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Volumn 85, Issue 4, 1996, Pages 563-572

Plant cells contain two functionally distinct vacuolar compartments

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN;

EID: 0030014157     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81256-8     Document Type: Article
Times cited : (341)

References (39)
  • 1
    • 0030038126 scopus 로고    scopus 로고
    • Isolation of intact protein storage vacuoles from barley aleurone: Identification of aspartic and cysteine proteases
    • Bethke, P.C., Hillmer, S., and Jones, R.L. (1996). Isolation of intact protein storage vacuoles from barley aleurone: identification of aspartic and cysteine proteases. Plant Physiol. 110, 521-529.
    • (1996) Plant Physiol. , vol.110 , pp. 521-529
    • Bethke, P.C.1    Hillmer, S.2    Jones, R.L.3
  • 2
    • 0000199795 scopus 로고
    • Dynamics of vacuolar compartmentation
    • Boller, T., and Wiemken, A. (1986). Dynamics of vacuolar compartmentation. Annu. Rev. Plant Physiol. 37, 137-164.
    • (1986) Annu. Rev. Plant Physiol. , vol.37 , pp. 137-164
    • Boller, T.1    Wiemken, A.2
  • 4
    • 0025718126 scopus 로고
    • Lectins, lectin genes, and their role in plant defense
    • Chrispeels, M.J., and Raikhel, N.V. (1991). Lectins, lectin genes, and their role in plant defense. Plant Cell 3, 1-9.
    • (1991) Plant Cell , vol.3 , pp. 1-9
    • Chrispeels, M.J.1    Raikhel, N.V.2
  • 5
    • 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
  • 6
    • 0002245187 scopus 로고
    • Structural aspects of protein accumulation in developing pea cotyledons. I. Qualitative and quantitative changes in parenchyma cell vacuoles
    • Craig, S., Goodchild, D.J., and Hardham, A.R. (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
    • Craig, S.1    Goodchild, D.J.2    Hardham, A.R.3
  • 7
    • 0013580656 scopus 로고
    • Structural aspects of protein accumulation in developing pea cotyledons. II. Three-dimensional reconstructions of vacuoles and protein bodies from serial sections
    • Craig, S., Goodchild, D.J., and 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
    • Craig, S.1    Goodchild, D.J.2    Miller, C.3
  • 8
    • 0028108664 scopus 로고
    • Comparative modelling of barley-grain aspartic proteinase: A structural rationale for observed hydrolytic specificity
    • Guruprasad, K., Törmäkangas, K., Kervinen, J., and Blundell, T.L. (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    Törmäkangas, K.2    Kervinen, J.3    Blundell, T.L.4
  • 9
    • 0003448569 scopus 로고
    • Cold Spring Harbor, New York: Cold Spring Harbor Laboratory
    • Harlow, E., and Lane, D. (1988). Antibodies: A Laboratory Manual (Cold Spring Harbor, New York: Cold Spring Harbor Laboratory).
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 10
    • 0000680069 scopus 로고
    • Multiple origins of intravacuolar protein accumulation of plant cells
    • S. Malhotra, ed. (Greenwich, Connecticut: JAI Press, Incorporated)
    • Herman, E.M. (1994). Multiple origins of intravacuolar protein accumulation of plant cells. In Advances in Structural Biology, S. Malhotra, ed. (Greenwich, Connecticut: JAI Press, Incorporated), pp. 243-283.
    • (1994) Advances in Structural Biology , pp. 243-283
    • Herman, E.M.1
  • 12
    • 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., and 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
  • 13
    • 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
  • 14
    • 0000677652 scopus 로고
    • Purification and characterization of aleurain: A plant thiol protease functionally homologous to mammalian cathepsin H
    • Holwerda, B.C., and Rogers, J.C. (1992). Purification and characterization of aleurain: a plant thiol protease functionally homologous to mammalian cathepsin H. Plant Physiol. 99, 848-855.
    • (1992) Plant Physiol. , vol.99 , pp. 848-855
    • Holwerda, B.C.1    Rogers, J.C.2
  • 15
    • 0001350519 scopus 로고
    • Structure, functional properties and vacuolar targeting of the barley thiol protease, aleurain
    • Holwerda, B.C., and Rogers, J.C. (1993). Structure, functional properties and vacuolar targeting of the barley thiol protease, aleurain. J. Exp. Bot. 44 (Suppl.), 321-339.
    • (1993) J. Exp. Bot. , vol.44 , Issue.SUPPL. , pp. 321-339
    • Holwerda, B.C.1    Rogers, J.C.2
  • 16
    • 0001600705 scopus 로고
    • In vitro processing of aleurain, a barley vacuolar thiol protease
    • Holwerda, B.C., Galvin, N J., Baranski, T.J., and Rogers, J.C. (1990). In vitro processing of aleurain, a barley vacuolar thiol protease. Plant Cell 2, 1091-1106.
    • (1990) Plant Cell , vol.2 , pp. 1091-1106
    • Holwerda, B.C.1    Galvin, N.J.2    Baranski, T.J.3    Rogers, J.C.4
  • 17
    • 0026828751 scopus 로고
    • Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions
    • Holwerda, B.C., Padgett, H.S., and Rogers, J.C. (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
  • 18
    • 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
  • 20
    • 0028201318 scopus 로고
    • Purification and initial characterization of a potential plant vacuolar targeting receptor
    • Kirsch, T., Paris, N., Butler, J.M., Beevers, L., and Rogers, J.C. (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, J.M.3    Beevers, L.4    Rogers, J.C.5
  • 22
    • 0142134290 scopus 로고
    • Cloning and characterization of root-specific barley lectin
    • Lerner, D.R., and Raikhel, N.V. (1989). Cloning and characterization of root-specific barley lectin. Plant Physiol. 91, 124-129.
    • (1989) Plant Physiol. , vol.91 , pp. 124-129
    • Lerner, D.R.1    Raikhel, N.V.2
  • 23
    • 0000436359 scopus 로고
    • The expression pattern of the tonoplast intrinsic protein γ-TIP in Arabidopsis thaliana is correlated with cell enlargement
    • Ludevid, D., Höfte, H., Himelblau, E., and Chrispeels, M.J. (1992). The expression pattern of the tonoplast intrinsic protein γ-TIP in Arabidopsis thaliana is correlated with cell enlargement. Plant Physiol. 100, 1633-1639.
    • (1992) Plant Physiol. , vol.100 , pp. 1633-1639
    • Ludevid, D.1    Höfte, H.2    Himelblau, E.3    Chrispeels, M.J.4
  • 24
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by VPS10 gene
    • Marcusson, E.G., Horazdovsky, B.F., Cereghino, J.L., Gharakhanian, E., and Emr, S.D. (1994). The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by VPS10 gene. Cell 77, 579-786.
    • (1994) Cell , vol.77 , pp. 579-786
    • Marcusson, E.G.1    Horazdovsky, B.F.2    Cereghino, J.L.3    Gharakhanian, E.4    Emr, S.D.5
  • 25
    • 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., Cozolme, 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    Cozolme, P.3    Marty, F.4
  • 26
    • 0026023554 scopus 로고
    • Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting
    • Matsuoka, K., and Nakamura, K. (1991). Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting. Proc. Natl. Acad. Sci. USA 88, 834-838.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 834-838
    • Matsuoka, K.1    Nakamura, K.2
  • 27
    • 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., and 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
    • Matsuoka, K.1    Bassham, D.C.2    Raikhel, N.3    Nakamura, K.4
  • 28
    • 0027134032 scopus 로고
    • Protein targeting to the vacuole in plant cells
    • Nakamura, K., and Matsuoka, K. (1993). Protein targeting to the vacuole in plant cells. Plant Physiol. 101, 1-6.
    • (1993) Plant Physiol. , vol.101 , pp. 1-6
    • Nakamura, K.1    Matsuoka, K.2
  • 29
    • 0000554345 scopus 로고
    • Processing and transport to the vacuole of a precursor to sweet potato sporamin in transformed tobacco cell line BY-2
    • Nakamura, K., Matsuoka, K., Mukumoto, F., and Watanabe, N. (1993). Processing and transport to the vacuole of a precursor to sweet potato sporamin in transformed tobacco cell line BY-2. J. Exp. Bot. 44 (Suppl.), 331-338.
    • (1993) J. Exp. Bot. , vol.44 , Issue.SUPPL. , pp. 331-338
    • Nakamura, K.1    Matsuoka, K.2    Mukumoto, F.3    Watanabe, N.4
  • 30
    • 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
  • 31
    • 0001405955 scopus 로고
    • Distribution and relationship of cell division and maturation events in Pisum sativum (Fabaceae) seedling roots
    • Rost, T.L., Jones, T.J., and Falk, R.H. (1988). Distribution and relationship of cell division and maturation events in Pisum sativum (Fabaceae) seedling roots. Am. J. Bot. 75, 1571-1583.
    • (1988) Am. J. Bot. , vol.75 , pp. 1571-1583
    • Rost, T.L.1    Jones, T.J.2    Falk, R.H.3
  • 32
    • 0026321028 scopus 로고
    • Primary structure of a barley-grain aspartic proteinase; a plant aspartic proteinae resembling mammalian cathepsin D
    • Runeberg-Roos, P., Törmäkangas, K., and Östman, A. (1991). Primary structure of a barley-grain aspartic proteinase; a plant aspartic proteinae 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
  • 33
    • 0028425479 scopus 로고
    • The aspartic proteinase of barley is avacuolar enzyme that processes probarley lectin in vitro
    • Runeberg-Roos, P., Kervinen, J., Kovaleva, V., Raikhel, N.V., and Gal, S. (1994). The aspartic proteinase of barley is avacuolar enzyme that processes probarley lectin in vitro. Plant Physiol. 105, 321-329.
    • (1994) Plant Physiol. , vol.105 , pp. 321-329
    • Runeberg-Roos, P.1    Kervinen, J.2    Kovaleva, V.3    Raikhel, N.V.4    Gal, S.5
  • 34
    • 0027539185 scopus 로고
    • Colocalization of barley lectin and sporamin in vacuoles of transgenic tobacco plants
    • Schroeder, M.R., Borkhsenious, O.N., Matsuoka, K., Nakamura, K., and Raikhel, N.V. (1993). Colocalization of barley lectin and sporamin in vacuoles of transgenic tobacco plants. Plant Physiol. 101, 451-458.
    • (1993) Plant Physiol. , vol.101 , pp. 451-458
    • Schroeder, M.R.1    Borkhsenious, O.N.2    Matsuoka, K.3    Nakamura, K.4    Raikhel, N.V.5
  • 35
    • 0027955997 scopus 로고
    • Asaposin-like domain influences the intracellular localization, stability, and catalytic activity of human acyloxyacyl hydrolase
    • Staab, J.F., Ginkel, D.L., Rosenberg, G.B., and Munford, R.S. (1994). Asaposin-like domain influences the intracellular localization, stability, and catalytic activity of human acyloxyacyl hydrolase. J. Biol. Chem. 269, 23736-23742.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23736-23742
    • Staab, J.F.1    Ginkel, D.L.2    Rosenberg, G.B.3    Munford, R.S.4
  • 36
    • 0028317608 scopus 로고
    • Tissue-specific localization of aspartic proteinase in developing and germinating barley grains
    • Törmäkangas, K., Kervinen, J., Östman, A., and Teeri, T. (1994). Tissue-specific localization of aspartic proteinase in developing and germinating barley grains. Planta 195, 116-125.
    • (1994) Planta , vol.195 , pp. 116-125
    • Törmäkangas, K.1    Kervinen, J.2    Östman, A.3    Teeri, T.4
  • 37
    • 0000484778 scopus 로고
    • Double immunofluorescence labeling of calmodulin and tubulin in dividing plant cells
    • Wick, S.M., Muto, S., and Duniec, J. (1985). Double immunofluorescence labeling of calmodulin and tubulin in dividing plant cells. Protoplasma 126, 198-206.
    • (1985) Protoplasma , vol.126 , pp. 198-206
    • Wick, S.M.1    Muto, S.2    Duniec, J.3
  • 38
    • 0001227894 scopus 로고
    • The plant vacuole: A multifunctional compartment
    • Wink, M. (1993). The plant vacuole: a multifunctional compartment. J. Exp. Bot. 44 (Supp.), 231-246.
    • (1993) J. Exp. Bot. , vol.44 , Issue.SUPPL. , pp. 231-246
    • Wink, M.1
  • 39
    • 0028049917 scopus 로고
    • Intermolecular association of lysosomal protein precursors during biosynthesis
    • Zhu, Y., and Conner, G.E. (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


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