메뉴 건너뛰기




Volumn 18, Issue 1, 2006, Pages 198-211

Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperon BiP may play an active role in quality control within the secretory pathway

Author keywords

[No Author keywords available]

Indexed keywords

DEGRADATION; QUALITY CONTROL; TOBACCO;

EID: 33645737420     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.105.036665     Document Type: Article
Times cited : (88)

References (82)
  • 2
    • 4444288866 scopus 로고    scopus 로고
    • Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones
    • Ben-Zvi, A., De Los Rios, P., Dietler, G., and Goloubinoff, P. (2004). Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones. J. Biol. Chem. 279, 37298-37303.
    • (2004) J. Biol. Chem. , vol.279 , pp. 37298-37303
    • Ben-Zvi, A.1    De Los Rios, P.2    Dietler, G.3    Goloubinoff, P.4
  • 3
    • 0027484417 scopus 로고
    • Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
    • Blond-Elguindi, S., Cwirla, S.E., Dower, W.J., Lipshutz, R.J., Sprang, S.R., Sambrook, J.F., and Gething, M.J. (1993). Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75, 717-728.
    • (1993) Cell , vol.75 , pp. 717-728
    • Blond-Elguindi, S.1    Cwirla, S.E.2    Dower, W.J.3    Lipshutz, R.J.4    Sprang, S.R.5    Sambrook, J.F.6    Gething, M.J.7
  • 4
    • 0038029881 scopus 로고    scopus 로고
    • ER quality control can lead to retrograde transport from the ER lumen to the cytosol and the nucleoplasm in plants
    • Brandizzi, F., Hanton, S., DaSilva, L.L., Boevink, P., Evans, D., Oparka, K., Denecke, J., and Hawes, C. (2003). ER quality control can lead to retrograde transport from the ER lumen to the cytosol and the nucleoplasm in plants. Plant J. 34, 269-281.
    • (2003) Plant J. , vol.34 , pp. 269-281
    • Brandizzi, F.1    Hanton, S.2    DaSilva, L.L.3    Boevink, P.4    Evans, D.5    Oparka, K.6    Denecke, J.7    Hawes, C.8
  • 5
    • 0035968205 scopus 로고    scopus 로고
    • Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi
    • Caldwell, S.R., Hill, K.J., and Cooper, A.A. (2001). Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi. J. Biol. Chem. 276, 23296-23303.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23296-23303
    • Caldwell, S.R.1    Hill, K.J.2    Cooper, A.A.3
  • 6
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M.J., and Cohen, S.N. (1980). Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Biol. Biol. 138, 179-207.
    • (1980) J. Biol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 7
    • 2442582580 scopus 로고    scopus 로고
    • Degradation of mutated bovine pancreatic trypsin inhibitor in the yeast vacuole suggests post-endoplasmic reticulum protein quality control
    • Coughlan, C.M., Walker, J.L., Cochran, J.C., Wittrup, K.D., and Brodsky, J.L. (2004). Degradation of mutated bovine pancreatic trypsin inhibitor in the yeast vacuole suggests post-endoplasmic reticulum protein quality control. J. Biol. Chem. 279, 15289-15297.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15289-15297
    • Coughlan, C.M.1    Walker, J.L.2    Cochran, J.C.3    Wittrup, K.D.4    Brodsky, J.L.5
  • 9
    • 0031774263 scopus 로고    scopus 로고
    • BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress
    • Crofts, A.J., Leborgne-Castel, N., Pesca, M., Vitale, A., and Denecke, J. (1998). BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress. Plant Cell 10, 813-824.
    • (1998) Plant Cell , vol.10 , pp. 813-824
    • Crofts, A.J.1    Leborgne-Castel, N.2    Pesca, M.3    Vitale, A.4    Denecke, J.5
  • 11
    • 0029123267 scopus 로고
    • Wortmannin causes mistargeting of procathepsin D. Evidence for the involvement of a phosphatidylinositol 3-kinase in vesicular transport to lysosomes
    • Davidson, H.W. (1995). Wortmannin causes mistargeting of procathepsin D. Evidence for the involvement of a phosphatidylinositol 3-kinase in vesicular transport to lysosomes. J. Cell Biol. 130, 797-805.
    • (1995) J. Cell Biol. , vol.130 , pp. 797-805
    • Davidson, H.W.1
  • 12
    • 0024982237 scopus 로고
    • Protein secretion in plant cells can occur via a default pathway
    • Denecke, J., Botterman, J., and 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
  • 13
    • 0026523624 scopus 로고
    • Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope
    • Denecke, J., De Rycke, R., and Botterman, J. (1992). Plant and mammalian sorting signals for protein retention in the endoplasmic reticulum contain a conserved epitope. EMBO J. 11, 2345-2355.
    • (1992) EMBO J. , vol.11 , pp. 2345-2355
    • Denecke, J.1    De Rycke, R.2    Botterman, J.3
  • 14
    • 0026216562 scopus 로고
    • The tobacco luminal binding protein is encoded by a multigene family
    • Denecke, J., Goldman, M.H., Demolder, J., Seurinck, J., and Botterman, J. (1991). The tobacco luminal binding protein is encoded by a multigene family. Plant Cell 3, 1025-1035.
    • (1991) Plant Cell , vol.3 , pp. 1025-1035
    • Denecke, J.1    Goldman, M.H.2    Demolder, J.3    Seurinck, J.4    Botterman, J.5
  • 15
    • 0029447035 scopus 로고
    • The use of protoplasts to study protein synthesis and transport by the plant endomembrane system
    • Denecke, J., and Vitale, A. (1995). The use of protoplasts to study protein synthesis and transport by the plant endomembrane system. Methods Cell Biol. 50, 335-348.
    • (1995) Methods Cell Biol. , vol.50 , pp. 335-348
    • Denecke, J.1    Vitale, A.2
  • 16
    • 0035807828 scopus 로고    scopus 로고
    • Ricin A chain without its partner B chain is degraded after retrotranslocation from the endoplasmic reticulum to the cytosol in plant cells
    • Di Cola, A., Frigerio, L., Lord, J.M., Ceriotti, A., and Roberts, L.M. (2001). Ricin A chain without its partner B chain is degraded after retrotranslocation from the endoplasmic reticulum to the cytosol in plant cells. Proc. Natl. Acad. Sci. USA 98, 14726-14731.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14726-14731
    • Di Cola, A.1    Frigerio, L.2    Lord, J.M.3    Ceriotti, A.4    Roberts, L.M.5
  • 17
    • 18744402497 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation of ricin A chain has unique and plant-specific features
    • Di Cola, A., Frigerio, L., Lord, J.M., Roberts, L.M., and Ceriotti, A. (2005). Endoplasmic reticulum-associated degradation of ricin a chain has unique and plant-specific features. Plant Physiol. 137, 287-296.
    • (2005) Plant Physiol. , vol.137 , pp. 287-296
    • Di Cola, A.1    Frigerio, L.2    Lord, J.M.3    Roberts, L.M.4    Ceriotti, A.5
  • 18
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L., and Kelenius, A. (2003). Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4, 181-191.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Kelenius, A.2
  • 19
    • 0026150602 scopus 로고
    • Characterization of an immunoglobulin binding protein homolog in the maize floury-2 endosperm mutant
    • Fontes, E.B., Shank, B.B., Wrobel, R.L., Moose, S.P., O'Brian, G.R., Wurtzel, E.T., and Boston, R.S. (1991). Characterization of an immunoglobulin binding protein homolog in the maize floury-2 endosperm mutant. Plant Cell 3, 483-496.
    • (1991) Plant Cell , vol.3 , pp. 483-496
    • Fontes, E.B.1    Shank, B.B.2    Wrobel, R.L.3    Moose, S.P.4    O'Brian, G.R.5    Wurtzel, E.T.6    Boston, R.S.7
  • 20
    • 0142092348 scopus 로고    scopus 로고
    • A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP
    • Foresti, O., Frigerio, L., Holkeri, H., de Virgilio, M., Vavassori, S., and Vitale, A. (2003). A phaseolin domain involved directly in trimer assembly is a determinant for binding by the chaperone BiP. Plant Cell 15, 2464-2475.
    • (2003) Plant Cell , vol.15 , pp. 2464-2475
    • Foresti, O.1    Frigerio, L.2    Holkeri, H.3    De Virgilio, M.4    Vavassori, S.5    Vitale, A.6
  • 21
    • 0033208953 scopus 로고    scopus 로고
    • Role and regulation of the ER chaperone BiP
    • Gething, M.J. (1999). Role and regulation of the ER chaperone BiP. Semin. Cell Dev. Biol. 10, 465-472.
    • (1999) Semin. Cell Dev. Biol. , vol.10 , pp. 465-472
    • Gething, M.J.1
  • 22
    • 0022552149 scopus 로고
    • Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
    • Gething, M.J., McCammon, K., and Sambrook, J. (1986). Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport. Cell 46, 939-950.
    • (1986) Cell , vol.46 , pp. 939-950
    • Gething, M.J.1    McCammon, K.2    Sambrook, J.3
  • 23
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J., and Sambrook, J. (1992). Protein folding in the cell. Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 24
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A.L. (2003). Protein degradation and protection against misfolded or damaged proteins. Nature 426, 895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 25
    • 12444343145 scopus 로고    scopus 로고
    • Starvation triggers the delivery of the endoplasmic reticulum to the vacuole via autophagy in yeast
    • Hamasaki, M., Noda, T., Baba, M., and Ohsumi, Y. (2005). Starvation triggers the delivery of the endoplasmic reticulum to the vacuole via autophagy in yeast. Traffic 6, 56-65.
    • (2005) Traffic , vol.6 , pp. 56-65
    • Hamasaki, M.1    Noda, T.2    Baba, M.3    Ohsumi, Y.4
  • 26
    • 0031795695 scopus 로고    scopus 로고
    • Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles
    • Hara-Nishimura, I., Shimada, T., Hatano, K., Takeuchi, V., and Nishimura, M, (1998). Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles. Plant Cell 10, 825-836.
    • (1998) Plant Cell , vol.10 , pp. 825-836
    • Hara-Nishimura, I.1    Shimada, T.2    Hatano, K.3    Takeuchi, V.4    Nishimura, M.5
  • 27
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 28
    • 0029890917 scopus 로고    scopus 로고
    • Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants
    • Hendershot, L., Wei, J., Gaut, J., Melnick, J., Aviel, S., and Argon, Y. (1996). Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants. Proc. Natl. Acad. Sci. USA 93, 5269-5274.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5269-5274
    • Hendershot, L.1    Wei, J.2    Gaut, J.3    Melnick, J.4    Aviel, S.5    Argon, Y.6
  • 29
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Killer, M.M., Finger, A., Schweiger, M., and Wolf, D.H. (1996). ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Killer, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 30
    • 0032511128 scopus 로고    scopus 로고
    • Different degradation pathways for heterologous glycoproteins in yeast
    • Holkeri, H., and Makarow, M. (1998). Different degradation pathways for heterologous glycoproteins in yeast. FEBS Lett. 429, 162-166.
    • (1998) FEBS Lett. , vol.429 , pp. 162-166
    • Holkeri, H.1    Makarow, M.2
  • 31
    • 0029829005 scopus 로고    scopus 로고
    • A pathway for targeting soluble misfolded proteins to the yeast vacuole
    • Hong, E., Davidson, A.R., and Kaiser, C.A. (1996). A pathway for targeting soluble misfolded proteins to the yeast vacuole. J. Cell Biol. 135, 623-633.
    • (1996) J. Cell Biol. , vol.135 , pp. 623-633
    • Hong, E.1    Davidson, A.R.2    Kaiser, C.A.3
  • 32
    • 0024400060 scopus 로고
    • Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
    • Hurtley, S.M., Bole, D.G., Hoover-Litty, H., Helenius, A., and Copeland, C.S. (1989). Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell Biol. 108, 2117-2126.
    • (1989) J. Cell Biol. , vol.108 , pp. 2117-2126
    • Hurtley, S.M.1    Bole, D.G.2    Hoover-Litty, H.3    Helenius, A.4    Copeland, C.S.5
  • 34
    • 0032712838 scopus 로고    scopus 로고
    • Anticipating endoplasmic reticulum stress. A novel early response before pathogenesis-related gene induction
    • Jelitto-Van Dooren, E.P., Vidal, S., and Denecke, J. (1999). Anticipating endoplasmic reticulum stress. A novel early response before pathogenesis-related gene induction. Plant Cell 11, 1935-1944.
    • (1999) Plant Cell , vol.11 , pp. 1935-1944
    • Jelitto-Van Dooren, E.P.1    Vidal, S.2    Denecke, J.3
  • 35
    • 0038785977 scopus 로고    scopus 로고
    • Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae
    • Jorgensen, M.U., Emr, S.D., and Winther, J.R. (1999). Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. Eur. J. Biochem. 260, 461-469.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 461-469
    • Jorgensen, M.U.1    Emr, S.D.2    Winther, J.R.3
  • 36
    • 0029105589 scopus 로고
    • Binding-protein expression is subject to temporal, developmental and stress-induced regulation in terminally differentiated soybean organs
    • Kalinski, A., Rowley, D.L., Loer, D.S., Foley, C., Buta, G., and Herman, E.M. (1995). Binding-protein expression is subject to temporal, developmental and stress-induced regulation in terminally differentiated soybean organs. Planta 195, 611-621.
    • (1995) Planta , vol.195 , pp. 611-621
    • Kalinski, A.1    Rowley, D.L.2    Loer, D.S.3    Foley, C.4    Buta, G.5    Herman, E.M.6
  • 37
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen, B., and Braakman, I. (2004). Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell Biol. 16, 343-349.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 38
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi, Y., Segal, M., Normington, K., Gething, M.J., and Sambrook, J. (1988). The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature 332, 462-464.
    • (1988) Nature , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 42
    • 0015914077 scopus 로고
    • Streptomycin-resistant plants from callus culture of haploid tobacco
    • Maliga, P., Sz-Breznovits, A., and Marton, L. (1973). Streptomycin-resistant plants from callus culture of haploid tobacco. Nat. New Biol. 244, 29-30.
    • (1973) Nat. New Biol. , vol.244 , pp. 29-30
    • Maliga, P.1    Sz-Breznovits, A.2    Marton, L.3
  • 43
    • 0037164807 scopus 로고    scopus 로고
    • Concentrative sorting of secretory cargo proteins into COPII-coated vesicles
    • Malkus, P., Jiang, F., and Schekman, R. (2002). Concentrative sorting of secretory cargo proteins into COPII-coated vesicles. J. Cell Biol. 159, 915-921.
    • (2002) J. Cell Biol. , vol.159 , pp. 915-921
    • Malkus, P.1    Jiang, F.2    Schekman, R.3
  • 44
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
    • Matlack, K.E., Misselwitz, B., Plath, K., and Rapoport, T.A. (1999). BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97, 553-564.
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 45
    • 0042318739 scopus 로고    scopus 로고
    • Evolving questions and paradigm shifts in endoplasmic-reticulum- associated degradation (ERAD)
    • McCracken, A.A., and Brodsky, J.L. (2003). Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bioessays 25, 868-877.
    • (2003) Bioessays , vol.25 , pp. 868-877
    • McCracken, A.A.1    Brodsky, J.L.2
  • 47
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro, S., and Pelham, H.R. (1986). An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46, 291-300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.2
  • 48
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro, S., and Pelham, H.R. (1987). A C-terminal signal prevents secretion of luminal ER proteins. Cell 48, 899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 49
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige, R., and Skoog, F. (1962). A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol. Plant. 15, 473-497.
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, R.1    Skoog, F.2
  • 50
    • 0028073895 scopus 로고
    • Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies
    • Nishikawa, S., Hirata, A., and Nakano, A. (1994). Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies. Mol. Biol. Cell 5, 1129-1143.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1129-1143
    • Nishikawa, S.1    Hirata, A.2    Nakano, A.3
  • 51
    • 3142645544 scopus 로고    scopus 로고
    • Disposal of chloroplasts with abnormal function into the vacuole in Arabidopsis thaliana cotyledon cells
    • Niwa, V., Kato, T., Tabata, S., Seki, M., Kobayashi, M., Shinozaki, K., and Moriyasu, Y. (2004). Disposal of chloroplasts with abnormal function into the vacuole in Arabidopsis thaliana cotyledon cells. Protoplasma 223, 229-232.
    • (2004) Protoplasma , vol.223 , pp. 229-232
    • Niwa, V.1    Kato, T.2    Tabata, S.3    Seki, M.4    Kobayashi, M.5    Shinozaki, K.6    Moriyasu, Y.7
  • 52
    • 18744378812 scopus 로고    scopus 로고
    • ER-resident chaperone interactions with recombinant antibodies in transgenic plants
    • Nuttall, J., Vine, N., Hadlington, J.L., Drake, P., Frigerio, L., and Ma, J.K. (2002). ER-resident chaperone interactions with recombinant antibodies in transgenic plants. Eur. J. Biochem. 269, 6042-6051.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 6042-6051
    • Nuttall, J.1    Vine, N.2    Hadlington, J.L.3    Drake, P.4    Frigerio, L.5    Ma, J.K.6
  • 55
    • 0036914505 scopus 로고    scopus 로고
    • Protein-protein interactions in the secretory pathway, a growing demand for experimental approaches in vivo
    • Pimpl, P., and Denecke, J. (2002). Protein-protein interactions in the secretory pathway, a growing demand for experimental approaches in vivo. Plant Mol. Biol. 50, 887-902.
    • (2002) Plant Mol. Biol. , vol.50 , pp. 887-902
    • Pimpl, P.1    Denecke, J.2
  • 56
    • 0038366776 scopus 로고    scopus 로고
    • The GTPase ARFIp controls the sequence-specific vacuolar sorting route to the lytic vacuole
    • Pimpl, P., Hanton, S.L., Taylor, J.P., Pinto-DaSilva, L.L., and Denecke, J. (2003). The GTPase ARFIp controls the sequence-specific vacuolar sorting route to the lytic vacuole. Plant Cell 15, 1242-1256.
    • (2003) Plant Cell , vol.15 , pp. 1242-1256
    • Pimpl, P.1    Hanton, S.L.2    Taylor, J.P.3    Pinto-DaSilva, L.L.4    Denecke, J.5
  • 58
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper, R.K., Bohmler, S., Bordallo, J., Sommer, T., and Wolf, D.H. (1997). Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388, 891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 59
    • 22444438991 scopus 로고    scopus 로고
    • BiP and zein binding domains within the delta zein protein
    • Randall, J.J., Sutton, D.W., Hanson, S.F., and Kemp, J.D. (2005). BiP and zein binding domains within the delta zein protein. Planta 221, 656-666.
    • (2005) Planta , vol.221 , pp. 656-666
    • Randall, J.J.1    Sutton, D.W.2    Hanson, S.F.3    Kemp, J.D.4
  • 60
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: Coping with stress
    • Rutkowski, D.T., and Kaufman, R.J. (2004). A trip to the ER: Coping with stress. Trends Cell Biol. 14, 20-28.
    • (2004) Trends Cell Biol. , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 62
    • 12344334864 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation: Exceptions to the rule
    • Schmitz, A., and Herzog, V. (2004). Endoplasmic reticulum-associated degradation: Exceptions to the rule. Eur. J. Cell Biol. 83, 501-509.
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 501-509
    • Schmitz, A.1    Herzog, V.2
  • 63
    • 13244275069 scopus 로고    scopus 로고
    • Recycle your receptors with retromer
    • Seaman, M.N. (2005). Recycle your receptors with retromer. Trends Cell Biol. 15, 68-75.
    • (2005) Trends Cell Biol. , vol.15 , pp. 68-75
    • Seaman, M.N.1
  • 64
    • 0025362445 scopus 로고
    • ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway
    • Semenza, J.C., Kardwick, K.G., Dean, N., and Pelham, H.R. (1990). ERD2, a yeast gene required for the receptor-mediated retrieval of luminal ER proteins from the secretory pathway. Cell 61, 1349-1357.
    • (1990) Cell , vol.61 , pp. 1349-1357
    • Semenza, J.C.1    Kardwick, K.G.2    Dean, N.3    Pelham, H.R.4
  • 65
    • 0037769904 scopus 로고    scopus 로고
    • Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathways
    • Spear, E.D., and Ng, D.T. (2003). Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathways. Mol. Biol. Cell 14, 2756-2767.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2756-2767
    • Spear, E.D.1    Ng, D.T.2
  • 66
    • 0033838323 scopus 로고    scopus 로고
    • A dominant negative mutant of Sari GTPase inhibits protein transport from the endoplasmic reticutum to the Golgi apparatus in tobacco and Arabidopsis cultured cells
    • Takeuchi, M., Ueda, T., Safo, K., Abe, H., Nagata, T., and Nakano, A. (2000). A dominant negative mutant of Sari GTPase inhibits protein transport from the endoplasmic reticutum to the Golgi apparatus in tobacco and Arabidopsis cultured cells. Plant J. 23, 517-525.
    • (2000) Plant J. , vol.23 , pp. 517-525
    • Takeuchi, M.1    Ueda, T.2    Safo, K.3    Abe, H.4    Nagata, T.5    Nakano, A.6
  • 67
    • 3843103539 scopus 로고    scopus 로고
    • Endoplasmic reticulum-resident proteins are constitutively transported to vacuoles for degradation
    • Tamura, K., Vamada, K., Shimada, T., and Hara-Nishimura, I. (2004). Endoplasmic reticulum-resident proteins are constitutively transported to vacuoles for degradation. Plant J. 39, 393-402.
    • (2004) Plant J. , vol.39 , pp. 393-402
    • Tamura, K.1    Vamada, K.2    Shimada, T.3    Hara-Nishimura, I.4
  • 68
    • 0035985150 scopus 로고    scopus 로고
    • ER-golgi traffic is a prerequisite for efficient ER degradation
    • Taxis, C., Vogel, F., and Wolf, D.H. (2002). ER-golgi traffic is a prerequisite for efficient ER degradation. Mol. Biol. Cell 13, 1806-1818.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1806-1818
    • Taxis, C.1    Vogel, F.2    Wolf, D.H.3
  • 69
    • 0031656514 scopus 로고    scopus 로고
    • Characterization of deletion mutations in the carboxy-terminal peptide-binding domain of the Kar2 protein in Sacchammyces cerevisiae
    • Tokunaga, M., Kato, S., Kawamura-Watabe, A., Tanaka, R., and Tokunaga, H. (1998). Characterization of deletion mutations in the carboxy-terminal peptide-binding domain of the Kar2 protein in Sacchammyces cerevisiae. Yeast 14, 1285-1295.
    • (1998) Yeast , vol.14 , pp. 1285-1295
    • Tokunaga, M.1    Kato, S.2    Kawamura-Watabe, A.3    Tanaka, R.4    Tokunaga, H.5
  • 70
    • 0034808250 scopus 로고    scopus 로고
    • A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum
    • Törmäkangas, K., Hadlington, J.L., Pimpl, P., Hillmer, S., Brandizzi, F., Teeri, T.H., and Denecke, J. (2001). A vacuolar sorting domain may also influence the way in which proteins leave the endoplasmic reticulum. Plant Cell 13, 2021-2032.
    • (2001) Plant Cell , vol.13 , pp. 2021-2032
    • Törmäkangas, K.1    Hadlington, J.L.2    Pimpl, P.3    Hillmer, S.4    Brandizzi, F.5    Teeri, T.H.6    Denecke, J.7
  • 71
    • 0028031043 scopus 로고
    • Retrieval of HDEL proteins is required for growth of yeast cells
    • Townsley, F.M., Frigerio, G., and Pelham, U.R. (1994). Retrieval of HDEL proteins is required for growth of yeast cells. J. Cell Biol. 127, 21-28.
    • (1994) J. Cell Biol. , vol.127 , pp. 21-28
    • Townsley, F.M.1    Frigerio, G.2    Pelham, U.R.3
  • 72
    • 0034614933 scopus 로고    scopus 로고
    • Mass transport of proform of a KDEL-tailed cysteine proteinase (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds
    • Toyooka, K., Okamoto, T., and Minamikawa, T. (2000). Mass transport of proform of a KDEL-tailed cysteine proteinase (SH-EP) to protein storage vacuoles by endoplasmic reticulum-derived vesicle is involved in protein mobilization in germinating seeds. J. Cell Biol. 148, 453-463.
    • (2000) J. Cell Biol. , vol.148 , pp. 453-463
    • Toyooka, K.1    Okamoto, T.2    Minamikawa, T.3
  • 73
    • 1542370795 scopus 로고    scopus 로고
    • Identification of multivesicular bodies as prevacuolar compartments in Nicotiana tabacum BY-2 cells
    • Tse, Y.C., Mo, B., Hillmer, S., Zhao, M., Lo, S.W., Robinson, D.G., and Jiang, L. (2004). Identification of multivesicular bodies as prevacuolar compartments in Nicotiana tabacum BY-2 cells. Plant Cell 16, 672-693.
    • (2004) Plant Cell , vol.16 , pp. 672-693
    • Tse, Y.C.1    Mo, B.2    Hillmer, S.3    Zhao, M.4    Lo, S.W.5    Robinson, D.G.6    Jiang, L.7
  • 74
    • 0035851911 scopus 로고    scopus 로고
    • Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding
    • Vashist, S., Kim, W., Belden, W.J., Spear, E.D., Barlowe, C., and Ng, D.T. (2001). Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding. J. Cell Biol. 155, 355-368.
    • (2001) J. Cell Biol. , vol.155 , pp. 355-368
    • Vashist, S.1    Kim, W.2    Belden, W.J.3    Spear, E.D.4    Barlowe, C.5    Ng, D.T.6
  • 75
    • 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
  • 76
    • 0032725633 scopus 로고    scopus 로고
    • The endoplasmic reticulum-gateway of the secretory pathway
    • Vitale, A., and Denecke, J. (1999). The endoplasmic reticulum-gateway of the secretory pathway. Plant Cell 11, 615-628.
    • (1999) Plant Cell , vol.11 , pp. 615-628
    • Vitale, A.1    Denecke, J.2
  • 77
    • 18644369120 scopus 로고    scopus 로고
    • Induction of protein secretory pathway is required for systemic acquired resistance
    • Wang, D., Weaver, N.D., Kesarwani, M., and Dong, X. (2005). Induction of protein secretory pathway is required for systemic acquired resistance. Science 308, 1036-1040.
    • (2005) Science , vol.308 , pp. 1036-1040
    • Wang, D.1    Weaver, N.D.2    Kesarwani, M.3    Dong, X.4
  • 78
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C.L., Omura, S., and Kopito, R.R. (1995). Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 79
    • 0035875665 scopus 로고    scopus 로고
    • The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum
    • Yamamoto, K., Fujii, R., Toyofuku, Y., Saito, T., Koseki, H., Hsu, V.W., and Aoe, T. (2001). The KDEL receptor mediates a retrieval mechanism that contributes to quality control at the endoplasmic reticulum. EMBO J. 20, 3082-3091.
    • (2001) EMBO J. , vol.20 , pp. 3082-3091
    • Yamamoto, K.1    Fujii, R.2    Toyofuku, Y.3    Saito, T.4    Koseki, H.5    Hsu, V.W.6    Aoe, T.7
  • 80
    • 0347626252 scopus 로고    scopus 로고
    • Autophagy: A regulated bulk degradation process inside cells
    • Yoshimori, T. (2004). Autophagy: A regulated bulk degradation process inside cells. Biochem. Biophys. Res. Commun. 313, 453-458.
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 453-458
    • Yoshimori, T.1
  • 81
    • 0035844876 scopus 로고    scopus 로고
    • Intracellular retention of newly synthesized insulin in yeast is caused by endoproteolytic processing in the Golgi complex
    • Zhang, B., Chang, A., Kjeldsen, T.B., and Arvan, P. (2001). Intracellular retention of newly synthesized insulin in yeast is caused by endoproteolytic processing in the Golgi complex. J. Cell Biol. 153, 1187-1198.
    • (2001) J. Cell Biol. , vol.153 , pp. 1187-1198
    • Zhang, B.1    Chang, A.2    Kjeldsen, T.B.3    Arvan, P.4
  • 82
    • 2942755868 scopus 로고    scopus 로고
    • Signaling the unfolded protein response from the endoplasmic reticulum
    • Zhang, K., and Kaufman, R.J. (2004). Signaling the unfolded protein response from the endoplasmic reticulum. J. Biol. Chem. 279, 25935-25938.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25935-25938
    • Zhang, K.1    Kaufman, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.