1209
    • Robert, C.J.1    Stevens, T.H.2
  • 152
    • 0028953080 scopus 로고
    • Golgi and vacuolar membrane proteins reach the vacuole in vpsl mutant yeast cells via the plasma membrane
    • Conibear E, Stevens TH (1995) Golgi and vacuolar membrane proteins reach the vacuole in vpsl mutant yeast cells via the plasma membrane. J Cell Biol 129: 35-46
    • (1995) J Cell Biol , vol.129 , pp. 35-46
    • Conibear, E.1    Stevens, T.H.2
  • 153
    • 0030013324 scopus 로고    scopus 로고
    • The newly identified yeast GRD genes are required for retention of late-Golgi membrane proteins
    • _ Bryant NJ, Stevens TH (1996) The newly identified yeast GRD genes are required for retention of late-Golgi membrane proteins. Mol Cell Biol 16: 2700-2707
    • (1996) Mol Cell Biol , vol.16 , pp. 2700-2707
    • Bryant, N.J.1    Stevens, T.H.2
  • 154
    • 0028239912 scopus 로고
    • GTPases: Multifunctional molecular switches regulating vesicular traffic
    • Nuoffer C, Balch WE (1994) GTPases: multifunctional molecular switches regulating vesicular traffic. Annu Rev Biochem 63: 949-990
    • (1994) Annu Rev Biochem , vol.63 , pp. 949-990
    • Nuoffer, C.1    Balch, W.E.2
  • 155
    • 0028007672 scopus 로고
    • V-type ATPase and pyrophosphatase in endomembranes of maize roots
    • Oberbeck K, Drucker M, Robinson DG (1994) V-type ATPase and pyrophosphatase in endomembranes of maize roots. J Exp Bot 45: 235-244
    • (1994) J Exp Bot , vol.45 , pp. 235-244
    • Oberbeck, K.1    Drucker, M.2    Robinson, D.G.3
  • 157
    • 0001009574 scopus 로고    scopus 로고
    • Compartmentation of proteins in the endomembrane system of plant cells
    • Okita TW, Rogers JC (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
  • 158
    • 0027067882 scopus 로고
    • Alternative pathways for the sorting of soluble vacuolar proteins in yeast: A vps35 null mutant missorts and secrets only a subset of vacuolar hydrolases
    • Paravicini G, Horndovsky BF, Emr SD (1992) Alternative pathways for the sorting of soluble vacuolar proteins in yeast: a vps35 null mutant missorts and secrets only a subset of vacuolar hydrolases. Mol Biol Cell 3: 415-427
    • (1992) Mol Biol Cell , vol.3 , pp. 415-427
    • Paravicini, G.1    Horndovsky, B.F.2    Emr, S.D.3
  • 159
    • 0030060549 scopus 로고    scopus 로고
    • The role of receptors in targeting soluble proteins from the secretory pathway to the vacuole
    • Paris N, Rogers JC (1996) The role of receptors in targeting soluble proteins from the secretory pathway to the vacuole. Plant Physiol Biochem 34: 223-227
    • (1996) Plant Physiol Biochem , vol.34 , pp. 223-227
    • Paris, N.1    Rogers, J.C.2
  • 160
    • 0030014157 scopus 로고    scopus 로고
    • Plant cells contain two functionally distinct vacuolar compartments
    • _ Stanley MC, Jones RL, Rogers JC (1996) Plant cells contain two functionally distinct vacuolar compartments. Cell 85: 563-572
    • (1996) Cell , vol.85 , pp. 563-572
    • Stanley, M.C.1    Jones, R.L.2    Rogers, J.C.3
  • 161
    • 0023517021 scopus 로고
    • Functional morphology of the Golgi apparatus
    • Pavelka M (1987) Functional morphology of the Golgi apparatus. Adv Anat Embryol Cell Biol 106: 1-96
    • (1987) Adv Anat Embryol Cell Biol , vol.106 , pp. 1-96
    • Pavelka, M.1
  • 162
    • 0023440747 scopus 로고
    • Genetic and biochemical characterization of clathrin-deficient Saccharomyces cerevisiae
    • Payne GS, Hasson TB, Hasson MS, Schekman R (1987) Genetic and biochemical characterization of clathrin-deficient Saccharomyces cerevisiae. Mol Cell Biol 7: 3888-3898
    • (1987) Mol Cell Biol , vol.7 , pp. 3888-3898
    • Payne, G.S.1    Hasson, T.B.2    Hasson, M.S.3    Schekman, R.4
  • 163
    • 0022134606 scopus 로고
    • Assembly of the mannose-6-phosphate receptor into reconstituted clathrin coats
    • Pearse BMF (1985) Assembly of the mannose-6-phosphate receptor into reconstituted clathrin coats. EMBO J 4: 2457-2460
    • (1985) EMBO J , vol.4 , pp. 2457-2460
    • Pearse, B.M.F.1
  • 164
    • 0025258892 scopus 로고
    • Clathrin, adaptors, and sorting
    • _ Robinson MS (1990) Clathrin, adaptors, and sorting. Annu Rev Cell Biol 6: 151-171
    • (1990) Annu Rev Cell Biol , vol.6 , pp. 151-171
    • Robinson, M.S.1
  • 165
    • 0030038133 scopus 로고    scopus 로고
    • The binding protein (BiP) and the synthesis of secretory proteins
    • Pedrazzini E, Vitale A (1996) The binding protein (BiP) and the synthesis of secretory proteins. Plant Physiol Biochem 34: 207-216
    • (1996) Plant Physiol Biochem , vol.34 , pp. 207-216
    • Pedrazzini, E.1    Vitale, A.2
  • 166
    • 0008016034 scopus 로고
    • Protein bodies of seeds: Ultrastructure, biochemistry, biosynthesis and degradation
    • Pernollet JC (1978) Protein bodies of seeds: ultrastructure, biochemistry, biosynthesis and degradation. Phytochem 17: 1473-1480
    • (1978) Phytochem , vol.17 , pp. 1473-1480
    • Pernollet, J.C.1
  • 167
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi
    • Pfeffer SR, Rothman JE (1987) Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu Rev Biochem 56: 829-852
    • (1987) Annu Rev Biochem , vol.56 , pp. 829-852
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 168
    • 0028904692 scopus 로고
    • Saccharomyces cerevisiae AP12p, a homologue of the mammalian AP β subunit, plays a role in clathrin-dependent Golgi functions
    • Rad MR, Phan HL, Kirchrath L, Tan PK, Kirchhausen T, Hollenberg CP, Payne GS (1995) Saccharomyces cerevisiae AP12p, a homologue of the mammalian AP β subunit, plays a role in clathrin-dependent Golgi functions. J Cell Sci 108: 1605-1615
    • (1995) J Cell Sci , vol.108 , pp. 1605-1615
    • Rad, M.R.1    Phan, H.L.2    Kirchrath, L.3    Tan, P.K.4    Kirchhausen, T.5    Hollenberg, C.P.6    Payne, G.S.7
  • 169
    • 0027083496 scopus 로고
    • Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class E vps mutants
    • Raymond CK, Howard-Stevendon I, Vater CA, Stevens TH (1992) Morphological classification of the yeast vacuolar protein sorting mutants: evidence for a prevacuolar compartment in class E vps mutants. Mol Biol Cell 3: 1389-1402
    • (1992) Mol Biol Cell , vol.3 , pp. 1389-1402
    • Raymond, C.K.1    Howard-Stevendon, I.2    Vater, C.A.3    Stevens, T.H.4
  • 171
    • 0009282840 scopus 로고
    • Convergence of the endocytic and lysosomal pathways in soybean protoplasts
    • Record RD. Griffing LR (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
  • 172
    • 0027389461 scopus 로고
    • cDNA cloning and expression of an Arabidopsis GTP-binding protein of the ARF family
    • Regad F, Bardet C, Tremousaygue D, Moisan A, Lescure B, Axelos M (1993) cDNA cloning and expression of an Arabidopsis GTP-binding protein of the ARF family. FEBS Lett 316: 133-136
    • (1993) FEBS Lett , vol.316 , pp. 133-136
    • Regad, F.1    Bardet, C.2    Tremousaygue, D.3    Moisan, A.4    Lescure, B.5    Axelos, M.6
  • 173
    • 8244265050 scopus 로고    scopus 로고
    • Targeting and trafficking of vacuolar proteins
    • Smallwood M, Knox JP, Bowles DJ (eds) Bios Scientific Publishers, Oxford
    • Reynolds TL, Raikhel NV (1996) Targeting and trafficking of vacuolar proteins. In: Smallwood M, Knox JP, Bowles DJ (eds) Membranes: specialized functions in plants. Bios Scientific Publishers, Oxford, pp 403-420
    • (1996) Membranes: Specialized Functions in Plants , pp. 403-420
    • Reynolds, T.L.1    Raikhel, N.V.2
  • 174
    • 0024653797 scopus 로고
    • Structure, biosynthesis, and localization of dipeptidyl aminopeptidase B, an integral membrane glycoprotein of the yeast vacuole
    • Roberts CJ, Pohling G, Rothman JH, Stevens TH (1989) Structure, biosynthesis, and localization of dipeptidyl aminopeptidase B, an integral membrane glycoprotein of the yeast vacuole. J Cell Biol 108: 1363-1373
    • (1989) J Cell Biol , vol.108 , pp. 1363-1373
    • Roberts, C.J.1    Pohling, G.2    Rothman, J.H.3    Stevens, T.H.4
  • 175
    • 0026727566 scopus 로고
    • Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment
    • _ Nothwehr SF, Stevens TH (1992) Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment. J Cell Biol 119: 69-83
    • (1992) J Cell Biol , vol.119 , pp. 69-83
    • Nothwehr, S.F.1    Stevens, T.H.2
  • 177
    • 0004896359 scopus 로고    scopus 로고
    • Pyrophosphatase is not (only) a vacuolar marker
    • _ (1996a) Pyrophosphatase is not (only) a vacuolar marker. Trends Plant Sci 1: 330
    • (1996) Trends Plant Sci , vol.1 , pp. 330
  • 178
    • 0030265227 scopus 로고    scopus 로고
    • Clathrin-mediated trafficking
    • _ (1996b) Clathrin-mediated trafficking. Trends Plant Sci 1: 349-355
    • (1996) Trends Plant Sci , vol.1 , pp. 349-355
  • 179
    • 0008959963 scopus 로고
    • Coated pits
    • Larsson C, Møller IM (eds) Springer, Berlin Heidelberg New York Tokyo
    • _ Hillmer S (1990) Coated pits. In: Larsson C, Møller IM (eds) The plant plasma membrane. Springer, Berlin Heidelberg New York Tokyo, pp 233-255
    • (1990) The Plant Plasma Membrane , pp. 233-255
    • Hillmer, S.1
  • 180
    • 0030019552 scopus 로고    scopus 로고
    • Multiple mechanisms of protein body formation in pea cotyledons
    • Hinz G (1996) Multiple mechanisms of protein body formation in pea cotyledons. Plant Physiol Biochem 34: 155-163
    • (1996) Plant Physiol Biochem , vol.34 , pp. 155-163
    • Hinz, G.1
  • 181
    • 1842361211 scopus 로고
    • Legumin antibodies recognize polypeptides in coated vesicles from developing pea cotyledons
    • _ Balusek K, 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
    • Balusek, K.1    Freundt, H.2
  • 182
    • 0000367861 scopus 로고
    • One vacuole or two vacuoles: Do protein storage vacuoles arise de novo during pea cotyledon development?
    • Hob B, Hinz G, 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
    • Hob, B.1    Hinz, G.2    Jeong, B.-K.3
  • 183
    • 0030020125 scopus 로고    scopus 로고
    • Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons
    • _ Haschke H-P, Hinz G, Hoh B, Maeshima M, Marty F (1996) Immunological detection of tonoplast polypeptides in the plasma membrane of pea cotyledons. Planta 198: 95-103
    • (1996) Planta , vol.198 , pp. 95-103
    • Haschke, H.-P.1    Hinz, G.2    Hoh, B.3    Maeshima, M.4    Marty, F.5
  • 184
    • 0011742571 scopus 로고
    • Aleurain: A barley thiol protease closely related to mammalian cathepsin H
    • Rogers JC, Dean D, Heck GR (1985) Aleurain: a barley thiol protease closely related to mammalian cathepsin H. Proc Natl Acad Sci USA 82: 6512-6516
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 6512-6516
    • Rogers, J.C.1    Dean, D.2    Heck, G.R.3
  • 185
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE (1994) Mechanisms of intracellular protein transport. Nature 372: 55-63
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 186
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • _ Warren G (1994) Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr Biol 4: 220-233
    • (1994) Curr Biol , vol.4 , pp. 220-233
    • Warren, G.1
  • 187
    • 0022470653 scopus 로고
    • Overproduction-induced mislocalization of yeast vacuolar protein allows isolation of its structural gene
    • Rothman JH, Hunter CP, Valls LA, Stevens TH (1986) Overproduction-induced mislocalization of yeast vacuolar protein allows isolation of its structural gene. Proc Natl Acad Sci USA 83: 3248-3252
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3248-3252
    • Rothman, J.H.1    Hunter, C.P.2    Valls, L.A.3    Stevens, T.H.4
  • 188
    • 0025376380 scopus 로고
    • A putative GTP-binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting
    • _ Raymond CK, Gilbert T, O'Hara PJ, Stevens TH (1990) A putative GTP-binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting. Cell 61: 1063-1074
    • (1990) Cell , vol.61 , pp. 1063-1074
    • Raymond, C.K.1    Gilbert, T.2    O'Hara, P.J.3    Stevens, T.H.4
  • 189
    • 11944255947 scopus 로고
    • Evidence for the presence of two different protein bodies in wheat endosperm
    • Rubin R, Levanony H, Galili G (1992) Evidence for the presence of two different protein bodies in wheat endosperm. Plant Physiol 99: 718-724
    • (1992) Plant Physiol , vol.99 , pp. 718-724
    • Rubin, R.1    Levanony, H.2    Galili, G.3
  • 190
    • 0026321028 scopus 로고
    • Primary structures of a barley grain aspartic proteinase: A plant aspartic proteinase resembling mammalian cathepsin D
    • Runeberg-Roos P, Törmäkangas K. Östman A (1991) Primary structures of a barley grain aspartic proteinase: a plant aspartic proteinase resembling mammalian cathepsin D. Eur J Biochem 202: 1021-1027
    • (1991) Eur J Biochem , vol.202 , pp. 1021-1027
    • Runeberg-Roos, P.1    Törmäkangas, K.2    Östman, A.3
  • 191
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: Genes for improving defenses against insects and pathogens
    • Ryan CA (1990) Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu Rev Phytopathol 28: 425-449
    • (1990) Annu Rev Phytopathol , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 193
    • 0022262565 scopus 로고
    • Transmembrane orientation of the mannose-6-phosphate receptor in isolated clathrin-coated vesicles
    • Sahagian GG, Steer CJ (1985) Transmembrane orientation of the mannose-6-phosphate receptor in isolated clathrin-coated vesicles. J Biol Chem 260: 9838-9842
    • (1985) J Biol Chem , vol.260 , pp. 9838-9842
    • Sahagian, G.G.1    Steer, C.J.2
  • 194
    • 0025561645 scopus 로고
    • Endocytosis in elongating root cells of Lobelia erinus
    • Samuels AI, Bisalputra T (1990) Endocytosis in elongating root cells of Lobelia erinus. J Cell Sci 97: 157-165
    • (1990) J Cell Sci , vol.97 , pp. 157-165
    • Samuels, A.I.1    Bisalputra, T.2
  • 195
    • 0028236274 scopus 로고
    • Targeting of membrane proteins to endosomes and lysosomes
    • Sandoval IV, Brakke O (1994) Targeting of membrane proteins to endosomes and lysosomes. Trends Cell Biol 4: 292-297
    • (1994) Trends Cell Biol , vol.4 , pp. 292-297
    • Sandoval, I.V.1    Brakke, O.2
  • 196
    • 0000746728 scopus 로고
    • Identification of vacuolar sorting information in phytohemagglutinin, an unprocessed vacuolar protein
    • Schaewen A van, Chrispeels MJ (1993) Identification of vacuolar sorting information in phytohemagglutinin, an unprocessed vacuolar protein. J Exp Bot 44: 339-342
    • (1993) J Exp Bot , vol.44 , pp. 339-342
    • Van Schaewen, A.1    Chrispeels, M.J.2
  • 197
    • 0028823381 scopus 로고
    • Coated vesicles: A diversity of form and function
    • Schmid SL, 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
  • 199
    • 0027905021 scopus 로고
    • Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting
    • Schu PV, Takegawa K, Fry MJ, Stack JH, Waterfield MD, Emr SD (1993) Phosphatidylinositol 3-kinase encoded by yeast VPS34 gene essential for protein sorting. Science 260: 88-91
    • (1993) Science , vol.260 , pp. 88-91
    • Schu, P.V.1    Takegawa, K.2    Fry, M.J.3    Stack, J.H.4    Waterfield, M.D.5    Emr, S.D.6
  • 201
    • 0026652588 scopus 로고
    • A role for clathrin in the sorting of vacuolar proteins in the Golgi complex of yeast
    • Seeger M, Payne GS (1992a) A role for clathrin in the sorting of vacuolar proteins in the Golgi complex of yeast. EMBO J 11: 2811-2818
    • (1992) EMBO J , vol.11 , pp. 2811-2818
    • Seeger, M.1    Payne, G.S.2
  • 202
    • 0026742306 scopus 로고
    • Selective and immediate effects of clathrin heavy chain mutations on
    • _ _ (1992b) Selective and immediate effects of clathrin heavy chain mutations on Golgi membrane protein retention in Saccharomyces cerevisiae. J Cell Biol 118: 531-540
    • (1992) J Cell Biol , vol.118 , pp. 531-540
  • 203
    • 0029328357 scopus 로고
    • Seed storage proteins: Structures and biosynthesis
    • Shewry PR, Napier JA, Tatham AS (1995) Seed storage proteins: structures and biosynthesis. Plant Cell 7: 945-956
    • (1995) Plant Cell , vol.7 , pp. 945-956
    • Shewry, P.R.1    Napier, J.A.2    Tatham, A.S.3
  • 204
    • 0025132351 scopus 로고
    • Yeast clathrin has a distinctive light chain that is important for cell growth
    • Silveira LA, Wong DH, Masiarz FR, Schekman R (1990) Yeast clathrin has a distinctive light chain that is important for cell growth. J Cell Biol 111: 1437-1449
    • (1990) J Cell Biol , vol.111 , pp. 1437-1449
    • Silveira, L.A.1    Wong, D.H.2    Masiarz, F.R.3    Schekman, R.4
  • 205
    • 0001270179 scopus 로고
    • Immunocytochemical localization of palatin, the major glycoprotein in potato (Solanum tuberosum L.) tubers
    • Sonnewald U, Studer D, Rocha-Sosa M, Wilmitzer L (1989) Immunocytochemical localization of palatin, the major glycoprotein in potato (Solanum tuberosum L.) tubers. Planta 178: 176-183
    • (1989) Planta , vol.178 , pp. 176-183
    • Sonnewald, U.1    Studer, D.2    Rocha-Sosa, M.3    Wilmitzer, L.4
  • 206
    • 0025405807 scopus 로고
    • Expression of mutant patatin protein in transgenic tobacco plants: Role of glycans and intracellular location
    • _ Schaewen A von, Willmitzer L (1990) Expression of mutant patatin protein in transgenic tobacco plants: role of glycans and intracellular location. Plant Cell 2: 345-355
    • (1990) Plant Cell , vol.2 , pp. 345-355
    • Von Schaewen, A.1    Willmitzer, L.2
  • 207
    • 0027180886 scopus 로고
    • In vitro binding of plasma membrane-coated vesicle adaptors to the cytoplasmic domain of lysosomal acid phosphatase
    • Sosa MA, Schmidt B, Figura K von, Hille-Rehfeld A (1993) In vitro binding of plasma membrane-coated vesicle adaptors to the cytoplasmic domain of lysosomal acid phosphatase. J Biol Chem 268: 12537-12543
    • (1993) J Biol Chem , vol.268 , pp. 12537-12543
    • Sosa, M.A.1    Schmidt, B.2    Von Figura, K.3    Hille-Rehfeld, A.4
  • 208
    • 0028110018 scopus 로고
    • Vps34p required for yeast vacuolar protein sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI 3-kinase activities
    • Stack JH, Emr SD (1994) Vps34p required for yeast vacuolar protein sorting is a multiple specificity kinase that exhibits both protein kinase and phosphatidylinositol-specific PI 3-kinase activities. J Biol Chem 269: 31552-31562
    • (1994) J Biol Chem , vol.269 , pp. 31552-31562
    • Stack, J.H.1    Emr, S.D.2
  • 209
    • 0029618201 scopus 로고
    • Receptor-mediated protein sorting to the vacuole in yeast: Roles for a protein kinase, a lipid kinase and GTP-binding protein
    • _ Horazdovsky B, Emr SD (1995) Receptor-mediated protein sorting to the vacuole in yeast: roles for a protein kinase, a lipid kinase and GTP-binding protein. Annu Rev Cell Dev Biol 11: 1-33
    • (1995) Annu Rev Cell Dev Biol , vol.11 , pp. 1-33
    • Horazdovsky, B.1    Emr, S.D.2
  • 210
    • 0028855261 scopus 로고
    • The plant Golgi apparatus: Structure, functional organization and trafficking mechanisms
    • Staehelin LA, Moore I (1995) The plant Golgi apparatus: structure, functional organization and trafficking mechanisms. Annu Rev Plant Physiol Mol Biol 46: 261-288
    • (1995) Annu Rev Plant Physiol Mol Biol , vol.46 , pp. 261-288
    • Staehelin, L.A.1    Moore, I.2
  • 211
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes MA, Rothman JE (1993) The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell 73: 999-1005
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 212
    • 0002635994 scopus 로고
    • Novel regulation of vegetative storage protein genes
    • Staswick PE (1990) Novel regulation of vegetative storage protein genes. Plant Cell 2: 1-6
    • (1990) Plant Cell , vol.2 , pp. 1-6
    • Staswick, P.E.1
  • 214
    • 0022493616 scopus 로고
    • Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y
    • Stevens TH, Rothman JH, Payne GS, Schekman R (1986) Gene dosage-dependent secretion of yeast vacuolar carboxypeptidase Y. J Cell Biol 102: 1551-1557
    • (1986) J Cell Biol , vol.102 , pp. 1551-1557
    • Stevens, T.H.1    Rothman, J.H.2    Payne, G.S.3    Schekman, R.4
  • 215
    • 0000864304 scopus 로고
    • Intracellular transport and processing of a tobacco vacuolar β-1,3-glucanase
    • Sticher L, Hinz U, Meyer AD, Meins F Jr (1992) Intracellular transport and processing of a tobacco vacuolar β-1,3-glucanase. Planta 188: 559-565
    • (1992) Planta , vol.188 , pp. 559-565
    • Sticher, L.1    Hinz, U.2    Meyer, A.D.3    Meins Jr., F.4
  • 216
    • 0030047961 scopus 로고    scopus 로고
    • A novel class of clathrin-coated vesicles budding from endosomes
    • Stoorvogel W, Oorschot V, Geuze HJ (1996) A novel class of clathrin-coated vesicles budding from endosomes. J Cell Biol 132:21-33
    • (1996) J Cell Biol , vol.132 , pp. 21-33
    • Stoorvogel, W.1    Oorschot, V.2    Geuze, H.J.3
  • 217
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof TC (1995) The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 375: 645-653
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 218
    • 0025443923 scopus 로고
    • A short domain of the plant vacuolar protein phytohemagglutinin targets invertase to the yeast vacuole
    • Tague BW, Dickingson CD, Chrispeels MJ (1990) A short domain of the plant vacuolar protein phytohemagglutinin targets invertase to the yeast vacuole. Plant Cell 2: 533-546
    • (1990) Plant Cell , vol.2 , pp. 533-546
    • Tague, B.W.1    Dickingson, C.D.2    Chrispeels, M.J.3
  • 219
    • 0008342761 scopus 로고
    • The morphology of multivesicular bodies in soybean protoplasts and their role in endocytosis
    • Tanchak MA, Fowke LC (1987) The morphology of multivesicular bodies in soybean protoplasts and their role in endocytosis. Protoplasma 138: 173-182
    • (1987) Protoplasma , vol.138 , pp. 173-182
    • Tanchak, M.A.1    Fowke, L.C.2
  • 221
    • 0001346114 scopus 로고
    • Ultrastructure of the partially coated reticulum and dictyosomes during endocytosis by soybean protoplasts
    • _ Rennie PJ, Fowke LC (1988) Ultrastructure of the partially coated reticulum and dictyosomes during endocytosis by soybean protoplasts. Planta 175: 433-441
    • (1988) Planta , vol.175 , pp. 433-441
    • Rennie, P.J.1    Fowke, L.C.2
  • 222
    • 0026061507 scopus 로고
    • Tubular early endosomal network in AtT20 and other cells
    • Tooze J, Hollinshead M (1991) Tubular early endosomal network in AtT20 and other cells. J Cell Biol 115: 635-653
    • (1991) J Cell Biol , vol.115 , pp. 635-653
    • Tooze, J.1    Hollinshead, M.2
  • 224
    • 0026215401 scopus 로고
    • The soybean 94-kilodalton vegetative storage protein is a lipoxygenase that is localized in paraveinal mesophyll cell vacuoles
    • Tranberger TJ, Franceschi VR, Hildebrand DF, Grimes HD (1991) The soybean 94-kilodalton vegetative storage protein is a lipoxygenase that is localized in paraveinal mesophyll cell vacuoles. Plant Cell 3: 973-987
    • (1991) Plant Cell , vol.3 , pp. 973-987
    • Tranberger, T.J.1    Franceschi, V.R.2    Hildebrand, D.F.3    Grimes, H.D.4
  • 225
    • 0027333415 scopus 로고
    • Signal-dependent membrane protein targeting in the endocytic pathway
    • Trowbridge IS, Collawn JF, Hopkins CR (1993) Signal-dependent membrane protein targeting in the endocytic pathway. Annu Rev Cell Biol 9: 129-161
    • (1993) Annu Rev Cell Biol , vol.9 , pp. 129-161
    • Trowbridge, I.S.1    Collawn, J.F.2    Hopkins, C.R.3
  • 226
    • 0023652379 scopus 로고
    • Protein sorting in yeast: The localization determinant of yeast vacuolar carboxypeptidase Y in the propeptide
    • Valls LA, Hunter CP, Rothman JH, Stevens TH (1987) Protein sorting in yeast: the localization determinant of yeast vacuolar carboxypeptidase Y in the propeptide. Cell 48: 887-897
    • (1987) Cell , vol.48 , pp. 887-897
    • Valls, L.A.1    Hunter, C.P.2    Rothman, J.H.3    Stevens, T.H.4
  • 227
    • 0025370505 scopus 로고
    • Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids
    • Valls SA, Winther JR, Stevens TH (1990) Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids. J Cell Biol 111: 361-368
    • (1990) J Cell Biol , vol.111 , pp. 361-368
    • Valls, S.A.1    Winther, J.R.2    Stevens, T.H.3
  • 228
    • 0027297956 scopus 로고
    • Yeast vacuolar proenzymes are sorted in the late Golgi complex and transported to the vacuole via a prevacuolar endosome-like compartment
    • Vida TA, Huyer G, Emr SD (1993) Yeast vacuolar proenzymes are sorted in the late Golgi complex and transported to the vacuole via a prevacuolar endosome-like compartment. J Cell Biol 121: 124-1256
    • (1993) J Cell Biol , vol.121 , pp. 124-1256
    • Vida, T.A.1    Huyer, G.2    Emr, S.D.3
  • 229
    • 0008059601 scopus 로고
    • Structural changes in protein bodies of cotton radicles during seed maturation and germination
    • Robards AW (ed) Oxford University Press, Oxford
    • Vigil EL, Steere RL, Christiansen MN, Erbe EF (1985) Structural changes in protein bodies of cotton radicles during seed maturation and germination. In: Robards AW (ed) Botanical microscopy. Oxford University Press, Oxford, pp 311-334
    • (1985) Botanical Microscopy , pp. 311-334
    • Vigil, E.L.1    Steere, R.L.2    Christiansen, M.N.3    Erbe, E.F.4
  • 230
    • 0026823307 scopus 로고
    • Sorting of proteins to the vacuoles of plant cells
    • Vitale A, Chrispeels MJ (1992) Sorting of proteins to the vacuoles of plant cells. Bio Essays 14: 151-160
    • (1992) Bio Essays , vol.14 , pp. 151-160
    • Vitale, A.1    Chrispeels, M.J.2
  • 231
    • 0001143106 scopus 로고
    • The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport
    • Ceriotti A, Denecke J (1993) The role of the endoplasmic reticulum in protein synthesis, modification and intracellular transport. J Exp Bot 44: 1417-1444
    • (1993) J Exp Bot , vol.44 , pp. 1417-1444
    • Ceriotti, A.1    Denecke, J.2
  • 232
    • 0024301301 scopus 로고
    • In vitro mutated phytohemagglutinin genes expressed in tobacco seeds: Role of glycans in protein targeting and stability
    • Voelker TA, Herman EM, Chrispeels MJ (1989) In vitro mutated phytohemagglutinin genes expressed in tobacco seeds: role of glycans in protein targeting and stability. Plant Cell 1: 95-104
    • (1989) Plant Cell , vol.1 , pp. 95-104
    • Voelker, T.A.1    Herman, E.M.2    Chrispeels, M.J.3
  • 234
    • 0027942615 scopus 로고
    • AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calcium-dependent lipid binding domain
    • Welters P, Takegawa K, Emr SD, Chrispeels MJ (1994) AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calcium-dependent lipid binding domain. Proc Natl Acad Sci USA 91: 11398-11412
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11398-11412
    • Welters, P.1    Takegawa, K.2    Emr, S.D.3    Chrispeels, M.J.4
  • 235
    • 0027080272 scopus 로고
    • Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole
    • Wilcox CA, Redding K, Wright R, Fuller RS (1992) Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole. Mol Biol Cell 3: 1353-1371
    • (1992) Mol Biol Cell , vol.3 , pp. 1353-1371
    • Wilcox, C.A.1    Redding, K.2    Wright, R.3    Fuller, R.S.4
  • 236
    • 0025405663 scopus 로고
    • Role of propeptide glycan in post-translational processing and transport of barley lectin to vacuoles in transgenic tobacco
    • Wilkins TA, Bednarek SY, Raikhel NV (1990) Role of propeptide glycan in post-translational processing and transport of barley lectin to vacuoles in transgenic tobacco. Plant Cell 2: 301-313
    • (1990) Plant Cell , vol.2 , pp. 301-313
    • Wilkins, T.A.1    Bednarek, S.Y.2    Raikhel, N.V.3
  • 237
    • 0027186301 scopus 로고
    • Vps1p, a member of the dynamin GTPase family, is necessary for Golgi membrane protein retention in S. cerevisiae
    • Wilsbach K, Payne GS (1993a) Vps1p, a member of the dynamin GTPase family, is necessary for Golgi membrane protein retention in S. cerevisiae. EMBO J 8: 3049-3059
    • (1993) EMBO J , vol.8 , pp. 3049-3059
    • Wilsbach, K.1    Payne, G.S.2
  • 238
    • 0027379234 scopus 로고
    • Dynamic retention of TGN proteins in Saccharomyces cerevisiae
    • - - (1993b) Dynamic retention of TGN proteins in Saccharomyces cerevisiae. Trends Cell Biol 3: 426-431
    • (1993) Trends Cell Biol , vol.3 , pp. 426-431
  • 239
    • 0001227894 scopus 로고
    • The plant vacuole: A multifunctional compartment
    • Wink M (1993) The plant vacuole: a multifunctional compartment. J Exp Bot 44 Suppl: 231-246
    • (1993) J Exp Bot , vol.44 , Issue.SUPPL. , pp. 231-246
    • Wink, M.1
  • 240
    • 0002371680 scopus 로고
    • Vacuolar localization of proteases and degradation of chloroplasts in mesophyll protoplasts from senescing primary wheat leaves
    • Wittenbach VA, Lin A, Hebert RR (1982) Vacuolar localization of proteases and degradation of chloroplasts in mesophyll protoplasts from senescing primary wheat leaves. Plant Physiol 69: 98-102
    • (1982) Plant Physiol , vol.69 , pp. 98-102
    • Wittenbach, V.A.1    Lin, A.2    Hebert, R.R.3
  • 241
    • 0021734410 scopus 로고
    • Segregation of transferrin to a mildly acidic (pH 6.5) para-Golgi compartment in the recycling pathway
    • Yamashiro DJ, Tycko B, Fluss SR, Maxfield FR (1984) Segregation of transferrin to a mildly acidic (pH 6.5) para-Golgi compartment in the recycling pathway. Cell 37: 789-800
    • (1984) Cell , vol.37 , pp. 789-800
    • Yamashiro, D.J.1    Tycko, B.2    Fluss, S.R.3    Maxfield, F.R.4
  • 242
    • 0025696339 scopus 로고
    • A novel pathway of import of alpha mannosidase, a marker of vacuolar membrane in Saccharomyces cervisiae
    • Yoshibisha T, Anraku Y (1990) A novel pathway of import of alpha mannosidase, a marker of vacuolar membrane in Saccharomyces cervisiae. J Biol Chem 265: 22418-22425
    • (1990) J Biol Chem , vol.265 , pp. 22418-22425
    • Yoshibisha, T.1    Anraku, Y.2
  • 243
    • 0000031926 scopus 로고
    • Increases in binding protein (BiP) accompany changes in protein body morphology in three highlysine mutants of maize
    • Zhang F, Boston RS (1992) Increases in binding protein (BiP) accompany changes in protein body morphology in three highlysine mutants of maize. Protoplasma 171: 142-152
    • (1992) Protoplasma , vol.171 , pp. 142-152
    • Zhang, F.1    Boston, R.S.2
  • 244
    • 0028049917 scopus 로고
    • Intermolecular association of lysosomal protein precursors during biosynthesis
    • Zhu Y, Conner GE (1994) Intermolecular association of lysosomal protein precursors during biosynthesis. J Biol Chem 269: 3846-3851
    • (1994) J Biol Chem , vol.269 , pp. 3846-3851
    • Zhu, Y.1    Conner, G.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.