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Volumn 10, Issue 5, 2000, Pages 203-210

Pathways for protein disulphide bond formation

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE; MEMBRANE PROTEIN; PROTEIN DISULFIDE ISOMERASE; SECRETORY PROTEIN; THIOL;

EID: 0034194815     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(00)01745-1     Document Type: Review
Times cited : (305)

References (56)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science. 181:1973;223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0026062381 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Dependence of the rate on the composition of the redox buffer
    • Lyles M.M., Gilbert H.F. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry. 30:1991;613-619.
    • (1991) Biochemistry , vol.30 , pp. 613-619
    • Lyles, M.M.1    Gilbert, H.F.2
  • 3
    • 0014937559 scopus 로고
    • Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme
    • Saxena V.P., Wetlaufer D.B. Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry. 9:1970;5015-5023.
    • (1970) Biochemistry , vol.9 , pp. 5015-5023
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 4
    • 73649177752 scopus 로고
    • Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver
    • Goldberger R.F.et al. Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver. J. Biol. Chem. 238:1963;628-635.
    • (1963) J. Biol. Chem. , vol.238 , pp. 628-635
    • Goldberger, R.F.1
  • 7
    • 0025972887 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: Pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase
    • Lyles M.M., Gilbert H.F. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase. Biochemistry. 30:1991;619-625.
    • (1991) Biochemistry , vol.30 , pp. 619-625
    • Lyles, M.M.1    Gilbert, H.F.2
  • 9
    • 0027203922 scopus 로고
    • The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity
    • LaMantia M.L., Lennarz W.J. The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity. Cell. 74:1993;899-908.
    • (1993) Cell , vol.74 , pp. 899-908
    • LaMantia, M.L.1    Lennarz, W.J.2
  • 10
    • 0026013390 scopus 로고
    • Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms
    • Scherens B.et al. Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms. Yeast. 7:1991;185-193.
    • (1991) Yeast , vol.7 , pp. 185-193
    • Scherens, B.1
  • 11
    • 0025816663 scopus 로고
    • Folding of influenza hemagglutinin in the endoplasmic reticulum
    • Braakman I.et al. Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol. 114:1991;401-411.
    • (1991) J. Cell Biol. , vol.114 , pp. 401-411
    • Braakman, I.1
  • 12
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C.et al. Oxidized redox state of glutathione in the endoplasmic reticulum. Science. 257:1992;1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1
  • 13
    • 0026604334 scopus 로고
    • Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum
    • Braakman I.et al. Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J. 11:1992;1717-1722.
    • (1992) EMBO J. , vol.11 , pp. 1717-1722
    • Braakman, I.1
  • 14
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand A.R., Kaiser C.A. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell. 1:1998;161-170.
    • (1998) Mol. Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 15
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard M.G.et al. Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol. Cell. 1:1998;171-182.
    • (1998) Mol. Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1
  • 16
    • 0033213605 scopus 로고    scopus 로고
    • Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • Frand A.R., Kaiser C.A. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol. Cell. 4:1999;469-477.
    • (1999) Mol. Cell , vol.4 , pp. 469-477
    • Frand, A.R.1    Kaiser, C.A.2
  • 17
    • 0030807389 scopus 로고    scopus 로고
    • Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum
    • Holst B.et al. Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J. Cell Biol. 138:1997;1229-1238.
    • (1997) J. Cell Biol. , vol.138 , pp. 1229-1238
    • Holst, B.1
  • 18
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari M., Helenius A. Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature. 402:1999;90-93.
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 19
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissiere M.C.et al. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270:1995;28006-28009.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28006-28009
    • Laboissiere, M.C.1
  • 20
    • 0029115691 scopus 로고
    • Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion
    • Tachikawa H.et al. Isolation and characterization of a yeast gene, MPD1, the overexpression of which suppresses inviability caused by protein disulfide isomerase depletion. FEBS Lett. 369:1995;212-216.
    • (1995) FEBS Lett. , vol.369 , pp. 212-216
    • Tachikawa, H.1
  • 21
    • 0031590425 scopus 로고    scopus 로고
    • Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner
    • Tachikawa H.et al. Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner. Biochem. Biophys. Res. Commun. 239:1997;710-714.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 710-714
    • Tachikawa, H.1
  • 22
    • 0033230434 scopus 로고    scopus 로고
    • Eps1, a novel PDI-related protein involved in ER quality control in yeast
    • Wang Q., Chang A. Eps1, a novel PDI-related protein involved in ER quality control in yeast. EMBO J. 18:1999;5972-5982.
    • (1999) EMBO J. , vol.18 , pp. 5972-5982
    • Wang, Q.1    Chang, A.2
  • 23
    • 0033163787 scopus 로고    scopus 로고
    • Protein oxidation: Prime suspect found 'not guilty'
    • Bader M.et al. Protein oxidation: prime suspect found 'not guilty'. Nat. Cell Biol. 1:1999;E56-E58.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 56-E58
    • Bader, M.1
  • 24
    • 0026338492 scopus 로고
    • Molecular cloning of the gamma-glutamylcysteine synthetase gene of Saccharomyces cerevisiae
    • Ohtake Y., Yabuuchi S. Molecular cloning of the gamma-glutamylcysteine synthetase gene of Saccharomyces cerevisiae. Yeast. 7:1991;953-961.
    • (1991) Yeast , vol.7 , pp. 953-961
    • Ohtake, Y.1    Yabuuchi, S.2
  • 25
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulphide-bond formation
    • Cuozzo J.W., Kaiser C.A. Competition between glutathione and protein thiols for disulphide-bond formation. Nat. Cell Biol. 1:1999;130-135.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 130-135
    • Cuozzo, J.W.1    Kaiser, C.A.2
  • 26
    • 0039251408 scopus 로고    scopus 로고
    • Preferential transport of glutathione versus glutathione disulfide in rat liver microsomal vesicles
    • Banhegyi G.et al. Preferential transport of glutathione versus glutathione disulfide in rat liver microsomal vesicles. J. Biol. Chem. 274:1999;12213-12216.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12213-12216
    • Banhegyi, G.1
  • 27
    • 0027293791 scopus 로고
    • Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin
    • Lundstrom J., Holmgren A. Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin. Biochemistry. 32:1993;6649-6655.
    • (1993) Biochemistry , vol.32 , pp. 6649-6655
    • Lundstrom, J.1    Holmgren, A.2
  • 28
    • 0032566752 scopus 로고    scopus 로고
    • Kinetic analysis of the mechanism and specificity of protein-disulfide isomerase using fluorescence-quenched peptides
    • Westphal V.et al. Kinetic analysis of the mechanism and specificity of protein-disulfide isomerase using fluorescence-quenched peptides. J. Biol. Chem. 273:1998;24992-24999.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24992-24999
    • Westphal, V.1
  • 29
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas D., Raina S. Protein folding in the bacterial periplasm. J. Bacteriol. 179:1997;2465-2471.
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 30
    • 0032720032 scopus 로고    scopus 로고
    • Electron avenue: Pathways of disulfide bond formation and isomerization
    • Debarbieux L., Beckwith J. Electron avenue: pathways of disulfide bond formation and isomerization. Cell. 99:1999;117-119.
    • (1999) Cell , vol.99 , pp. 117-119
    • Debarbieux, L.1    Beckwith, J.2
  • 31
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell J.C.et al. Identification of a protein required for disulfide bond formation in vivo. Cell. 67:1991;581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.1
  • 32
    • 0033597878 scopus 로고    scopus 로고
    • Oxidative protein folding is driven by the electron transport system
    • Bader M.et al. Oxidative protein folding is driven by the electron transport system. Cell. 98:1999;217-227.
    • (1999) Cell , vol.98 , pp. 217-227
    • Bader, M.1
  • 33
    • 0029161150 scopus 로고
    • DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA
    • Kishigami S.et al. DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA. J. Biol. Chem. 270:1995;17072-17074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17072-17074
    • Kishigami, S.1
  • 34
    • 0028971218 scopus 로고
    • Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA
    • Guilhot C.et al. Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA. Proc. Natl. Acad. Sci. U. S. A. 92:1995;9895-9899.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9895-9899
    • Guilhot, C.1
  • 35
    • 0028850389 scopus 로고
    • Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli
    • Humphreys D.P.et al. Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli. J. Biol. Chem. 270:1995;28210-28215.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28210-28215
    • Humphreys, D.P.1
  • 36
    • 0027475212 scopus 로고
    • A pathway for disulfide bond formation in vivo
    • Bardwell J.C.et al. A pathway for disulfide bond formation in vivo. Proc. Natl. Acad. Sci. U. S. A. 90:1993;1038-1042.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 1038-1042
    • Bardwell, J.C.1
  • 37
    • 0029822654 scopus 로고    scopus 로고
    • An in vivo pathway for disulfide bond isomerization in Escherichia coli
    • Rietsch A.et al. An in vivo pathway for disulfide bond isomerization in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 93:1996;13048-13053.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 13048-13053
    • Rietsch, A.1
  • 38
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch A.et al. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol. 179:1997;6602-6608.
    • (1997) J. Bacteriol. , vol.179 , pp. 6602-6608
    • Rietsch, A.1
  • 39
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • Ferrari D.M., Soling H.D. The protein disulphide-isomerase family: unravelling a string of folds. Biochem. J. 339:1999;1-10.
    • (1999) Biochem. J. , vol.339 , pp. 1-10
    • Ferrari, D.M.1    Soling, H.D.2
  • 40
    • 0026738643 scopus 로고
    • The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase
    • Tachibana C., Stevens T.H. The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell. Biol. 12:1992;4601-4611.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4601-4611
    • Tachibana, C.1    Stevens, T.H.2
  • 41
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver J.D.et al. Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science. 275:1997;86-88.
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1
  • 42
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun A.et al. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 273:1998;6009-6012.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6009-6012
    • Zapun, A.1
  • 43
    • 0032101239 scopus 로고    scopus 로고
    • The unfolded protein response: An intracellular signalling pathway with many surprising features
    • Sidrauski C.et al. The unfolded protein response: an intracellular signalling pathway with many surprising features. Trends Cell Biol. 8:1998;245-249.
    • (1998) Trends Cell Biol. , vol.8 , pp. 245-249
    • Sidrauski, C.1
  • 44
    • 0030671552 scopus 로고    scopus 로고
    • Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells
    • Kobayashi T.et al. Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells. Proc. Natl. Acad. Sci. U. S. A. 94:1997;11857-11862.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11857-11862
    • Kobayashi, T.1
  • 45
    • 0033106153 scopus 로고    scopus 로고
    • Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway
    • Kobayashi T., Ito K. Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway. EMBO J. 18:1999;1192-1198.
    • (1999) EMBO J. , vol.18 , pp. 1192-1198
    • Kobayashi, T.1    Ito, K.2
  • 46
    • 0032412784 scopus 로고    scopus 로고
    • Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae
    • Daum G.et al. Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae. Yeast. 14:1998;1471-1510.
    • (1998) Yeast , vol.14 , pp. 1471-1510
    • Daum, G.1
  • 47
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas D.et al. Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14:1995;3415-3424.
    • (1995) EMBO J. , vol.14 , pp. 3415-3424
    • Missiakas, D.1
  • 48
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman J.C.et al. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature. 317:1985;267-270.
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1
  • 49
    • 0032481380 scopus 로고    scopus 로고
    • The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • Klappa P.et al. The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J. 17:1998;927-935.
    • (1998) EMBO J. , vol.17 , pp. 927-935
    • Klappa, P.1
  • 50
    • 0025070112 scopus 로고
    • ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase
    • Mazzarella R.A.et al. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J. Biol. Chem. 265:1990;1094-1101.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1094-1101
    • Mazzarella, R.A.1
  • 51
    • 0027957793 scopus 로고
    • A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily
    • Nigam S.K.et al. A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily. J. Biol. Chem. 269:1994;1744-1749.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1744-1749
    • Nigam, S.K.1
  • 52
    • 0028795422 scopus 로고
    • Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: Comparison with protein disulfide isomerase
    • Lundstrom-Ljung J.et al. Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase. FEBS Lett. 357:1995;305-308.
    • (1995) FEBS Lett. , vol.357 , pp. 305-308
    • Lundstrom-Ljung, J.1
  • 53
    • 0028823248 scopus 로고
    • Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation
    • Hirano N.et al. Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation. Eur. J. Biochem. 234:1995;336-342.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 336-342
    • Hirano, N.1
  • 54
    • 0028001714 scopus 로고
    • CaBP1, a calcium binding protein of the thioredoxin family, is a resident KDEL protein of the ER and not of the intermediate compartment
    • Fullekrug J.et al. CaBP1, a calcium binding protein of the thioredoxin family, is a resident KDEL protein of the ER and not of the intermediate compartment. J. Cell Sci. 107:1994;2719-2727.
    • (1994) J. Cell Sci. , vol.107 , pp. 2719-2727
    • Fullekrug, J.1
  • 55
    • 0029121158 scopus 로고
    • Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR)
    • Hayano T., Kikuchi M. Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR). FEBS Lett. 372:1995;210-214.
    • (1995) FEBS Lett. , vol.372 , pp. 210-214
    • Hayano, T.1    Kikuchi, M.2
  • 56
    • 0030934557 scopus 로고    scopus 로고
    • Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp
    • Desilva M.G.et al. Molecular characterization of a pancreas-specific protein disulfide isomerase, PDIp. DNA Cell Biol. 16:1997;269-274.
    • (1997) DNA Cell Biol. , vol.16 , pp. 269-274
    • Desilva, M.G.1


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