Reexamination of the role of interplay between glutathione and protein disulfide isomerase

Journal of Molecular Biology

Volumn 409, Issue 2, 2011, Pages 238-249

  Lappi, Anna Kaisa ^a   Ruddock, Lloyd W ^a  

^a UNIVERSITY OF OULU   (Finland)

Author keywords

disulfide bond formation; oxidation; PDI; reduction; stopped flow kinetics

Indexed keywords

CYSTEINE; FUNGAL PROTEIN; GLUTATHIONE; GLUTATHIONE DISULFIDE; PROTEIN DISULFIDE ISOMERASE; PROTEIN PDI1P; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL REACTION; DISULFIDE BOND; ENZYME ACTIVE SITE; NONHUMAN; OXIDATION KINETICS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; REDUCTION;

EID: 79955878526     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.03.024     Document Type: Article

References (36)

1. Freedman R.B. Native disulphide bond formation in biosynthesis: evidence for the role of protein disulphide isomerase TIBS 9 1984 438 441
2. Freedman R.B., Klappa P., and Ruddock L.W. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains EMBO Rep. 3 2002 136 140 (Pubitemid 34213490)
3. Ellgaard L., and Ruddock L.W. The human protein disulphide isomerase family: substrate interactions and functional properties EMBO Rep. 6 2005 28 32 (Pubitemid 41710070)
4. Hatahet F., and Ruddock L.W. Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation Antioxid. Redox Signal. 11 2009 2807 2850
5. Freedman R.B. The formation of protein disulphide bonds Curr. Opin. Struct. Biol. 5 1995 85 91
6. Cumming R.C., Andon N.L., Haynes P.A., Park M., Fischer W.H., and Schubert D. Protein disulfide bond formation in the cytoplasm during oxidative stress J. Biol. Chem. 279 2004 21749 21758 (Pubitemid 38679361)
7. Saurin A.T., Neubert H., Brennan J.P., and Eaton P. Widespread sulfenic acid formation in tissues response to hydrogen peroxide Proc. Natl Acad. Sci. USA 101 2004 17982 17987 (Pubitemid 40054061)
8. Bánhegyi G., Marcolongo P., Puskás F., Fulceri R., Mandl J., and Benedetti A. Dehydroascorbate and ascorbate transport in rat liver microsomal vesicles J. Biol. Chem. 279 1998 39872 39879
9. Bánhegyi G., Csala M., Nagy G., Sorrentino V., Fulceri R., and Benedetti A. Evidence for the transport of glutathione through ryanodine receptor channel type I Biochem. J. 376 2003 807 812 (Pubitemid 38058082)
10. Saaranen M.J., Karala A.R., Lappi A. -K., and Ruddock L.W. The role of dehydroascorbate in disulfide bond formation Antioxid. Redox Signal. 12 2010 15 25
11. Ferrari D.M., and Söling H.D. The protein disulphide-isomerase family: unraveling a string of folds Biochem. J. 339 1999 1 10 (Pubitemid 29179283)
12. Frand A.R., and 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 (Pubitemid 128378657)
13. Pollard M.G., Travers K.J., and Weissman J.S. Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum Mol. Cell 1 1998 171 182 (Pubitemid 128378658)
14. Frand A.R., and Kaiser C.A. The Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum Mol. Cell 4 1999 469 477 (Pubitemid 29531127)
15. Tu B.P., Ho-Schleyer S.C., Travers K.J., and Weissman J.S. Biochemical basis of oxidative protein folding in the endoplasmic reticulum Science 290 2000 1571 1574
16. Gross E., Sevier C.S., Heldman N., Vitu E., Bentzur M., and Kaiser C.A. Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic thiol oxidase Ero1p Proc. Natl Acad. Sci. 103 2006 299 304 (Pubitemid 43122395)
17. Sevier C.S., Qu H., Heldman N., Gross E., Fass D., and Kaiser C.A. Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1 Cell 129 2007 333 344 (Pubitemid 46574965)
18. Zito E., Chin K.T., Blais J., Harding H.P., and Ron D. ERO1-β, a pancreas-specific disulfide oxidase, promotes insulin biogenesis and glucose homeostasis J. Cell Biol. 188 2010 821 832
19. Darby N.J., and Creighton T.E. Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase Biochemistry 34 1995 16770 16780 (Pubitemid 26011802)
20. Jessop C.E., and Bulleid N.J. Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells J. Biol. Chem. 279 2004 55341 55347 (Pubitemid 40066532)
21. Karala A. -R., Lappi A. -K., Saaranen M.J., and Ruddock L.W. Efficient peroxide mediated oxidative folding of protein at physiological pH and implications for oxidative folding in the endoplasmic reticulum Antioxid. Redox Signal. 11 2009 963 970
22. Lappi A. -K., Lensink M., Alanen H.I., Salo K.E.H., Lobell M., Juffer A., and Ruddock L.W. A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases J. Mol. Biol. 335 2004 283 295 (Pubitemid 37494979)
23. Ruddock L.W., Hirst T.R., and Freedman R.B. pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate Biochem. J. 315 1996 1001 1005 (Pubitemid 26147634)
24. Chakravarthi S., and Bulleid N.J. Glutathione is required to regulate the formation of native disulphide bonds within proteins entering the secretory pathway J. Biol. Chem. 279 2004 39872 39879 (Pubitemid 39258259)
25. Molteni S.N., Fassio A., Ciriolo M.R., Filomeni G., Pasqualetto E., Fagiolo C., and Sitia R. Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum J. Biol. Chem. 279 2004 32667 32673 (Pubitemid 39014725)
26. Hwang C., Sinskey A.J., and Lodish H.F. Oxidized redox state of glutathione in the endoplasmic reticulum Science 257 1992 1496 1502
27. Bass R., Ruddock L.W., Klappa P., and Freedman R.B. A major fraction of endoplasmic reticulum-located glutathione is present as mixed-disulfides with protein J. Biol. Chem. 279 2004 5257 5262 (Pubitemid 38220545)
28. Appenzeller-Herzog C., Riemer J., Zito E., Chin K. -T., Ron D., Spiess M., and Ellgaard L. Disulphide production by Ero1α-PDI relay is rapid and effectively regulated EMBO J. 29 2010 3318 3329
29. Cuozzo J.W., and Kaiser C.A. Competition between glutathione and protein thiols for disulphide-bond formation Nat. Cell Biol. 1 1999 130 135 (Pubitemid 129656016)
30. Delic M., Mattanovich D., and Gasser B. Monitoring intracellular redox conditions in the endoplasmic reticulum of living yeasts FEMS Microbiol. Lett. 306 2010 61 66
31. a allows PDI to act both as a catalyst of disulfide bond formation and isomerization J. Mol. Biol. 396 2010 883 892
32. Kadokura H., Tian H., Zander T., Bardwell J.C., and Beckwith J. Snapshots of DsbA in action: detection of proteins in the process of oxidative folding Science 303 2004 534 537 (Pubitemid 38120853)
33. Jessop C.E., Chakravarthi S., Garbi N., Hämmerling G.J., Lovell S., and Bulleid N.J. ERp57 is essential for efficient folding of glycoproteins sharing common structural domains EMBO J. 26 2007 28 40 (Pubitemid 46094697)
34. Hatahet F., and Ruddock L.W. Substrate recognition by the protein disulfide isomerases FEBS J. 274 2007 5223 5234 (Pubitemid 47512369)
35. Saaranen M.J., Salo K.E.H., Latva-Ranta M.K., Kinnula V.L., and Ruddock L.W. The C-terminal active site cysteine of Escherichia coli glutaredoxin 1 determines the glutathione specificity of the second step of peptide deglutathionylation Antioxid. Redox Signal. 11 2009 1819 1828
36. Alanen H.I., Salo K.E.H., Pekkala M., Siekkinen H.M., Pirneskoski A., and Ruddock L.W. Defining the domain boundaries of the human protein disulphide isomerases Antioxid. Redox Signal. 5 2003 367 377