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Volumn 21, Issue 5, 2010, Pages 472-478

Life and death of a BiP substrate

Author keywords

BiP Hsp70; ER associated degradation; ERdjs; Non glycosylated proteins; Nucleotide exchange factors

Indexed keywords

ERDJ 1 PROTEIN; ERDJ 2 PROTEIN; ERDJ 3 PROTEIN; ERDJ 4 PROTEIN; ERDJ 5 PROTEIN; ERDJ 6 PROTEIN; ERDJ 7PROTEIN; GLUCOSE REGULATED PROTEIN 78; HEAT SHOCK PROTEIN 70; INITIATION FACTOR; MEMBRANE PROTEIN; PROTEIN DNAJ; UNCLASSIFIED DRUG;

EID: 77952580752     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2009.12.008     Document Type: Review
Times cited : (146)

References (77)
  • 1
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond C., and Helenius A. Quality control in the secretory pathway. Curr Opin Cell Biol 7 (1995) 523-529
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 2
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate
    • Werner E.D., Brodsky J.L., and McCracken A.A. Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc Natl Acad Sci USA 93 (1996) 13797-13801
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 3
    • 0037287977 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein degradation
    • Jarosch E., Lenk U., and Sommer T. Endoplasmic reticulum-associated protein degradation. Int Rev Cytol 223 (2003) 39-81
    • (2003) Int Rev Cytol , vol.223 , pp. 39-81
    • Jarosch, E.1    Lenk, U.2    Sommer, T.3
  • 4
    • 7444240833 scopus 로고    scopus 로고
    • BiP is a master regulator of ER function
    • Hendershot L.M. BiP is a master regulator of ER function. Mt Sinai J Med 71 (2004) 289-297
    • (2004) Mt Sinai J Med , vol.71 , pp. 289-297
    • Hendershot, L.M.1
  • 5
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
    • Molinari M., and Helenius A. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 288 (2000) 331-333
    • (2000) Science , vol.288 , pp. 331-333
    • Molinari, M.1    Helenius, A.2
  • 6
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D., and Walter P. Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8 (2007) 519-529
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 7
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton R.Y. ER-associated degradation in protein quality control and cellular regulation. Curr Opin Cell Biol 14 (2002) 476-482
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 8
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar S.S., and Brodsky J.L. One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9 (2008) 944-957
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 9
    • 36249014338 scopus 로고    scopus 로고
    • The EDEM and Yos9p families of lectin-like ERAD factors
    • Kanehara K., Kawaguchi S., and Ng D.T. The EDEM and Yos9p families of lectin-like ERAD factors. Semin Cell Dev Biol 18 (2007) 743-750
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 743-750
    • Kanehara, K.1    Kawaguchi, S.2    Ng, D.T.3
  • 10
    • 36249022750 scopus 로고    scopus 로고
    • Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp
    • Okuda-Shimizu Y., and Hendershot L.M. Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp. Mol Cell 28 (2007) 544-554
    • (2007) Mol Cell , vol.28 , pp. 544-554
    • Okuda-Shimizu, Y.1    Hendershot, L.M.2
  • 11
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer M.P., and Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 62 (2005) 670-684
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 12
    • 27944436648 scopus 로고    scopus 로고
    • Structural basis of interdomain communication in the Hsc70 chaperone
    • Jiang J., Prasad K., Lafer E.M., and Sousa R. Structural basis of interdomain communication in the Hsc70 chaperone. Mol Cell 20 (2005) 513-524
    • (2005) Mol Cell , vol.20 , pp. 513-524
    • Jiang, J.1    Prasad, K.2    Lafer, E.M.3    Sousa, R.4
  • 13
    • 39549101755 scopus 로고    scopus 로고
    • BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP
    • Awad W., Estrada I., Shen Y., and Hendershot L.M. BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP. Proc Natl Acad Sci USA 105 (2008) 1164-1169
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1164-1169
    • Awad, W.1    Estrada, I.2    Shen, Y.3    Hendershot, L.M.4
  • 14
    • 0347033285 scopus 로고    scopus 로고
    • BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP
    • Chung K.T., Shen Y., and Hendershot L.M. BAP, a mammalian BiP-associated protein, is a nucleotide exchange factor that regulates the ATPase activity of BiP. J Biol Chem 277 (2002) 47557-47563
    • (2002) J Biol Chem , vol.277 , pp. 47557-47563
    • Chung, K.T.1    Shen, Y.2    Hendershot, L.M.3
  • 15
    • 51249111066 scopus 로고    scopus 로고
    • Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein
    • Awe K., Lambert C., and Prange R. Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein. FEBS Lett 582 (2008) 3179-3184
    • (2008) FEBS Lett , vol.582 , pp. 3179-3184
    • Awe, K.1    Lambert, C.2    Prange, R.3
  • 17
    • 28444497039 scopus 로고    scopus 로고
    • Mutations in SIL1 cause Marinesco-Sjogren syndrome, a cerebellar ataxia with cataract and myopathy
    • Senderek J., Krieger M., Stendel C., Bergmann C., Moser M., Breitbach-Faller N., et al. Mutations in SIL1 cause Marinesco-Sjogren syndrome, a cerebellar ataxia with cataract and myopathy. Nat Genet 37 (2005) 1312-1314
    • (2005) Nat Genet , vol.37 , pp. 1312-1314
    • Senderek, J.1    Krieger, M.2    Stendel, C.3    Bergmann, C.4    Moser, M.5    Breitbach-Faller, N.6
  • 18
    • 13244278043 scopus 로고    scopus 로고
    • Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange
    • Shomura Y., Dragovic Z., Chang H.C., Tzvetkov N., Young J.C., Brodsky J.L., et al. Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Mol Cell 17 (2005) 367-379
    • (2005) Mol Cell , vol.17 , pp. 367-379
    • Shomura, Y.1    Dragovic, Z.2    Chang, H.C.3    Tzvetkov, N.4    Young, J.C.5    Brodsky, J.L.6
  • 19
    • 25144520251 scopus 로고    scopus 로고
    • Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP
    • Zhao L., Longo-Guess C., Harris B.S., Lee J.W., and Ackerman S.L. Protein accumulation and neurodegeneration in the woozy mutant mouse is caused by disruption of SIL1, a cochaperone of BiP. Nat Genet 37 (2005) 974-979
    • (2005) Nat Genet , vol.37 , pp. 974-979
    • Zhao, L.1    Longo-Guess, C.2    Harris, B.S.3    Lee, J.W.4    Ackerman, S.L.5
  • 20
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • Dragovic Z., Broadley S.A., Shomura Y., Bracher A., and Hartl F.U. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 25 (2006) 2519-2528
    • (2006) EMBO J , vol.25 , pp. 2519-2528
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3    Bracher, A.4    Hartl, F.U.5
  • 22
    • 33748776034 scopus 로고    scopus 로고
    • The nucleotide exchange factor activity of Grp170 may explain the non-lethal phenotype of loss of Sil1 function in man and mouse
    • Weitzmann A., Volkmer J., and Zimmermann R. The nucleotide exchange factor activity of Grp170 may explain the non-lethal phenotype of loss of Sil1 function in man and mouse. FEBS Lett 580 (2006) 5237-5240
    • (2006) FEBS Lett , vol.580 , pp. 5237-5240
    • Weitzmann, A.1    Volkmer, J.2    Zimmermann, R.3
  • 23
    • 44649110104 scopus 로고    scopus 로고
    • Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
    • Polier S., Dragovic Z., Hartl F.U., and Bracher A. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133 (2008) 1068-1079
    • (2008) Cell , vol.133 , pp. 1068-1079
    • Polier, S.1    Dragovic, Z.2    Hartl, F.U.3    Bracher, A.4
  • 24
    • 0034388026 scopus 로고    scopus 로고
    • LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum
    • Tyson J.R., and Stirling C.J. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. EMBO J 19 (2000) 6440-6452
    • (2000) EMBO J , vol.19 , pp. 6440-6452
    • Tyson, J.R.1    Stirling, C.J.2
  • 25
    • 77649314881 scopus 로고    scopus 로고
    • Alteration of the unfolded protein response modifies neurodegeneration in a mouse model of Marinesco-Sjogren syndrome
    • Zhao L., Rosales C., Seburn K., Ron D., and Ackerman S.L. Alteration of the unfolded protein response modifies neurodegeneration in a mouse model of Marinesco-Sjogren syndrome. Hum Mol Genet (2009)
    • (2009) Hum Mol Genet
    • Zhao, L.1    Rosales, C.2    Seburn, K.3    Ron, D.4    Ackerman, S.L.5
  • 26
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek K., Marszalek J., Ang D., Georgopoulos C., and Zylicz M. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci USA 88 (1991) 2874-2878
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 27
    • 34748918368 scopus 로고    scopus 로고
    • The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum - a quantitative approach
    • Weitzmann A., Baldes C., Dudek J., and Zimmermann R. The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum - a quantitative approach. FEBS J 274 (2007) 5175-5187
    • (2007) FEBS J , vol.274 , pp. 5175-5187
    • Weitzmann, A.1    Baldes, C.2    Dudek, J.3    Zimmermann, R.4
  • 28
    • 55549139747 scopus 로고    scopus 로고
    • Regulated release of ERdj3 from unfolded proteins by BiP
    • Jin Y., Awad W., Petrova K., and Hendershot L.M. Regulated release of ERdj3 from unfolded proteins by BiP. EMBO J 27 (2008) 2873-2882
    • (2008) EMBO J , vol.27 , pp. 2873-2882
    • Jin, Y.1    Awad, W.2    Petrova, K.3    Hendershot, L.M.4
  • 29
    • 55549141494 scopus 로고    scopus 로고
    • Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3
    • Petrova K., Oyadomari S., Hendershot L.M., and Ron D. Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3. EMBO J 27 (2008) 2862-2872
    • (2008) EMBO J , vol.27 , pp. 2862-2872
    • Petrova, K.1    Oyadomari, S.2    Hendershot, L.M.3    Ron, D.4
  • 31
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman B.D., Hendershot L.M., and Johnson A.E. BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92 (1998) 747-758
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 32
    • 13444271726 scopus 로고    scopus 로고
    • The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum
    • Alder N.N., Shen Y., Brodsky J.L., Hendershot L.M., and Johnson A.E. The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum. J Cell Biol 168 (2005) 389-399
    • (2005) J Cell Biol , vol.168 , pp. 389-399
    • Alder, N.N.1    Shen, Y.2    Brodsky, J.L.3    Hendershot, L.M.4    Johnson, A.E.5
  • 34
    • 0028822223 scopus 로고
    • BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum
    • Brodsky J.L., Goeckeler J., and Schekman R. BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum. Proc Natl Acad Sci USA 92 (1995) 9643-9646
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9643-9646
    • Brodsky, J.L.1    Goeckeler, J.2    Schekman, R.3
  • 35
    • 33751185584 scopus 로고    scopus 로고
    • Protein transport into the endoplasmic reticulum: mechanisms and pathologies
    • Zimmermann R., Muller L., and Wullich B. Protein transport into the endoplasmic reticulum: mechanisms and pathologies. Trends Mol Med 12 (2006) 567-573
    • (2006) Trends Mol Med , vol.12 , pp. 567-573
    • Zimmermann, R.1    Muller, L.2    Wullich, B.3
  • 36
    • 2942724434 scopus 로고    scopus 로고
    • Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p
    • Bies C., Blum R., Dudek J., Nastainczyk W., Oberhauser S., Jung M., et al. Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p. Biol Chem 385 (2004) 389-395
    • (2004) Biol Chem , vol.385 , pp. 389-395
    • Bies, C.1    Blum, R.2    Dudek, J.3    Nastainczyk, W.4    Oberhauser, S.5    Jung, M.6
  • 37
    • 0034637459 scopus 로고    scopus 로고
    • HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells
    • Yu M., Haslam R.H., and Haslam D.B. HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells. J Biol Chem 275 (2000) 24984-24992
    • (2000) J Biol Chem , vol.275 , pp. 24984-24992
    • Yu, M.1    Haslam, R.H.2    Haslam, D.B.3
  • 38
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L., Usherwood Y.K., Chung K.T., and Hendershot L.M. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13 (2002) 4456-4469
    • (2002) Mol Biol Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 39
    • 11144249887 scopus 로고    scopus 로고
    • ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates
    • Shen Y., and Hendershot L.M. ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates. Mol Biol Cell 16 (2005) 40-50
    • (2005) Mol Biol Cell , vol.16 , pp. 40-50
    • Shen, Y.1    Hendershot, L.M.2
  • 40
    • 70450273171 scopus 로고    scopus 로고
    • The mammalian HSP40 ERdj3 requires its HSP70 interaction and substrate binding properties to complement various yeast HSP40-dependent functions
    • Vembar S.S., Jin Y., Brodsky J.L., and Hendershot L.M. The mammalian HSP40 ERdj3 requires its HSP70 interaction and substrate binding properties to complement various yeast HSP40-dependent functions. J Biol Chem (2009)
    • (2009) J Biol Chem
    • Vembar, S.S.1    Jin, Y.2    Brodsky, J.L.3    Hendershot, L.M.4
  • 41
    • 0037013252 scopus 로고    scopus 로고
    • Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress
    • Shen Y., Meunier L., and Hendershot L.M. Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress. J Biol Chem 277 (2002) 15947-15956
    • (2002) J Biol Chem , vol.277 , pp. 15947-15956
    • Shen, Y.1    Meunier, L.2    Hendershot, L.M.3
  • 42
    • 0037323012 scopus 로고    scopus 로고
    • MDG1/ERdj4, an ER-resident DnaJ family member, suppresses cell death induced by ER stress
    • Kurisu J., Honma A., Miyajima H., Kondo S., Okumura M., and Imaizumi K. MDG1/ERdj4, an ER-resident DnaJ family member, suppresses cell death induced by ER stress. Genes Cells 8 (2003) 189-202
    • (2003) Genes Cells , vol.8 , pp. 189-202
    • Kurisu, J.1    Honma, A.2    Miyajima, H.3    Kondo, S.4    Okumura, M.5    Imaizumi, K.6
  • 43
    • 0035840154 scopus 로고    scopus 로고
    • Upregulation of the cochaperone Mdg1 in endothelial cells is induced by stress and during in vitro angiogenesis
    • Prols F., Mayer M.P., Renner O., Czarnecki P.G., Ast M., Gassler C., et al. Upregulation of the cochaperone Mdg1 in endothelial cells is induced by stress and during in vitro angiogenesis. Exp Cell Res 269 (2001) 42-53
    • (2001) Exp Cell Res , vol.269 , pp. 42-53
    • Prols, F.1    Mayer, M.P.2    Renner, O.3    Czarnecki, P.G.4    Ast, M.5    Gassler, C.6
  • 44
    • 48249155627 scopus 로고    scopus 로고
    • ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C
    • Dong M., Bridges J.P., Apsley K., Xu Y., and Weaver T.E. ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C. Mol Biol Cell 19 (2008) 2620-2630
    • (2008) Mol Biol Cell , vol.19 , pp. 2620-2630
    • Dong, M.1    Bridges, J.P.2    Apsley, K.3    Xu, Y.4    Weaver, T.E.5
  • 45
    • 0037462652 scopus 로고    scopus 로고
    • JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs
    • Hosoda A., Kimata Y., Tsuru A., and Kohno K. JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs. J Biol Chem 278 (2003) 2669-2676
    • (2003) J Biol Chem , vol.278 , pp. 2669-2676
    • Hosoda, A.1    Kimata, Y.2    Tsuru, A.3    Kohno, K.4
  • 46
    • 0037428470 scopus 로고    scopus 로고
    • ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress
    • Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T., Damdimopoulos A.E., Hermann S., et al. ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. J Biol Chem 278 (2003) 1059-1066
    • (2003) J Biol Chem , vol.278 , pp. 1059-1066
    • Cunnea, P.M.1    Miranda-Vizuete, A.2    Bertoli, G.3    Simmen, T.4    Damdimopoulos, A.E.5    Hermann, S.6
  • 47
    • 48249117110 scopus 로고    scopus 로고
    • ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
    • Ushioda R., Hoseki J., Araki K., Jansen G., Thomas D.Y., and Nagata K. ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321 (2008) 569-572
    • (2008) Science , vol.321 , pp. 569-572
    • Ushioda, R.1    Hoseki, J.2    Araki, K.3    Jansen, G.4    Thomas, D.Y.5    Nagata, K.6
  • 49
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson J.C., Shaler T.A., Tyler R.E., and Kopito R.R. OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol 10 (2008) 272-282
    • (2008) Nat Cell Biol , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 50
    • 0037058574 scopus 로고    scopus 로고
    • Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK
    • Yan W., Frank C.L., Korth M.J., Sopher B.L., Novoa I., Ron D., et al. Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc Natl Acad Sci USA 99 (2002) 15920-15925
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15920-15925
    • Yan, W.1    Frank, C.L.2    Korth, M.J.3    Sopher, B.L.4    Novoa, I.5    Ron, D.6
  • 51
    • 20144386666 scopus 로고    scopus 로고
    • Pancreatic beta-cell failure and diabetes in mice with a deletion mutation of the endoplasmic reticulum molecular chaperone gene P58IPK
    • Ladiges W.C., Knoblaugh S.E., Morton J.F., Korth M.J., Sopher B.L., Baskin C.R., et al. Pancreatic beta-cell failure and diabetes in mice with a deletion mutation of the endoplasmic reticulum molecular chaperone gene P58IPK. Diabetes 54 (2005) 1074-1081
    • (2005) Diabetes , vol.54 , pp. 1074-1081
    • Ladiges, W.C.1    Knoblaugh, S.E.2    Morton, J.F.3    Korth, M.J.4    Sopher, B.L.5    Baskin, C.R.6
  • 53
    • 67651211597 scopus 로고    scopus 로고
    • Analysis of the membrane proteome of canine pancreatic rough microsomes identifies a novel Hsp40, termed ERj7
    • Zahedi R.P., Volzing C., Schmitt A., Frien M., Jung M., Dudek J., et al. Analysis of the membrane proteome of canine pancreatic rough microsomes identifies a novel Hsp40, termed ERj7. Proteomics 9 (2009) 3463-3473
    • (2009) Proteomics , vol.9 , pp. 3463-3473
    • Zahedi, R.P.1    Volzing, C.2    Schmitt, A.3    Frien, M.4    Jung, M.5    Dudek, J.6
  • 55
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly H., Rape M., Braun S., Rumpf S., Hoege C., and Jentsch S. A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120 (2005) 73-84
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 56
    • 43149096666 scopus 로고    scopus 로고
    • The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum
    • Nakatsukasa K., and Brodsky J.L. The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic 9 (2008) 861-870
    • (2008) Traffic , vol.9 , pp. 861-870
    • Nakatsukasa, K.1    Brodsky, J.L.2
  • 57
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller M.M., Finger A., Schweiger M., and Wolf D.H. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273 (1996) 1725-1728
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 58
    • 0030041781 scopus 로고    scopus 로고
    • Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast
    • Knop M., Finger A., Braun T., Hellmuth K., and Wolf D.H. Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J 15 (1996) 753-763
    • (1996) EMBO J , vol.15 , pp. 753-763
    • Knop, M.1    Finger, A.2    Braun, T.3    Hellmuth, K.4    Wolf, D.H.5
  • 59
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye Y., Shibata Y., Yun C., Ron D., and Rapoport T.A. A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol. Nature 429 (2004) 841-847
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 60
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley B.N., and Ploegh H.L. A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429 (2004) 834-840
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 61
    • 31944450850 scopus 로고    scopus 로고
    • Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation
    • Oda Y., Okada T., Yoshida H., Kaufman R.J., Nagata K., and Mori K. Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation. J Cell Biol 172 (2006) 383-393
    • (2006) J Cell Biol , vol.172 , pp. 383-393
    • Oda, Y.1    Okada, T.2    Yoshida, H.3    Kaufman, R.J.4    Nagata, K.5    Mori, K.6
  • 62
    • 0034693217 scopus 로고    scopus 로고
    • Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress
    • Kokame K., Agarwala K.L., Kato H., and Miyata T. Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress. J Biol Chem 275 (2000) 32846-32853
    • (2000) J Biol Chem , vol.275 , pp. 32846-32853
    • Kokame, K.1    Agarwala, K.L.2    Kato, H.3    Miyata, T.4
  • 63
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich E., Kerem A., Frohlich K.U., Diamant N., and Bar-Nun S. AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 22 (2002) 626-634
    • (2002) Mol Cell Biol , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frohlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 65
    • 0037929972 scopus 로고    scopus 로고
    • Overexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cells
    • Liang J.S., Kim T., Fang S., Yamaguchi J., Weissman A.M., Fisher E.A., et al. Overexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cells. J Biol Chem 278 (2003) 23984-23988
    • (2003) J Biol Chem , vol.278 , pp. 23984-23988
    • Liang, J.S.1    Kim, T.2    Fang, S.3    Yamaguchi, J.4    Weissman, A.M.5    Fisher, E.A.6
  • 66
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annu Rev Biochem 70 (2001) 503-533
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 67
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • Voeltz G.K., Rolls M.M., and Rapoport T.A. Structural organization of the endoplasmic reticulum. EMBO Rep 3 (2002) 944-950
    • (2002) EMBO Rep , vol.3 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 69
    • 33745752369 scopus 로고    scopus 로고
    • Endoplasmic reticulum architecture: structures in flux
    • Borgese N., Francolini M., and Snapp E. Endoplasmic reticulum architecture: structures in flux. Curr Opin Cell Biol 18 (2006) 358-364
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 358-364
    • Borgese, N.1    Francolini, M.2    Snapp, E.3
  • 71
    • 0035999994 scopus 로고    scopus 로고
    • Probing for membrane domains in the endoplasmic reticulum: retention and degradation of unassembled MHC class I molecules
    • Spiliotis E.T., Pentcheva T., and Edidin M. Probing for membrane domains in the endoplasmic reticulum: retention and degradation of unassembled MHC class I molecules. Mol Biol Cell 13 (2002) 1566-1581
    • (2002) Mol Biol Cell , vol.13 , pp. 1566-1581
    • Spiliotis, E.T.1    Pentcheva, T.2    Edidin, M.3
  • 72
    • 84934442760 scopus 로고    scopus 로고
    • Organization of the functions and components of the endoplasmic reticulum
    • Shimizu Y., and Hendershot L.M. Organization of the functions and components of the endoplasmic reticulum. Adv Exp Med Biol 594 (2007) 37-46
    • (2007) Adv Exp Med Biol , vol.594 , pp. 37-46
    • Shimizu, Y.1    Hendershot, L.M.2
  • 73
    • 41449116766 scopus 로고    scopus 로고
    • Ero1 and redox homeostasis in the endoplasmic reticulum
    • Sevier C.S., and Kaiser C.A. Ero1 and redox homeostasis in the endoplasmic reticulum. Biochim Biophys Acta 1783 (2008) 549-556
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 549-556
    • Sevier, C.S.1    Kaiser, C.A.2
  • 74
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response
    • Pagani M., Fabbri M., Benedetti C., Fassio A., Pilati S., Bulleid N.J., et al. Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J Biol Chem 275 (2000) 23685-23692
    • (2000) J Biol Chem , vol.275 , pp. 23685-23692
    • Pagani, M.1    Fabbri, M.2    Benedetti, C.3    Fassio, A.4    Pilati, S.5    Bulleid, N.J.6
  • 75
    • 41549159471 scopus 로고    scopus 로고
    • The human PDI family: versatility packed into a single fold
    • Appenzeller-Herzog C., and Ellgaard L. The human PDI family: versatility packed into a single fold. Biochim Biophys Acta 1783 (2008) 535-548
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 535-548
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 76
    • 48249138088 scopus 로고    scopus 로고
    • Bap31 is an itinerant protein that moves between the peripheral endoplasmic reticulum (ER) and a juxtanuclear compartment related to ER-associated degradation
    • Wakana Y., Takai S., Nakajima K., Tani K., Yamamoto A., Watson P., et al. Bap31 is an itinerant protein that moves between the peripheral endoplasmic reticulum (ER) and a juxtanuclear compartment related to ER-associated degradation. Mol Biol Cell 19 (2008) 1825-1836
    • (2008) Mol Biol Cell , vol.19 , pp. 1825-1836
    • Wakana, Y.1    Takai, S.2    Nakajima, K.3    Tani, K.4    Yamamoto, A.5    Watson, P.6
  • 77
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function
    • Cheetham M.E., and Caplan A.J. Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3 (1998) 28-36
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2


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