메뉴 건너뛰기




Volumn 20, Issue 12, 2008, Pages 3418-3429

Multiple mechanism-mediated retention of a defective brassinosteroid receptor in the endoplasmic reticulum of Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; MAMMALIA;

EID: 62549084306     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.108.061879     Document Type: Article
Times cited : (155)

References (73)
  • 1
    • 0025146994 scopus 로고
    • Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents
    • Alberini, C.M., Bet, P., Milstein, C., and Sitia, R. (1990). Secretion of immunoglobulin M assembly intermediates in the presence of reducing agents. Nature 347: 485-487.
    • (1990) Nature , vol.347 , pp. 485-487
    • Alberini, C.M.1    Bet, P.2    Milstein, C.3    Sitia, R.4
  • 2
    • 0042768158 scopus 로고    scopus 로고
    • Genome-wide insertional mutagenesis of Arabidopsis thaliana
    • Alonso, J.M., et al. (2003). Genome-wide insertional mutagenesis of Arabidopsis thaliana. Science 301: 653-657.
    • (2003) Science , vol.301 , pp. 653-657
    • Alonso, J.M.1
  • 4
    • 34948899397 scopus 로고    scopus 로고
    • Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis
    • Anelli, T., Ceppi, S., Bergamelli, L., Cortini, M., Masciarelli, S., Valetti, C., and Sitia, R. (2007). Sequential steps and checkpoints in the early exocytic compartment during secretory IgM biogenesis. EMBO J. 26: 4177-4188.
    • (2007) EMBO J , vol.26 , pp. 4177-4188
    • Anelli, T.1    Ceppi, S.2    Bergamelli, L.3    Cortini, M.4    Masciarelli, S.5    Valetti, C.6    Sitia, R.7
  • 6
    • 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
  • 8
    • 17144474857 scopus 로고
    • Genomic sequence of a calnexin homolog from Arabidopsis thaliana
    • Boyce, J.M., Coates, D., Fricker, M.D., and Evans, D.E. (1994). Genomic sequence of a calnexin homolog from Arabidopsis thaliana. Plant Physiol. 106: 1691.
    • (1994) Plant Physiol , vol.106 , pp. 1691
    • Boyce, J.M.1    Coates, D.2    Fricker, M.D.3    Evans, D.E.4
  • 9
    • 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
  • 10
    • 36248973177 scopus 로고    scopus 로고
    • The activities and function of molecular chaperones in the endoplasmic reticulum
    • Buck, T.M., Wright, C.M., and Brodsky, J.L. (2007). The activities and function of molecular chaperones in the endoplasmic reticulum. Semin. Cell Dev. Biol. 18: 751-761.
    • (2007) Semin. Cell Dev. Biol , vol.18 , pp. 751-761
    • Buck, T.M.1    Wright, C.M.2    Brodsky, J.L.3
  • 11
    • 0036949462 scopus 로고    scopus 로고
    • The cellulose-deficient Arabidopsis mutant rsw3 is defective in a gene encoding a putative glucosidase II, an enzyme processing N-glycans during ER quality control
    • Burn, J.E., Hurley, U.A., Birch, R.J., Arioli, T., Cork, A., and Williamson, R.E. (2002). The cellulose-deficient Arabidopsis mutant rsw3 is defective in a gene encoding a putative glucosidase II, an enzyme processing N-glycans during ER quality control. Plant J. 32: 949-960.
    • (2002) Plant J , vol.32 , pp. 949-960
    • Burn, J.E.1    Hurley, U.A.2    Birch, R.J.3    Arioli, T.4    Cork, A.5    Williamson, R.E.6
  • 12
    • 36249022072 scopus 로고    scopus 로고
    • How sugars convey information on protein conformation in the endoplasmic reticulum
    • Caramelo, J.J., and Parodi, A.J. (2007). How sugars convey information on protein conformation in the endoplasmic reticulum. Semin. Cell Dev. Biol. 18: 732-742.
    • (2007) Semin. Cell Dev. Biol , vol.18 , pp. 732-742
    • Caramelo, J.J.1    Parodi, A.J.2
  • 13
    • 34250669555 scopus 로고    scopus 로고
    • PSITE vectors for stable integration or transient expression of autofluorescent protein fusions in plants: Probing Nicotiana benthamiana-virus interactions
    • Chakrabarty, R., Banerjee, R., Chung, S.M., Farman, M., Citovsky, V., Hogenhout, S.A., Tzfira, T., and Goodin, M. (2007). PSITE vectors for stable integration or transient expression of autofluorescent protein fusions in plants: Probing Nicotiana benthamiana-virus interactions. Mol. Plant Microbe Interact. 20: 740-750.
    • (2007) Mol. Plant Microbe Interact , vol.20 , pp. 740-750
    • Chakrabarty, R.1    Banerjee, R.2    Chung, S.M.3    Farman, M.4    Citovsky, V.5    Hogenhout, S.A.6    Tzfira, T.7    Goodin, M.8
  • 14
    • 23044445303 scopus 로고    scopus 로고
    • Crystal structure of human toll-like receptor 3 (TLR3) ectodomain
    • Choe, J., Kelker, M.S., and Wilson, I.A. (2005). Crystal structure of human toll-like receptor 3 (TLR3) ectodomain. Science 309: 581-585.
    • (2005) Science , vol.309 , pp. 581-585
    • Choe, J.1    Kelker, M.S.2    Wilson, I.A.3
  • 15
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S.J., and Bent, A.F. (1998). Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16: 735-743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 16
    • 0030194927 scopus 로고    scopus 로고
    • A brassinosteroid-insensitive mutant in Arabidopsis thaliana exhibits multiple defects in growth and development
    • Clouse, S.D., Langford, M., and McMorris, T.C. (1996). A brassinosteroid-insensitive mutant in Arabidopsis thaliana exhibits multiple defects in growth and development. Plant Physiol. 111: 671-678.
    • (1996) Plant Physiol , vol.111 , pp. 671-678
    • Clouse, S.D.1    Langford, M.2    McMorris, T.C.3
  • 17
    • 0035816569 scopus 로고    scopus 로고
    • The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo
    • Danilczyk, U.G., and Williams, D.B. (2001). The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo. J. Biol. Chem. 276: 25532-25540.
    • (2001) J. Biol. Chem , vol.276 , pp. 25532-25540
    • Danilczyk, U.G.1    Williams, D.B.2
  • 18
    • 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
  • 19
    • 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
  • 21
    • 0042262430 scopus 로고    scopus 로고
    • Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins
    • Dixon, D.P., Van Lith, M., Edwards, R., and Benham, A. (2003). Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins. Antioxid. Redox Signal. 5: 389-396.
    • (2003) Antioxid. Redox Signal , vol.5 , pp. 389-396
    • Dixon, D.P.1    Van Lith, M.2    Edwards, R.3    Benham, A.4
  • 22
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L., and Helenius, 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    Helenius, A.2
  • 23
    • 0033612143 scopus 로고    scopus 로고
    • PKS1, a substrate phosphorylated by phytochrome that modulates light signaling in Arabidopsis
    • Fankhauser, C., Yeh, K.C., Lagarias, J.C., Zhang, H., Elich, T.D., and Chory, J. (1999). PKS1, a substrate phosphorylated by phytochrome that modulates light signaling in Arabidopsis. Science 284: 1539-1541.
    • (1999) Science , vol.284 , pp. 1539-1541
    • Fankhauser, C.1    Yeh, K.C.2    Lagarias, J.C.3    Zhang, H.4    Elich, T.D.5    Chory, J.6
  • 24
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, G.C., Pohl, J., Flocco, M.T., and Rothman, J.E. (1991). Peptide-binding specificity of the molecular chaperone BiP. Nature 353: 726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 25
    • 0033836946 scopus 로고    scopus 로고
    • Brassinosteroid-insensitive-1 is a ubiquitously expressed leucine-rich repeat receptor serine/threonine kinase
    • Friedrichsen, D.M., Joazeiro, C.A., Li, J., Hunter, T., and Chory, J. (2000). Brassinosteroid-insensitive-1 is a ubiquitously expressed leucine-rich repeat receptor serine/threonine kinase. Plant Physiol. 123: 1247-1256.
    • (2000) Plant Physiol , vol.123 , pp. 1247-1256
    • Friedrichsen, D.M.1    Joazeiro, C.A.2    Li, J.3    Hunter, T.4    Chory, J.5
  • 26
    • 34547395050 scopus 로고    scopus 로고
    • An essential role for 14-3-3 proteins in brassinosteroid signal transduction in Arabidopsis
    • Gampala, S.S., et al. (2007). An essential role for 14-3-3 proteins in brassinosteroid signal transduction in Arabidopsis. Dev. Cell 13: 177-189.
    • (2007) Dev. Cell , vol.13 , pp. 177-189
    • Gampala, S.S.1
  • 27
    • 0037128937 scopus 로고    scopus 로고
    • Alpha-glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis
    • Gillmor, C.S., Poindexter, P., Lorieau, J., Palcic, M.M., and Somerville, C. (2002). Alpha-glucosidase I is required for cellulose biosynthesis and morphogenesis in Arabidopsis. J. Cell Biol. 156: 1003-1013.
    • (2002) J. Cell Biol , vol.156 , pp. 1003-1013
    • Gillmor, C.S.1    Poindexter, P.2    Lorieau, J.3    Palcic, M.M.4    Somerville, C.5
  • 28
    • 0027012738 scopus 로고
    • A versatile binary vector system with a T-DNA organisational structure conducive to efficient integration of cloned DNA into the plant genome
    • Gleave, A.P. (1992). A versatile binary vector system with a T-DNA organisational structure conducive to efficient integration of cloned DNA into the plant genome. Plant Mol. Biol. 20: 1203-1207.
    • (1992) Plant Mol. Biol , vol.20 , pp. 1203-1207
    • Gleave, A.P.1
  • 29
    • 0037162537 scopus 로고    scopus 로고
    • The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive regulator of the brassinosteroid signaling pathway in Arabidopsis
    • He, J.X., Gendron, J.M., Yang, Y., Li, J., and Wang, Z.Y. (2002). The GSK3-like kinase BIN2 phosphorylates and destabilizes BZR1, a positive regulator of the brassinosteroid signaling pathway in Arabidopsis. Proc. Natl. Acad. Sci. USA 99: 10185-10190.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10185-10190
    • He, J.X.1    Gendron, J.M.2    Yang, Y.3    Li, J.4    Wang, Z.Y.5
  • 30
    • 19044379862 scopus 로고    scopus 로고
    • Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins
    • Houston, N.L., Fan, C., Xiang, J.Q., Schulze, J.M., Jung, R., and Boston, R.S. (2005). Phylogenetic analyses identify 10 classes of the protein disulfide isomerase family in plants, including single-domain protein disulfide isomerase-related proteins. Plant Physiol. 137: 762-778.
    • (2005) Plant Physiol , vol.137 , pp. 762-778
    • Houston, N.L.1    Fan, C.2    Xiang, J.Q.3    Schulze, J.M.4    Jung, R.5    Boston, R.S.6
  • 31
    • 0027415665 scopus 로고
    • Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein
    • Huang, L., Franklin, A.E., and Hoffman, N.E. (1993). Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein. J. Biol. Chem. 268: 6560-6566.
    • (1993) J. Biol. Chem , vol.268 , pp. 6560-6566
    • Huang, L.1    Franklin, A.E.2    Hoffman, N.E.3
  • 32
    • 34250346376 scopus 로고    scopus 로고
    • Allele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality control
    • Jin, H., Yan, Z., Nam, K.H., and Li, J. (2007). Allele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality control. Mol. Cell 26: 821-830.
    • (2007) Mol. Cell , vol.26 , pp. 821-830
    • Jin, H.1    Yan, Z.2    Nam, K.H.3    Li, J.4
  • 33
    • 12744273399 scopus 로고    scopus 로고
    • Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1
    • Kinoshita, T., Cano-Delgado, A., Seto, H., Hiranuma, S., Fujioka, S., Yoshida, S., and Chory, J. (2005). Binding of brassinosteroids to the extracellular domain of plant receptor kinase BRI1. Nature 433: 167-171.
    • (2005) Nature , vol.433 , pp. 167-171
    • Kinoshita, T.1    Cano-Delgado, A.2    Seto, H.3    Hiranuma, S.4    Fujioka, S.5    Yoshida, S.6    Chory, J.7
  • 34
    • 27244433760 scopus 로고    scopus 로고
    • Identification and characterization of endoplasmic reticulum-associated degradation proteins differentially affected by endoplasmic reticulum stress
    • Kirst, M.E., Meyer, D.J., Gibbon, B.C., Jung, R., and Boston, R.S. (2005). Identification and characterization of endoplasmic reticulum-associated degradation proteins differentially affected by endoplasmic reticulum stress. Plant Physiol. 138: 218-231.
    • (2005) Plant Physiol , vol.138 , pp. 218-231
    • Kirst, M.E.1    Meyer, D.J.2    Gibbon, B.C.3    Jung, R.4    Boston, R.S.5
  • 35
    • 0028928021 scopus 로고
    • Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
    • Knittler, M.R., Dirks, S., and Haas, I.G. (1995). Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 92: 1764-1768.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1764-1768
    • Knittler, M.R.1    Dirks, S.2    Haas, I.G.3
  • 36
    • 33745218268 scopus 로고    scopus 로고
    • In vitro characterization of the cysteinerich capping domains in a plant leucine rich repeat protein
    • Kolade, O.O., Bamford, V.A., Ancillo Anton, G., Jones, J.D., Vera, P., and Hemmings, A.M. (2006). In vitro characterization of the cysteinerich capping domains in a plant leucine rich repeat protein. Biochim. Biophys. Acta 1764: 1043-1053.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1043-1053
    • Kolade, O.O.1    Bamford, V.A.2    Ancillo Anton, G.3    Jones, J.D.4    Vera, P.5    Hemmings, A.M.6
  • 37
    • 33745252002 scopus 로고    scopus 로고
    • Transient expression assay by agroinfiltration of leaves
    • Lee, M.W., and Yang, Y. (2006). Transient expression assay by agroinfiltration of leaves. Methods Mol. Biol. 323: 225-229.
    • (2006) Methods Mol. Biol , vol.323 , pp. 225-229
    • Lee, M.W.1    Yang, Y.2
  • 38
    • 0030866902 scopus 로고    scopus 로고
    • A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction
    • Li, J., and Chory, J. (1997). A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction. Cell 90: 929-938.
    • (1997) Cell , vol.90 , pp. 929-938
    • Li, J.1    Chory, J.2
  • 39
    • 0037083609 scopus 로고    scopus 로고
    • Regulation of brassinosteroid signaling by a GSK3/SHAGGY-like kinase
    • Li, J., and Nam, K.H. (2002). Regulation of brassinosteroid signaling by a GSK3/SHAGGY-like kinase. Science 295: 1299-1301.
    • (2002) Science , vol.295 , pp. 1299-1301
    • Li, J.1    Nam, K.H.2
  • 40
    • 0034835137 scopus 로고    scopus 로고
    • BIN2, a new brassinosteroid-insensitive locus in Arabidopsis
    • Li, J., Nam, K.H., Vafeados, D., and Chory, J. (2001). BIN2, a new brassinosteroid-insensitive locus in Arabidopsis. Plant Physiol. 127: 14-22.
    • (2001) Plant Physiol , vol.127 , pp. 14-22
    • Li, J.1    Nam, K.H.2    Vafeados, D.3    Chory, J.4
  • 41
    • 0037178776 scopus 로고    scopus 로고
    • BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling
    • Li, J., Wen, J., Lease, K.A., Doke, J.T., Tax, F.E., and Walker, J.C. (2002). BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling. Cell 110: 213-222.
    • (2002) Cell , vol.110 , pp. 213-222
    • Li, J.1    Wen, J.2    Lease, K.A.3    Doke, J.T.4    Tax, F.E.5    Walker, J.C.6
  • 42
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP
    • McCracken, A.A., and Brodsky, J.L. (1996). Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP. J. Cell Biol. 132: 291-298.
    • (1996) J. Cell Biol , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 43
    • 1542373671 scopus 로고    scopus 로고
    • Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis
    • Mora-Garcia, S., Vert, G., Yin, Y., Cano-Delgado, A., Cheong, H., and Chory, J. (2004). Nuclear protein phosphatases with Kelch-repeat domains modulate the response to brassinosteroids in Arabidopsis. Genes Dev. 18: 448-460.
    • (2004) Genes Dev , vol.18 , pp. 448-460
    • Mora-Garcia, S.1    Vert, G.2    Yin, Y.3    Cano-Delgado, A.4    Cheong, H.5    Chory, J.6
  • 45
    • 0037178782 scopus 로고    scopus 로고
    • BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling
    • Nam, K.H., and Li, J. (2002). BRI1/BAK1, a receptor kinase pair mediating brassinosteroid signaling. Cell 110: 203-212.
    • (2002) Cell , vol.110 , pp. 203-212
    • Nam, K.H.1    Li, J.2
  • 47
    • 0034657712 scopus 로고    scopus 로고
    • Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation
    • Parodi, A.J. (2000). Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation. Biochem. J. 348: 1-13.
    • (2000) Biochem. J , vol.348 , pp. 1-13
    • Parodi, A.J.1
  • 49
    • 0344961215 scopus 로고    scopus 로고
    • Phylogenetic analyses and expression studies reveal two distinct groups of calreticulin isoforms in higher plants
    • Persson, S., Rosenquist, M., Svensson, K., Galvao, R., Boss, W.F., and Sommarin, M. (2003). Phylogenetic analyses and expression studies reveal two distinct groups of calreticulin isoforms in higher plants. Plant Physiol. 133: 1385-1396.
    • (2003) Plant Physiol , vol.133 , pp. 1385-1396
    • Persson, S.1    Rosenquist, M.2    Svensson, K.3    Galvao, R.4    Boss, W.F.5    Sommarin, M.6
  • 50
    • 33645737420 scopus 로고    scopus 로고
    • Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway
    • Pimpl, P., Taylor, J.P., Snowden, C., Hillmer, S., Robinson, D.G., and Denecke, J. (2006). Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway. Plant Cell 18: 198-211.
    • (2006) Plant Cell , vol.18 , pp. 198-211
    • Pimpl, P.1    Taylor, J.P.2    Snowden, C.3    Hillmer, S.4    Robinson, D.G.5    Denecke, J.6
  • 51
    • 0029944851 scopus 로고    scopus 로고
    • Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains
    • Reddy, P., Sparvoli, A., Fagioli, C., Fassina, G., and Sitia, R. (1996). Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains. EMBO J. 15: 2077-2085.
    • (1996) EMBO J , vol.15 , pp. 2077-2085
    • Reddy, P.1    Sparvoli, A.2    Fagioli, C.3    Fassina, G.4    Sitia, R.5
  • 52
    • 24944446266 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation
    • Romisch, K. (2005). Endoplasmic reticulum-associated degradation. Annu. Rev. Cell Dev. Biol. 21: 435-456.
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 435-456
    • Romisch, K.1
  • 53
    • 35748933556 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of BZR1 mediated by phosphorylation is essential in Arabidopsis brassinosteroid signaling
    • Ryu, H., Kim, K., Cho, H., Park, J., Choe, S., and Hwang, I. (2007). Nucleocytoplasmic shuttling of BZR1 mediated by phosphorylation is essential in Arabidopsis brassinosteroid signaling. Plant Cell 19: 2749-2762.
    • (2007) Plant Cell , vol.19 , pp. 2749-2762
    • Ryu, H.1    Kim, K.2    Cho, H.3    Park, J.4    Choe, S.5    Hwang, I.6
  • 54
    • 0022368666 scopus 로고
    • Castanospermine inhibits glucosidase I and glycoprotein secretion in human hepatoma cells
    • Sasak, V.W., Ordovas, J.M., Elbein, A.D., and Berninger, R.W. (1985). Castanospermine inhibits glucosidase I and glycoprotein secretion in human hepatoma cells. Biochem. J. 232: 759-766.
    • (1985) Biochem. J , vol.232 , pp. 759-766
    • Sasak, V.W.1    Ordovas, J.M.2    Elbein, A.D.3    Berninger, R.W.4
  • 55
    • 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
  • 56
    • 0032912589 scopus 로고    scopus 로고
    • Structure and function of the CFTR chloride channel
    • Sheppard, D.N., and Welsh, M.J. (1999). Structure and function of the CFTR chloride channel. Physiol. Rev. 79: S23-S45.
    • (1999) Physiol. Rev , vol.79
    • Sheppard, D.N.1    Welsh, M.J.2
  • 57
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia, R., and Braakman, I. (2003). Quality control in the endoplasmic reticulum protein factory. Nature 426: 891-894.
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 58
    • 0025230696 scopus 로고
    • Developmental regulation of IgM secretion: The role of the carboxy-terminal cysteine
    • Sitia, R., Neuberger, M., Alberini, C., Bet, P., Fra, A., Valetti, C., Williams, G., and Milstein, C. (1990). Developmental regulation of IgM secretion: The role of the carboxy-terminal cysteine. Cell 60: 781-790.
    • (1990) Cell , vol.60 , pp. 781-790
    • Sitia, R.1    Neuberger, M.2    Alberini, C.3    Bet, P.4    Fra, A.5    Valetti, C.6    Williams, G.7    Milstein, C.8
  • 59
    • 0034978496 scopus 로고    scopus 로고
    • Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family
    • Sung, D.Y., Vierling, E., and Guy, C.L. (2001). Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family. Plant Physiol. 126: 789-800.
    • (2001) Plant Physiol , vol.126 , pp. 789-800
    • Sung, D.Y.1    Vierling, E.2    Guy, C.L.3
  • 60
    • 3843103539 scopus 로고    scopus 로고
    • Endoplasmic reticulum-resident proteins are constitutively transported to vacuoles for degradation
    • Tamura, K., Yamada, 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    Yamada, K.2    Shimada, T.3    Hara-Nishimura, I.4
  • 61
    • 0034731340 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER)-associated degradation of misfolded N-linked glycoproteins is suppressed upon inhibition of ER mannosidase I
    • Tokunaga, F., Brostrom, C., Koide, T., and Arvan, P. (2000). Endoplasmic reticulum (ER)-associated degradation of misfolded N-linked glycoproteins is suppressed upon inhibition of ER mannosidase I. J. Biol. Chem. 275: 40757-40764.
    • (2000) J. Biol. Chem , vol.275 , pp. 40757-40764
    • Tokunaga, F.1    Brostrom, C.2    Koide, T.3    Arvan, P.4
  • 63
    • 33646908809 scopus 로고    scopus 로고
    • Downstream nuclear events in brassinosteroid signalling
    • Vert, G., and Chory, J. (2006). Downstream nuclear events in brassinosteroid signalling. Nature 441: 96-100.
    • (2006) Nature , vol.441 , pp. 96-100
    • Vert, G.1    Chory, J.2
  • 65
    • 33748040449 scopus 로고    scopus 로고
    • Brassinosteroids regulate dissociation of BKI1, a negative regulator of BRI1 signaling, from the plasma membrane
    • Wang, X., and Chory, J. (2006). Brassinosteroids regulate dissociation of BKI1, a negative regulator of BRI1 signaling, from the plasma membrane. Science 313: 1118-1122.
    • (2006) Science , vol.313 , pp. 1118-1122
    • Wang, X.1    Chory, J.2
  • 66
    • 23944457745 scopus 로고    scopus 로고
    • Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase
    • Wang, X., Goshe, M.B., Soderblom, E.J., Phinney, B.S., Kuchar, J.A., Li, J., Asami, T., Yoshida, S., Huber, S.C., and Clouse, S.D. (2005). Identification and functional analysis of in vivo phosphorylation sites of the Arabidopsis BRASSINOSTEROID-INSENSITIVE1 receptor kinase. Plant Cell 17: 1685-1703.
    • (2005) Plant Cell , vol.17 , pp. 1685-1703
    • Wang, X.1    Goshe, M.B.2    Soderblom, E.J.3    Phinney, B.S.4    Kuchar, J.A.5    Li, J.6    Asami, T.7    Yoshida, S.8    Huber, S.C.9    Clouse, S.D.10
  • 68
    • 34248197560 scopus 로고    scopus 로고
    • Secretion of the adipocyte-specific secretory protein adiponectin critically depends on thiol-mediated protein retention
    • Wang, Z.V., Schraw, T.D., Kim, J.Y., Khan, T., Rajala, M.W., Follenzi, A., and Scherer, P.E. (2007). Secretion of the adipocyte-specific secretory protein adiponectin critically depends on thiol-mediated protein retention. Mol. Cell. Biol. 27: 3716-3731.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 3716-3731
    • Wang, Z.V.1    Schraw, T.D.2    Kim, J.Y.3    Khan, T.4    Rajala, M.W.5    Follenzi, A.6    Scherer, P.E.7
  • 69
    • 0035869056 scopus 로고    scopus 로고
    • BRI1 is a critical component of a plasma-membrane receptor for plant steroids
    • Wang, Z.Y., Seto, H., Fujioka, S., Yoshida, S., and Chory, J. (2001). BRI1 is a critical component of a plasma-membrane receptor for plant steroids. Nature 410: 380-383.
    • (2001) Nature , vol.410 , pp. 380-383
    • Wang, Z.Y.1    Seto, H.2    Fujioka, S.3    Yoshida, S.4    Chory, J.5
  • 70
    • 0034800385 scopus 로고    scopus 로고
    • Construct design for efficient, effective and high-throughput gene silencing in plants
    • Wesley, S.V., et al. (2001). Construct design for efficient, effective and high-throughput gene silencing in plants. Plant J. 27: 581-590.
    • (2001) Plant J , vol.27 , pp. 581-590
    • Wesley, S.V.1
  • 71
    • 33645080188 scopus 로고    scopus 로고
    • Beyond lectins: The calnexin/calreticulin chaperone system of the endoplasmic reticulum
    • Williams, D.B. (2006). Beyond lectins: The calnexin/calreticulin chaperone system of the endoplasmic reticulum. J. Cell Sci. 119: 615-623.
    • (2006) J. Cell Sci , vol.119 , pp. 615-623
    • Williams, D.B.1
  • 72
    • 0037133960 scopus 로고    scopus 로고
    • BES1 accumulates in the nucleus in response to brassinosteroids to regulate gene expression and promote stem elongation
    • Yin, Y., Wang, Z.Y., Mora-Garcia, S., Li, J., Yoshida, S., Asami, T., and Chory, J. (2002). BES1 accumulates in the nucleus in response to brassinosteroids to regulate gene expression and promote stem elongation. Cell 109: 181-191.
    • (2002) Cell , vol.109 , pp. 181-191
    • Yin, Y.1    Wang, Z.Y.2    Mora-Garcia, S.3    Li, J.4    Yoshida, S.5    Asami, T.6    Chory, J.7
  • 73
    • 0036851211 scopus 로고    scopus 로고
    • Two putative BIN2 substrates are nuclear components of brassinosteroid signaling
    • Zhao, J., Peng, P., Schmitz, R.J., Decker, A.D., Tax, F.E., and Li, J. (2002). Two putative BIN2 substrates are nuclear components of brassinosteroid signaling. Plant Physiol. 130: 1221-1229.
    • (2002) Plant Physiol , vol.130 , pp. 1221-1229
    • Zhao, J.1    Peng, P.2    Schmitz, R.J.3    Decker, A.D.4    Tax, F.E.5    Li, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.