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Volumn 143, Issue 5, 1998, Pages 1183-1189

Integral membrane protein sorting to vacuoles in plant cells: Evidence for two pathways

Author keywords

Brefeldin A; Cytoplasmic tail; Sorting determinant; Transmembrane domain; Vacuolar sorting receptor

Indexed keywords

ALPHA TONOPLAST INTRINSIC PROTEIN; BREFELDIN A; GAMMA TONOPLAST INTRINSIC PROTEIN; GLYCAN DERIVATIVE; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 0032583163     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.5.1183     Document Type: Article
Times cited : (188)

References (44)
  • 1
    • 0031055434 scopus 로고    scopus 로고
    • Two separate signals act independently to localize a yeast late golgi membrane protein through a combination of retrieval and retention
    • Bryant, N.J., and T.H. Stevens. 1997. Two separate signals act independently to localize a yeast late golgi membrane protein through a combination of retrieval and retention. J. Cell Biol. 136:287-297.
    • (1997) J. Cell Biol. , vol.136 , pp. 287-297
    • Bryant, N.J.1    Stevens, T.H.2
  • 2
    • 0029088909 scopus 로고
    • The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localisation
    • Cereghino, J.L., E.G. Marcusson, and S.D. Emr. 1995. The cytoplasmic tail domain of the vacuolar protein sorting receptor Vps10p and a subset of VPS gene products regulate receptor stability, function, and localisation. Mol. Biol. Cell. 6:1089-1102.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 1089-1102
    • Cereghino, J.L.1    Marcusson, E.G.2    Emr, S.D.3
  • 3
    • 0001069047 scopus 로고
    • Tonoplast and soluble vacuolar proteins are targeted by different mechanisms
    • Gomez, L., and M.J. Chrispeels. 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
  • 4
    • 0006758536 scopus 로고
    • Direct evidence for a sugar transport mechanism in isolated vacuoles
    • Guy, M., L. Reinhold, and D. Michaeli. 1979. Direct evidence for a sugar transport mechanism in isolated vacuoles. Plant Physiol. 64:61-64.
    • (1979) Plant Physiol. , vol.64 , pp. 61-64
    • Guy, M.1    Reinhold, L.2    Michaeli, D.3
  • 5
    • 0029157875 scopus 로고
    • Stratification of storage proteins in the protein storage vacuole of developing cotyledons of Pisum sativum L.
    • Hinz, G., B. Hoh, I. Hohl, and D.G. Robinson. 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
    • Hinz, G.1    Hoh, B.2    Hohl, I.3    Robinson, D.G.4
  • 6
    • 0026903856 scopus 로고
    • Protein sorting to the vacuolar membrane
    • Höfte, H., and M.J. Chrispeels. 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
  • 7
    • 8244222779 scopus 로고
    • Vegetative and seed-specific forms of tonoplast intrinsic protein in the vacuolar membrane of Arabidopsis thaliana
    • Höfte, H., L. Hubbard, J. Reizer, D. Ludevid, E.M. Herman, and M.J. Chrispeels. 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
  • 8
    • 0029860460 scopus 로고    scopus 로고
    • Transport of storage proteins to the vacuole is mediated by vesicles without a clathrin coat
    • Hohl, I., D.G. Robinson, M.C. Chrispeels, and G. Hinz. 1996. Transport of storage proteins to the vacuole is mediated by vesicles without a clathrin coat. J. Cell Sci. 109:2539-2550.
    • (1996) J. Cell Sci. , vol.109 , pp. 2539-2550
    • Hohl, I.1    Robinson, D.G.2    Chrispeels, M.C.3    Hinz, G.4
  • 9
    • 0000677652 scopus 로고
    • Purification and characterization of aleurain: A plant thiol protease functionally homologous to mammalian cathepsin H
    • Holwerda, B.C., and J.C. Rogers. 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
  • 10
    • 0001600705 scopus 로고
    • In vitro processing of aleurain, a barley vacuolar thiol protease
    • Holwerda, B.C., N.J. Galvin, T.J. Baranski, and J.C. Rogers. 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
  • 11
    • 0026828751 scopus 로고
    • Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions
    • Holwerda, B.C., H.S. Padgett, and J.C. Rogers. 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
  • 13
    • 0342444416 scopus 로고
    • GUS fusions: Beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson, R.A., T.A. Kavanaugh, and M.W. Bevan. 1987. GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO (Eur. Mol. Biol. Organ.) J. 6:3901-3907.
    • (1987) EMBO (Eur. Mol. Biol. Organ.) J. , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanaugh, T.A.2    Bevan, M.W.3
  • 14
    • 0001438180 scopus 로고
    • An abundant, highly conserved tonoplast protein in seeds
    • Johnson, K.D., E.M. Herman, and M.J. Chrispeels. 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
  • 15
    • 0032518685 scopus 로고    scopus 로고
    • Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with α-1,6-mannosyltransferase activity
    • Jungmann, J., and S. Munro. 1998. Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with α-1,6-mannosyltransferase activity. EMBO (Eur. Mol Biol. Organ.) J. 17:423-434.
    • (1998) EMBO (Eur. Mol Biol. Organ.) J. , vol.17 , pp. 423-434
    • Jungmann, J.1    Munro, S.2
  • 16
    • 0028201318 scopus 로고
    • Purification and initial characterization of a potential plant vacuolar targeting receptor
    • Kirsch, T., N. Paris, J.M. Butler, L. Beevers, and J.C. Rogers. 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
  • 17
    • 0026561901 scopus 로고
    • Brefeldin A: Insights into the control of membrane traffic and organelle structure
    • Klausner, R.D., J.G. Donaldson, and J. Lippincott-Schwartz. 1992. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol. 116:1071-1080.
    • (1992) J. Cell Biol. , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 18
    • 0032510146 scopus 로고    scopus 로고
    • Immunoreceptor DAP12 bearing a tyrosine-based activation motif is involved in activating NK cells
    • Lanier, L.L., B.C. Corliss, J. Wu, C. Leong, and J.H. Phillips. 1998. Immunoreceptor DAP12 bearing a tyrosine-based activation motif is involved in activating NK cells. Nature. 391:703-707.
    • (1998) Nature , vol.391 , pp. 703-707
    • Lanier, L.L.1    Corliss, B.C.2    Wu, J.3    Leong, C.4    Phillips, J.H.5
  • 19
    • 0000406542 scopus 로고
    • Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins
    • Lauriér, M., M.C. Lauriér, M.J. Chrispeels, K.D. Johnson, and A. Sturm. 1989. Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins. Plant Physiol. 90:1182-1188.
    • (1989) Plant Physiol. , vol.90 , pp. 1182-1188
    • Lauriér, M.1    Lauriér, M.C.2    Chrispeels, M.J.3    Johnson, K.D.4    Sturm, A.5
  • 20
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER
    • Lippincott-Schwartz, J., L.C. Yuan, J.S. Bonifacino, and R.D. Klausner. 1989. Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell. 56:801-813.
    • (1989) Cell , vol.56 , pp. 801-813
    • Lippincott-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 21
    • 0028332917 scopus 로고
    • The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by VPS10 gene
    • Marcusson, E.G., B.F. Horazdovsky, J.L. Cereghino, E. Gharakhanian, and S.D. Emr. 1994. The sorting receptor for yeast vacuolar carboxypeptidase Y is encoded by VPS10 gene. Cell. 77:579-586.
    • (1994) Cell , vol.77 , pp. 579-586
    • Marcusson, E.G.1    Horazdovsky, B.F.2    Cereghino, J.L.3    Gharakhanian, E.4    Emr, S.D.5
  • 22
    • 0031106781 scopus 로고    scopus 로고
    • Protein sorting by tryosine-based signals: Adapting to the Ys and wherefores
    • Marks, M.S., H. Ohno, T. Kirchhausen, and J.S. Bonifacino. 1997. Protein sorting by tryosine-based signals: adapting to the Ys and wherefores. Trends Cell Biol. 7:124-128.
    • (1997) Trends Cell Biol. , vol.7 , pp. 124-128
    • Marks, M.S.1    Ohno, H.2    Kirchhausen, T.3    Bonifacino, J.S.4
  • 23
    • 0028981718 scopus 로고
    • Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells
    • Matsuoka, K., D.C. Bassham, N. Raikhel, and K. Nakamura. 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
  • 24
    • 0001033053 scopus 로고
    • A revised medium for rapid growth and bio-assays with tobacco tissue culture
    • Murashige, T., and F. Skoog. 1962. A revised medium for rapid growth and bio-assays with tobacco tissue culture. Plant Physiol. 78:876-882.
    • (1962) Plant Physiol. , vol.78 , pp. 876-882
    • Murashige, T.1    Skoog, F.2
  • 25
    • 0032169928 scopus 로고    scopus 로고
    • Sorting of proteins to vacuoles in plant cells
    • Neuhaus, J.-M., and J.C. Rogers. 1998. Sorting of proteins to vacuoles in plant cells. Plant Mol. Biol. 38:127-144.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 127-144
    • Neuhaus, J.-M.1    Rogers, J.C.2
  • 26
    • 0028283489 scopus 로고
    • Sorting of membrane proteins in the yeast secretory pathway
    • Nothwehr, S.F., and T.H. Stevens. 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
  • 27
    • 0027204816 scopus 로고
    • Membrane protein retention in the yeast Golgi apparatus: Dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues
    • Nothwehr, S.F., C.J. Roberts, and T.H. Stevens. 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
    • Nothwehr, S.F.1    Roberts, C.J.2    Stevens, T.H.3
  • 28
    • 0028953080 scopus 로고
    • Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane
    • Nothwehr, S.F., E. Conibear, and T.H. Stevens. 1995. Golgi and vacuolar membrane proteins reach the vacuole in vps1 mutant yeast cells via the plasma membrane. J. Cell Biol. 129:35-46.
    • (1995) J. Cell Biol. , vol.129 , pp. 35-46
    • Nothwehr, S.F.1    Conibear, E.2    Stevens, T.H.3
  • 30
    • 0001009574 scopus 로고    scopus 로고
    • Compartmentation of proteins in the endomembrane system of plant cells
    • Okita, T.W., and J.C. Rogers. 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
  • 32
    • 0030060549 scopus 로고    scopus 로고
    • The role of receptors in targeting soluble proteins from the secretory pathway to the vacuole
    • Paris, N., and J.C. Rogers. 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
  • 33
    • 0030014157 scopus 로고    scopus 로고
    • Plant cells contain two functionally distinct vacuolar compartments
    • Paris, N., C.M. Stanley, R.L. Jones, and J.C. Rogers. 1996. Plant cells contain two functionally distinct vacuolar compartments. Cell. 85:563-572.
    • (1996) Cell , vol.85 , pp. 563-572
    • Paris, N.1    Stanley, C.M.2    Jones, R.L.3    Rogers, J.C.4
  • 35
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner, J.C., and H.R.B. Pelham. 1997. Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO (Eur. Mol. Biol. Organ.) J. 16:1832-1841.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.B.2
  • 36
    • 0026727566 scopus 로고
    • Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment
    • Roberts, C.J., S.F. Nothwehr, and T.H. Stevens. 1992. Membrane protein sorting in the yeast secretory pathway: evidence that the vacuole may be the default compartment. J. Cell Biol. 119:63-83.
    • (1992) J. Cell Biol. , vol.119 , pp. 63-83
    • Roberts, C.J.1    Nothwehr, S.F.2    Stevens, T.H.3
  • 37
    • 0000367861 scopus 로고
    • One vacuole or two vacuoles: Do protein storage vacuoles arise de novo during pea cotyledon development?
    • Robinson, D.G., B. Hoh, G. Hinz., and B.-K. Jeong. 1995. One vacuole or two vacuoles: do protein storage vacuoles arise de novo during pea cotyledon development? J. Plant Physiol. 145:654-664.
    • (1995) J. Plant Physiol. , vol.145 , pp. 654-664
    • Robinson, D.G.1    Hoh, B.2    Hinz, G.3    Jeong, B.-K.4
  • 38
    • 0031817650 scopus 로고    scopus 로고
    • Vesicle transfer of storage protein to the vacuole: The role of the Golgi apparatus and multivesicular bodies
    • Robinson, D.G., M. Baumer, G. Hinz, and I. Hohl. 1998. Vesicle transfer of storage protein to the vacuole: the role of the Golgi apparatus and multivesicular bodies. J. Plant Physiol. 152:659-667.
    • (1998) J. Plant Physiol. , vol.152 , pp. 659-667
    • Robinson, D.G.1    Baumer, M.2    Hinz, G.3    Hohl, I.4
  • 39
    • 0011742571 scopus 로고
    • Aleurain: A barley thiol protease closely related to mammalian cathepsin H
    • Rogers, J.C., D. Dean, and G.R. Heck. 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
  • 40
    • 0031170950 scopus 로고    scopus 로고
    • Monoclonal antibodies to barley aleurain and homologues from other plants
    • Rogers, S.W., M. Burks, and J.C. Rogers. 1997. Monoclonal antibodies to barley aleurain and homologues from other plants. Plant J. 11:1359-1368.
    • (1997) Plant J. , vol.11 , pp. 1359-1368
    • Rogers, S.W.1    Burks, M.2    Rogers, J.C.3
  • 41
    • 0029953563 scopus 로고    scopus 로고
    • Endoplasmic reticulum localization of Sec12p is achieved by two mechanism: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain
    • Sato, M., K. Sato, and A. Nakano. 1996. Endoplasmic reticulum localization of Sec12p is achieved by two mechanism: Rer1p-dependent retrieval that requires the transmembrane domain and Rer1p-independent retention that involves the cytoplasmic domain. J. Cell Biol. 134:279-293.
    • (1996) J. Cell Biol. , vol.134 , pp. 279-293
    • Sato, M.1    Sato, K.2    Nakano, A.3
  • 42
  • 43
    • 0031439665 scopus 로고    scopus 로고
    • A pumpkin 72-kDa membrane protein of precursor-accumulating vesicles has characteristics of a vacuolar sorting receptor
    • Shimada, T., M. Kuroyanagi, M. Nishimura, and I. Hara-Nishimura. 1997. A pumpkin 72-kDa membrane protein of precursor-accumulating vesicles has characteristics of a vacuolar sorting receptor. Plant Cell Physiol. 38:1414-1420.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1414-1420
    • Shimada, T.1    Kuroyanagi, M.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 44
    • 0025211918 scopus 로고
    • The Ustilago maydis KP6 killer toxin: Structure, expression in Saccharomyces cerevisiae and relationship to other cellular toxins
    • Tao, J., I. Ginsberg, N. Banerjee, Y. Koltin, W. Held, and J.A. Bruenn. 1990. The Ustilago maydis KP6 killer toxin: structure, expression in Saccharomyces cerevisiae and relationship to other cellular toxins. Mol. Cell. Biol. 10: 1373-1381.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1373-1381
    • Tao, J.1    Ginsberg, I.2    Banerjee, N.3    Koltin, Y.4    Held, W.5    Bruenn, J.A.6


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