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Volumn 52, Issue 9, 2012, Pages 2000-2012

Oxidative protein folding and unfolded protein response elicit differing redox regulation in endoplasmic reticulum and cytosol of yeast

Author keywords

Free radicals; Glutathione; Redox sensitive roGFP; Secretion; UPR

Indexed keywords

GLUTATHIONE PEROXIDASE 1; GLUTATHIONE REDUCTASE; PROTEIN DISULFIDE ISOMERASE; TRYPSINOGEN;

EID: 84859484553     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.02.048     Document Type: Article
Times cited : (75)

References (55)
  • 1
    • 77957293977 scopus 로고    scopus 로고
    • Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation
    • J.L. Goeckeler, and J.L. Brodsky Molecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation Diabetes Obes. Metab. 12 Suppl. 2 2010 32 38
    • (2010) Diabetes Obes. Metab. , vol.12 , Issue.SUPPL. 2 , pp. 32-38
    • Goeckeler, J.L.1    Brodsky, J.L.2
  • 2
    • 36248949141 scopus 로고    scopus 로고
    • The endoplasmic reticulum and the unfolded protein response
    • J.D. Malhotra, and R.J. Kaufman The endoplasmic reticulum and the unfolded protein response Semin. Cell Dev. Biol. 18 2007 716 731
    • (2007) Semin. Cell Dev. Biol. , vol.18 , pp. 716-731
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 3
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • H. Yoshida ER stress and diseases FEBS J. 274 2007 630 658
    • (2007) FEBS J. , vol.274 , pp. 630-658
    • Yoshida, H.1
  • 6
    • 34447550255 scopus 로고    scopus 로고
    • Managing and exploiting stress in the antibody factory
    • S. Cenci, and R. Sitia Managing and exploiting stress in the antibody factory FEBS Lett. 581 2007 3652 3657
    • (2007) FEBS Lett. , vol.581 , pp. 3652-3657
    • Cenci, S.1    Sitia, R.2
  • 7
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • B.P. Tu, S.C. Ho-Schleyer, K.J. Travers, and J.S. Weissman Biochemical basis of oxidative protein folding in the endoplasmic reticulum Science 290 2000 1571 1574
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 8
    • 0036052119 scopus 로고    scopus 로고
    • An overview on glutathione in Saccharomyces versus non-conventional yeasts
    • M.J. Penninckx An overview on glutathione in Saccharomyces versus non-conventional yeasts FEMS Yeast Res. 2 2002 295 305
    • (2002) FEMS Yeast Res. , vol.2 , pp. 295-305
    • Penninckx, M.J.1
  • 9
  • 10
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • C. Hwang, A. Sinskey, and H. Lodish Oxidized redox state of glutathione in the endoplasmic reticulum Science 257 1992 1496 1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.2    Lodish, H.3
  • 11
    • 39749200944 scopus 로고    scopus 로고
    • Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation
    • B.M. Dixon, S.H. Heath, R. Kim, J.H. Suh, and T.M. Hagen Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation Antioxid. Redox Signal. 10 2008 963 972
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 963-972
    • Dixon, B.M.1    Heath, S.H.2    Kim, R.3    Suh, J.H.4    Hagen, T.M.5
  • 12
    • 56349087407 scopus 로고    scopus 로고
    • Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions
    • P. Merksamer, A. Trusina, and F. Papa Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions Cell 135 2008 933 947
    • (2008) Cell , vol.135 , pp. 933-947
    • Merksamer, P.1    Trusina, A.2    Papa, F.3
  • 13
    • 77950501289 scopus 로고    scopus 로고
    • Monitoring intracellular redox conditions in the endoplasmic reticulum of living yeasts
    • M. Delic, D. Mattanovich, and B. Gasser Monitoring intracellular redox conditions in the endoplasmic reticulum of living yeasts FEMS Microbiol. Lett. 306 2010 61 66
    • (2010) FEMS Microbiol. Lett. , vol.306 , pp. 61-66
    • Delic, M.1    Mattanovich, D.2    Gasser, B.3
  • 14
    • 75649118565 scopus 로고    scopus 로고
    • Stress-sensing mechanisms in the unfolded protein response: Similarities and differences between yeast and mammals
    • K. Kohno Stress-sensing mechanisms in the unfolded protein response: similarities and differences between yeast and mammals J. Biochem. 147 2010 27 33
    • (2010) J. Biochem. , vol.147 , pp. 27-33
    • Kohno, K.1
  • 15
    • 70450224859 scopus 로고    scopus 로고
    • The yeast Golgi apparatus: Insights and mysteries
    • E. Papanikou, and B.S. Glick The yeast Golgi apparatus: insights and mysteries FEBS Lett. 583 2009 3746 3751
    • (2009) FEBS Lett. , vol.583 , pp. 3746-3751
    • Papanikou, E.1    Glick, B.S.2
  • 17
    • 49749114828 scopus 로고    scopus 로고
    • Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments
    • J. Lohman, and S. Remington Development of a family of redox-sensitive green fluorescent protein indicators for use in relatively oxidizing subcellular environments Biochemistry 47 2008 8678 8688
    • (2008) Biochemistry , vol.47 , pp. 8678-8688
    • Lohman, J.1    Remington, S.2
  • 18
    • 79960420766 scopus 로고    scopus 로고
    • Real-time monitoring of redox changes in the mammalian endoplasmic reticulum
    • M. van Lith, S. Tiwari, J. Pediani, G. Milligan, and N.J. Bulleid Real-time monitoring of redox changes in the mammalian endoplasmic reticulum J. Cell Sci. 124 2011 2349 2356
    • (2011) J. Cell Sci. , vol.124 , pp. 2349-2356
    • Van Lith, M.1    Tiwari, S.2    Pediani, J.3    Milligan, G.4    Bulleid, N.J.5
  • 20
    • 49949115796 scopus 로고    scopus 로고
    • Overexpression of the riboflavin biosynthetic pathway in Pichia pastoris
    • H. Marx, D. Mattanovich, and M. Sauer Overexpression of the riboflavin biosynthetic pathway in Pichia pastoris Microb. Cell Fact. 7 2008 23
    • (2008) Microb. Cell Fact. , vol.7 , pp. 23
    • Marx, H.1    Mattanovich, D.2    Sauer, M.3
  • 22
    • 77954356493 scopus 로고    scopus 로고
    • Fluorescent protein-based redox probes
    • A.J. Meyer, and T.P. Dick Fluorescent protein-based redox probes Antioxid. Redox Signal. 13 2010 621 650
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 621-650
    • Meyer, A.J.1    Dick, T.P.2
  • 23
    • 0038364057 scopus 로고    scopus 로고
    • Assessing viability and cell-associated product of recombinant protein producing Pichia pastoris with flow cytometry
    • H. Hohenblum, N. Borth, and D. Mattanovich Assessing viability and cell-associated product of recombinant protein producing Pichia pastoris with flow cytometry J. Biotechnol. 102 2003 281 290
    • (2003) J. Biotechnol. , vol.102 , pp. 281-290
    • Hohenblum, H.1    Borth, N.2    Mattanovich, D.3
  • 25
    • 4444265582 scopus 로고    scopus 로고
    • Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death
    • C.M. Haynes, E.A. Titus, and A.A. Cooper Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death Mol. Cell 15 2004 767 776
    • (2004) Mol. Cell , vol.15 , pp. 767-776
    • Haynes, C.M.1    Titus, E.A.2    Cooper, A.A.3
  • 26
    • 65249134998 scopus 로고    scopus 로고
    • Cu, Zn superoxide dismutase and NADP(H) homeostasis are required for tolerance of endoplasmic reticulum stress in Saccharomyces cerevisiae
    • S.X. Tan, M. Teo, Y.T. Lam, I.W. Dawes, and G.G. Perrone Cu, Zn superoxide dismutase and NADP(H) homeostasis are required for tolerance of endoplasmic reticulum stress in Saccharomyces cerevisiae Mol. Biol. Cell 20 2009 1493 1508
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1493-1508
    • Tan, S.X.1    Teo, M.2    Lam, Y.T.3    Dawes, I.W.4    Perrone, G.G.5
  • 27
    • 0023352241 scopus 로고
    • Functional expression of the cre-lox site-specific recombination system in the yeast Saccharomyces cerevisiae
    • B. Sauer Functional expression of the cre-lox site-specific recombination system in the yeast Saccharomyces cerevisiae Mol. Cell. Biol. 7 1987 2087 2096
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2087-2096
    • Sauer, B.1
  • 28
    • 64749095823 scopus 로고    scopus 로고
    • Yap1-regulated glutathione redox system curtails accumulation of formaldehyde and reactive oxygen species in methanol metabolism of Pichia pastoris
    • T. Yano, E. Takigami, H. Yurimoto, and Y. Sakai Yap1-regulated glutathione redox system curtails accumulation of formaldehyde and reactive oxygen species in methanol metabolism of Pichia pastoris Eukaryot. Cell 8 2009 540 549
    • (2009) Eukaryot. Cell , vol.8 , pp. 540-549
    • Yano, T.1    Takigami, E.2    Yurimoto, H.3    Sakai, Y.4
  • 30
    • 79961127125 scopus 로고    scopus 로고
    • Glutathione peroxidase 2 in Saccharomyces cerevisiae is distributed in mitochondria and involved in sporulation
    • Y. Ukai, T. Kishimoto, T. Ohdate, S. Izawa, and Y. Inoue Glutathione peroxidase 2 in Saccharomyces cerevisiae is distributed in mitochondria and involved in sporulation Biochem. Biophys. Res. Commun. 411 2011 580 585
    • (2011) Biochem. Biophys. Res. Commun. , vol.411 , pp. 580-585
    • Ukai, Y.1    Kishimoto, T.2    Ohdate, T.3    Izawa, S.4    Inoue, Y.5
  • 31
    • 79955878526 scopus 로고    scopus 로고
    • Reexamination of the role of interplay between glutathione and protein disulfide isomerase
    • A.K. Lappi, and L.W. Ruddock Reexamination of the role of interplay between glutathione and protein disulfide isomerase J. Mol. Biol. 409 2011 238 249
    • (2011) J. Mol. Biol. , vol.409 , pp. 238-249
    • Lappi, A.K.1    Ruddock, L.W.2
  • 32
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulphide-bond formation
    • J.W. Cuozzo, and C.A. Kaiser 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
  • 34
    • 0036186384 scopus 로고    scopus 로고
    • Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum
    • A. Fassio, and R. Sitia Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum Histochem. Cell Biol. 117 2002 151 157
    • (2002) Histochem. Cell Biol. , vol.117 , pp. 151-157
    • Fassio, A.1    Sitia, R.2
  • 35
    • 75649114551 scopus 로고    scopus 로고
    • Mechanism and components of endoplasmic reticulum-associated degradation
    • J. Hoseki, R. Ushioda, and K. Nagata Mechanism and components of endoplasmic reticulum-associated degradation J. Biochem. 147 2010 19 25
    • (2010) J. Biochem. , vol.147 , pp. 19-25
    • Hoseki, J.1    Ushioda, R.2    Nagata, K.3
  • 36
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • S.S. Vembar, and J.L. Brodsky 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
  • 37
    • 4544249202 scopus 로고    scopus 로고
    • Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway
    • S. Chakravarthi, and N.J. Bulleid Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway J. Biol. Chem. 279 2004 39872 39879
    • (2004) J. Biol. Chem. , vol.279 , pp. 39872-39879
    • Chakravarthi, S.1    Bulleid, N.J.2
  • 39
    • 79959393858 scopus 로고    scopus 로고
    • Modeling and measuring intracellular fluxes of secreted recombinant protein in Pichia pastoris with a novel 34S labeling procedure
    • M. Pfeffer, M. Maurer, G. Kollensperger, S. Hann, A.B. Graf, and D. Mattanovich Modeling and measuring intracellular fluxes of secreted recombinant protein in Pichia pastoris with a novel 34S labeling procedure Microb. Cell Fact. 10 2011 47
    • (2011) Microb. Cell Fact. , vol.10 , pp. 47
    • Pfeffer, M.1    Maurer, M.2    Kollensperger, G.3    Hann, S.4    Graf, A.B.5    Mattanovich, D.6
  • 40
    • 0034281801 scopus 로고    scopus 로고
    • Effect of PDI overexpression on recombinant protein secretion in CHO cells
    • R. Davis, K. Schooley, B. Rasmussen, J. Thomas, and P. Reddy Effect of PDI overexpression on recombinant protein secretion in CHO cells Biotechnol. Prog. 16 2000 736 743
    • (2000) Biotechnol. Prog. , vol.16 , pp. 736-743
    • Davis, R.1    Schooley, K.2    Rasmussen, B.3    Thomas, J.4    Reddy, P.5
  • 41
    • 77956334107 scopus 로고    scopus 로고
    • Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum
    • T.J. Tavender, and N.J. Bulleid Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum Antioxid. Redox Signal. 13 2010 1177 1187
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1177-1187
    • Tavender, T.J.1    Bulleid, N.J.2
  • 42
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells
    • A. Mezghrani, A. Fassio, A. Benham, T. Simmen, I. Braakman, and R. Sitia Manipulation of oxidative protein folding and PDI redox state in mammalian cells EMBO J. 20 2001 6288 6296
    • (2001) EMBO J. , vol.20 , pp. 6288-6296
    • Mezghrani, A.1    Fassio, A.2    Benham, A.3    Simmen, T.4    Braakman, I.5    Sitia, R.6
  • 43
    • 0033213605 scopus 로고    scopus 로고
    • Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • A.R. Frand, and C.A. Kaiser 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
  • 44
    • 77953313165 scopus 로고    scopus 로고
    • Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum
    • E. Vitu, S. Kim, C.S. Sevier, O. Lutzky, N. Heldman, M. Bentzur, T. Unger, M. Yona, C.A. Kaiser, and D. Fass Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum J. Biol. Chem. 285 2010 18155 18165
    • (2010) J. Biol. Chem. , vol.285 , pp. 18155-18165
    • Vitu, E.1    Kim, S.2    Sevier, C.S.3    Lutzky, O.4    Heldman, N.5    Bentzur, M.6    Unger, T.7    Yona, M.8    Kaiser, C.A.9    Fass, D.10
  • 45
    • 0842266604 scopus 로고    scopus 로고
    • Oxidative protein folding in eukaryotes: Mechanisms and consequences
    • B.P. Tu, and J.S. Weissman Oxidative protein folding in eukaryotes: mechanisms and consequences J. Cell Biol. 164 2004 341 346
    • (2004) J. Cell Biol. , vol.164 , pp. 341-346
    • Tu, B.P.1    Weissman, J.S.2
  • 46
    • 34147126077 scopus 로고    scopus 로고
    • Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1
    • C.S. Sevier, H. Qu, N. Heldman, E. Gross, D. Fass, and C.A. Kaiser Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1 Cell 129 2007 333 344
    • (2007) Cell , vol.129 , pp. 333-344
    • Sevier, C.S.1    Qu, H.2    Heldman, N.3    Gross, E.4    Fass, D.5    Kaiser, C.A.6
  • 47
    • 71549132149 scopus 로고    scopus 로고
    • Protein disulfide isomerase: A critical evaluation of its function in disulfide bond formation
    • F. Hatahet, and L.W. Ruddock Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation Antioxid. Redox Signal. 11 2009 2807 2850
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 2807-2850
    • Hatahet, F.1    Ruddock, L.W.2
  • 50
    • 78650031117 scopus 로고    scopus 로고
    • Oxidative protein folding in the secretory pathway and redox signaling across compartments and cells
    • E. Margittai, and R. Sitia Oxidative protein folding in the secretory pathway and redox signaling across compartments and cells Traffic 12 2011 1 8
    • (2011) Traffic , vol.12 , pp. 1-8
    • Margittai, E.1    Sitia, R.2
  • 52
    • 35448965117 scopus 로고    scopus 로고
    • Transcriptomics-based identification of novel factors enhancing heterologous protein secretion in yeasts
    • B. Gasser, M. Sauer, M. Maurer, G. Stadlmayr, and D. Mattanovich Transcriptomics-based identification of novel factors enhancing heterologous protein secretion in yeasts Appl. Environ. Microbiol. 73 2007 6499 6507
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 6499-6507
    • Gasser, B.1    Sauer, M.2    Maurer, M.3    Stadlmayr, G.4    Mattanovich, D.5
  • 53
    • 42549132542 scopus 로고    scopus 로고
    • Hypoxic fed-batch cultivation of Pichia pastoris increases specific and volumetric productivity of recombinant proteins
    • K. Baumann, M. Maurer, M. Dragosits, O. Cos, P. Ferrer, and D. Mattanovich Hypoxic fed-batch cultivation of Pichia pastoris increases specific and volumetric productivity of recombinant proteins Biotechnol. Bioeng. 100 2008 177 183
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 177-183
    • Baumann, K.1    Maurer, M.2    Dragosits, M.3    Cos, O.4    Ferrer, P.5    Mattanovich, D.6
  • 54
    • 0021369651 scopus 로고
    • Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces
    • J.V. Kilmartin, and A.E. Adams Structural rearrangements of tubulin and actin during the cell cycle of the yeast Saccharomyces J. Cell Biol. 98 1984 922 933
    • (1984) J. Cell Biol. , vol.98 , pp. 922-933
    • Kilmartin, J.V.1    Adams, A.E.2
  • 55
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae
    • O.W. Rossanese, J. Sonderholm, B.J. Bevis, I.B. Sears, J. O'Connor, E.K. Williamson, and B.S. Glick Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae J. Cell Biol. 145 1999 69 81
    • (1999) J. Cell Biol. , vol.145 , pp. 69-81
    • Rossanese, O.W.1    Sonderholm, J.2    Bevis, B.J.3    Sears, I.B.4    O'Connor, J.5    Williamson, E.K.6    Glick, B.S.7


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