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Volumn 9, Issue 10, 1997, Pages 1869-1880

Protein quality control along the route to the plant vacuole

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EID: 0031251943     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.9.10.1869     Document Type: Article
Times cited : (150)

References (41)
  • 1
    • 0000086183 scopus 로고
    • New cloning vehicles for transformation of higher plants
    • An, G., Watson, B.D., Stachel, S., Gordon, M.P., and Nester, E.W. (1985). New cloning vehicles for transformation of higher plants. EMBO J. 4, 277-284.
    • (1985) EMBO J. , vol.4 , pp. 277-284
    • An, G.1    Watson, B.D.2    Stachel, S.3    Gordon, M.P.4    Nester, E.W.5
  • 2
    • 0000105263 scopus 로고
    • Transformation of tobacco, tomato, potato, and Arabidopsis thaliana using a binary Ti vector system
    • An, G., Watson, B.D., and Chiang, C.C. (1986). Transformation of tobacco, tomato, potato, and Arabidopsis thaliana using a binary Ti vector system. Plant Physiol. 81, 301-305.
    • (1986) Plant Physiol. , vol.81 , pp. 301-305
    • An, G.1    Watson, B.D.2    Chiang, C.C.3
  • 3
    • 0026912939 scopus 로고
    • Constitutive expression of the β-phaseolin gene in different tissues of transgenic alfalfa does not ensure phaseolin accumulation in non-seed tissue
    • Bagga, S., Sutton, D., Kemp, J.D., and Sengupta-Gopalan, C. (1992). Constitutive expression of the β-phaseolin gene in different tissues of transgenic alfalfa does not ensure phaseolin accumulation in non-seed tissue. Plant Mol. Biol. 19, 951-958.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 951-958
    • Bagga, S.1    Sutton, D.2    Kemp, J.D.3    Sengupta-Gopalan, C.4
  • 4
    • 0026127990 scopus 로고
    • Differential accumulation of four phaseolin glycoforms in transgenic tobacco
    • Bustos, M.M., Kalkan, F.A., VandenBosh, K.A., and Hall, T.C. (1991). Differential accumulation of four phaseolin glycoforms in transgenic tobacco. Plant Mol. Biol. 16,381-395.
    • (1991) Plant Mol. Biol. , pp. 381-395
    • Bustos, M.M.1    Kalkan, F.A.2    Vandenbosh, K.A.3    Hall, T.C.4
  • 5
    • 0026316263 scopus 로고
    • Expression of wild-type and mutated vacuolar storage protein phaseolin in Xenopus oocytes reveals relationships between assembly and intracellular transport
    • Ceriotti, A., Pedrazzini, E., Fabbrini, M.S., Zoppè, M., Bollini, Ft., and Vitale, A. (1991). Expression of wild-type and mutated vacuolar storage protein phaseolin in Xenopus oocytes reveals relationships between assembly and intracellular transport. Eur. J. Biochem. 202,959-968.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 959-968
    • Ceriotti, A.1    Pedrazzini, E.2    Fabbrini, M.S.3    Zoppè, M.4    Bollini, F.5    Vitale, A.6
  • 6
    • 0029445420 scopus 로고
    • Import into the endoplasmic reticulum
    • Plant Cell Biology, D.W. Galbraith, O.P. Bourque, and H.J. Bohnert, eds (San Diego, CA: Academic Press)
    • Ceriotti, A., Pedrazzini, E., De Silvestris, M., and Vitale, A. (1995). Import into the endoplasmic reticulum. In Methods in Cell Biology, Vol. 50, Plant Cell Biology, D.W. Galbraith, O.P. Bourque, and H.J. Bohnert, eds (San Diego, CA: Academic Press), pp. 295-308.
    • (1995) Methods in Cell Biology , vol.50 , pp. 295-308
    • Ceriotti, A.1    Pedrazzini, E.2    De Silvestris, M.3    Vitale, A.4
  • 7
    • 0001672203 scopus 로고
    • Heat stress enhances phytohemagglutinin synthesis but inhibits its transport out of the endoplasmic reticulum
    • Chrispeels, M.J., and Greenwood, U.S. (1987). Heat stress enhances phytohemagglutinin synthesis but inhibits its transport out of the endoplasmic reticulum. Plant Physiol. 83,778-784.
    • (1987) Plant Physiol. , vol.83 , pp. 778-784
    • Chrispeels, M.J.1    Greenwood, U.S.2
  • 8
    • 0030339563 scopus 로고    scopus 로고
    • The maize γ-zein sequesters a-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm
    • Coleman, C.E., Herman, E.M., Takasaki, K., and Larkins, B.A. (1996). The maize γ-zein sequesters a-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm. Plant Cell 8, 2335-2345.
    • (1996) Plant Cell , vol.8 , pp. 2335-2345
    • Coleman, C.E.1    Herman, E.M.2    Takasaki, K.3    Larkins, B.A.4
  • 9
    • 0026893762 scopus 로고
    • Bean homologs of the mammalian glucose regulated proteins: Induction by tunicamycin and interaction with newly synthesized storage proteins in the endoplasmic reticulum
    • D'Amico, L, Valsasina, B., Daminati, M.G., Fabbrini, M.S., Nitti, G., Bollini, R., Ceriotti, A., and Vitale, A. (1992). Bean homologs of the mammalian glucose regulated proteins: Induction by tunicamycin and interaction with newly synthesized storage proteins in the endoplasmic reticulum. Plant J. 2,443-455.
    • (1992) Plant J. , vol.2 , pp. 443-455
    • D'Amico, L.1    Valsasina, B.2    Daminati, M.G.3    Fabbrini, M.S.4    Nitti, G.5    Bollini, R.6    Ceriotti, A.7    Vitale, A.8
  • 10
    • 0030019434 scopus 로고    scopus 로고
    • Soluble endoplasmic reticulum proteins and their function in protein synthesis and transport
    • Denecke, J. (1996). Soluble endoplasmic reticulum proteins and their function in protein synthesis and transport. Plant Physiol. Biochem. 34,197-205.
    • (1996) Plant Physiol. Biochem. , vol.34 , pp. 197-205
    • Denecke, J.1
  • 11
  • 12
    • 0000695967 scopus 로고
    • Heat-induced conformational changes in phaseolin and its relation to proteolysis
    • Deshpande, S.S., and Damodaran, S. (1989). Heat-induced conformational changes in phaseolin and its relation to proteolysis. Biochim. Biophys. Acta 998,179-188.
    • (1989) Biochim. Biophys. Acta , vol.998 , pp. 179-188
    • Deshpande, S.S.1    Damodaran, S.2
  • 13
    • 0024639678 scopus 로고
    • Role of posttranslational cleavage in glycinin assembly
    • Dickinson, C.D., Hussein, E.H.A., and Nielsen, N.C. (1989). Role of posttranslational cleavage in glycinin assembly. Plant Cell 1, 459-469.
    • (1989) Plant Cell , vol.1 , pp. 459-469
    • Dickinson, C.D.1    Hussein, E.H.A.2    Nielsen, N.C.3
  • 14
    • 0027137885 scopus 로고
    • Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast
    • Finger, A., Knop, M., and Wolf, D.H. (1993). Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Eur. J. Biochem. 218,565-574.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 565-574
    • Finger, A.1    Knop, M.2    Wolf, D.H.3
  • 15
    • 0028103135 scopus 로고
    • Distribution of xylosylation and fucosylation in the plant Golgi apparatus
    • Fitchette-Lainé, A.-C., Gomord, V., Chekkafi, A., and Faye, L. (1994). Distribution of xylosylation and fucosylation in the plant Golgi apparatus. Plant J. 5,673-682.
    • (1994) Plant J. , vol.5 , pp. 673-682
    • Fitchette-Lainé, A.-C.1    Gomord, V.2    Chekkafi, A.3    Faye, L.4
  • 16
    • 0027440769 scopus 로고
    • Quality control of ER synthesized proteins: An exposed thiol group as a three-way switch mediating assembly, retention and degradation
    • Fra, A., Fagioli, C., Finazzi, D., Sitia, R., and Alberini, C. (1993). Quality control of ER synthesized proteins: An exposed thiol group as a three-way switch mediating assembly, retention and degradation. EMBO J. 12,4755-4761.
    • (1993) EMBO J. , vol.12 , pp. 4755-4761
    • Fra, A.1    Fagioli, C.2    Finazzi, D.3    Sitia, R.4    Alberini, C.5
  • 18
    • 0001069047 scopus 로고
    • Tonoplast and soluble vacuolar proteins are targeted by different mechanisms
    • Gomez, L., and Chrispeels, M.J. (1993). Tonoplast and soluble vacuolar proteins are targeted by different mechanisms. Plant Cell 5,1113-1124.
    • (1993) Plant Cell , vol.5 , pp. 1113-1124
    • Gomez, L.1    Chrispeels, M.J.2
  • 19
    • 0030060527 scopus 로고    scopus 로고
    • Effect of gibberellin and heat shock on the lipid composition of endoplasmic reticulum in barley aleurone layers
    • Grindstaff, K.K., Fielding, L.A., and Brodl, M.R. (1996). Effect of gibberellin and heat shock on the lipid composition of endoplasmic reticulum in barley aleurone layers. Plant Physiol. 110,571-581.
    • (1996) Plant Physiol. , vol.110 , pp. 571-581
    • Grindstaff, K.K.1    Fielding, L.A.2    Brodl, M.R.3
  • 20
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C., and Helenius, A. (1995). Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7, 523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 21
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants
    • Hiatt, A., Cafferkey, R., and Bowdish, K. (1989). Production of antibodies in transgenic plants. Nature 342, 76-78.
    • (1989) Nature , vol.342 , pp. 76-78
    • Hiatt, A.1    Cafferkey, R.2    Bowdish, K.3
  • 22
    • 34250095670 scopus 로고
    • A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants
    • Huffman, L.M., Donaldson, D.D., and Herman, E.M. (1988). A modified storage protein is synthesized, processed, and degraded in the seeds of transgenic plants. Plant Mol. Biol. 11, 717-729.
    • (1988) Plant Mol. Biol. , vol.11 , pp. 717-729
    • Huffman, L.M.1    Donaldson, D.D.2    Herman, E.M.3
  • 23
    • 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
  • 24
    • 0000502672 scopus 로고
    • KDEL-containing auxin binding protein is secreted to the plasma membrane and cell wall
    • Jones, A.M., and Herman, E.M. (1993). KDEL-containing auxin binding protein is secreted to the plasma membrane and cell wall. Plant Physiol. 101, 595-606.
    • (1993) Plant Physiol. , vol.101 , pp. 595-606
    • Jones, A.M.1    Herman, E.M.2
  • 25
    • 0028815044 scopus 로고
    • Accumulation and proteolytic processing of vicilin deletion-mutant proteins in the leaf and seed of transgenic tobacco
    • Kermode, A.R., Fisher, S.A., Polishchuk, E., Wandelt, C., Spencer, D., and Higgins, T.J.V. (1995). Accumulation and proteolytic processing of vicilin deletion-mutant proteins in the leaf and seed of transgenic tobacco. Planta 197,501-513.
    • (1995) Planta , vol.197 , pp. 501-513
    • Kermode, A.R.1    Fisher, S.A.2    Polishchuk, E.3    Wandelt, C.4    Spencer, D.5    Higgins, T.J.V.6
  • 26
    • 0026332974 scopus 로고
    • Xylose-specific antibodies as markers of subcompartmentation of terminal glycosylation in the Golgi apparatus of sycamore cells
    • Laine, A.-C., Gomord, V., and Faye, L. (1991). Xylose-specific antibodies as markers of subcompartmentation of terminal glycosylation in the Golgi apparatus of sycamore cells. FEES Lett. 295, 179-184.
    • (1991) FEES Lett. , vol.295 , pp. 179-184
    • Laine, A.-C.1    Gomord, V.2    Faye, L.3
  • 28
    • 0030229971 scopus 로고    scopus 로고
    • Go outside and see the proteasome
    • Lord, J.M. (1996). Go outside and see the proteasome. Curr. Biol. 6, 1067-1069.
    • (1996) Curr. Biol. , vol.6 , pp. 1067-1069
    • Lord, J.M.1
  • 29
    • 0030900410 scopus 로고    scopus 로고
    • The rate of phaseotin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains
    • Lupattelli, F., Pedrazzini, E., Boilini, R., Vitale, A., and Ceriotti, A. (1997). The rate of phaseotin assembly is controlled by the glucosylation state of its N-linked oligosaccharide chains. Plant Cell 9, 597-609.
    • (1997) Plant Cell , vol.9 , pp. 597-609
    • Lupattelli, F.1    Pedrazzini, E.2    Boilini, R.3    Vitale, A.4    Ceriotti, A.5
  • 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
    • 0030038133 scopus 로고    scopus 로고
    • The binding protein (BiP) and the synthesis of secretory proteins
    • Pedrazzini, E., and 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
  • 33
    • 0028894404 scopus 로고
    • Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole
    • Pueyo, J.J., Chrispeels, M.J., and Herman, E.M. (1995). Degradation of transport-competent destabilized phaseolin with a signal for retention in the endoplasmic reticulum occurs in the vacuole. Planta 196,586-596.
    • (1995) Planta , vol.196 , pp. 586-596
    • Pueyo, J.J.1    Chrispeels, M.J.2    Herman, E.M.3
  • 34
    • 0001895061 scopus 로고
    • Expression and purification of maltose-binding protein fusions
    • P.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, and K. Struhl, eds (New York: Greene Publishing Associates/Wiley and Sons)
    • Riggs, P. (1992). Expression and purification of maltose-binding protein fusions. In Short Protocols in Molecular Biology, 2nd ed, P.M. Ausubel, R. Brent, R.E. Kingston, D.D. Moore, J.G. Seidman, J.A. Smith, and K. Struhl, eds (New York: Greene Publishing Associates/Wiley and Sons), pp. 1621-1627.
    • (1992) Short Protocols in Molecular Biology, 2nd Ed , pp. 1621-1627
    • Riggs, P.1
  • 35
    • 0029328357 scopus 로고
    • Seed storage proteins: Structures and biosynthesis
    • Shewry, P.R., Napier, J.A., and Tatham, A.S. (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
  • 36
    • 0022432415 scopus 로고
    • Nucleotide sequences from phaseolin cDNA clones: The major storage proteins from Phaseolus vulgaris are encoded by two unique gene families
    • Slightom, J.L., Drong, R.F., Klassy, R.C., and Hoffman, L.M. (1985). Nucleotide sequences from phaseolin cDNA clones: The major storage proteins from Phaseolus vulgaris are encoded by two unique gene families. Nucleic Acids Res. 13,6483-6498.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 6483-6498
    • Slightom, J.L.1    Drong, R.F.2    Klassy, R.C.3    Hoffman, L.M.4
  • 37
    • 0023645611 scopus 로고
    • Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side chains of the bean storage protein phaseolin
    • Sturm, A., Van Kuik, U.A., Vliegenthart, J.F.G., and Chrispeels, M.J. (1987). Structure, position, and biosynthesis of the high mannose and the complex oligosaccharide side chains of the bean storage protein phaseolin. J. Biol. Chem. 262,13392-13403.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13392-13403
    • Sturm, A.1    Van Kuik, U.A.2    Vliegenthart, J.F.G.3    Chrispeels, M.J.4
  • 39
    • 85051589413 scopus 로고
    • Legume storage proteins
    • J. Kigel and G. Galili, eds (New York: Marcel Dekker)
    • Vitale, A., and Bollini, R. (1995). Legume storage proteins. In Seed Development and Germination, J. Kigel and G. Galili, eds (New York: Marcel Dekker), pp. 73-102.
    • (1995) Seed Development and Germination , pp. 73-102
    • Vitale, A.1    Bollini, R.2
  • 40
    • 0021274996 scopus 로고
    • Transient W-acetylglucosamine in the biosynthesis of phytohemagglutinin: Attachment in the Golgi apparatus and removal in protein bodies
    • Vitale, A., and Chrispeels, M.J. (1984). Transient W-acetylglucosamine in the biosynthesis of phytohemagglutinin: Attachment in the Golgi apparatus and removal in protein bodies. J. Cell Biol. 99,133-140.
    • (1984) J. Cell Biol. , vol.99 , pp. 133-140
    • Vitale, A.1    Chrispeels, M.J.2
  • 41
    • 0029167492 scopus 로고
    • The binding protein associates with monomeric phaseolin
    • Vitale, A., Bielli, A., and Ceriotti, A. (1995). The binding protein associates with monomeric phaseolin. Plant Physiol. 107,1411-1418.
    • (1995) Plant Physiol. , vol.107 , pp. 1411-1418
    • Vitale, A.1    Bielli, A.2    Ceriotti, A.3


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