Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases

Biochemical Journal

Volumn 461, Issue 1, 2014, Pages 107-113

  Shepherd, Colin ^a   Oka, Ojore B V ^a   Bulleid, Neil J ^a  

^a UNIVERSITY OF GLASGOW   (United Kingdom)

Author keywords

Disulfide formation; Endoplasmic reticulum; Endoplasmic reticulum oxidase 1 (Ero1); Protein disulfide isomerase (PDI); Protein folding

Indexed keywords

DISULFIDE; ENDOPLASMIC RETICULUM OXIDASE 1ALPHA; ENDOPLASMIC RETICULUM RESIDENT PROTEIN 46; HYDROGEN PEROXIDE; OXIDIZING AGENT; OXIDOREDUCTASE; OXYGEN; PROTEIN DISULFIDE ISOMERASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME MECHANISM; ENZYME METABOLISM; NONHUMAN; OXYGEN CONCENTRATION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM;

CATALYSIS; ENZYME ACTIVATION; HUMANS; MEMBRANE GLYCOPROTEINS; OXIDOREDUCTASES; PROTEIN DISULFIDE-ISOMERASES; SUBSTRATE SPECIFICITY;

EID: 84902338966     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20140234     Document Type: Article

References (20)

1. Hatahet, F. and Ruddock, L. W. (2007) Substrate recognition by the protein disulfide isomerases. FEBS J. 274, 5223-5234 CrossRef PubMed (Pubitemid 47512369)
2. Bulleid, N. J. and Ellgaard, L. (2011) Multiple ways to make disulfides. Trends Biochem. Sci. 36, 485-492 CrossRef PubMed
3. Tavender, T. J. and Bulleid, N. J. (2010) Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum. Antioxid. Redox Signal. 13, 1177-1187 CrossRef PubMed
4. Appenzeller-Herzog, C., Riemer, J., Christensen, B., Sorensen, E. S. and Ellgaard, L. (2008) A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells. EMBO J. 27, 2977-2987 CrossRef PubMed
5. Baker, K. M., Chakravarthi, S., Langton, K. P., Sheppard, A. M., Lu, H. and Bulleid, N. J. (2008) Low reduction potential of Ero1α regulatory disulphides ensures tight control of substrate oxidation. EMBO J. 27, 2988-2997 CrossRef PubMed
6. Inaba, K., Masui, S., Iida, H., Vavassori, S., Sitia, R. and Suzuki, M. (2010) Crystal structures of human Ero1alpha reveal the mechanisms of regulated and targeted oxidation of PDI. EMBO J. 29, 3330-3343 CrossRef PubMed
7. Chambers, J. E., Tavender, T. J., Oka, O. B. V., Warwood, S., Knight, D. and Bulleid, N. J. (2010) The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α. J. Biol. Chem. 285, 29200-29207 CrossRef PubMed
8. Wang, L., Li, S. J., Sidhu, A., Zhu, L., Liang, Y., Freedman, R. B. and Wang, C. C. (2009) Reconstitution of human Ero1-Lα/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a′ domains of protein-disulfide isomerase. J. Biol. Chem. 284, 199-206 CrossRef PubMed
9. Sevier, C. S., Qu, H., Heldman, N., Gross, E., Fass, D. and Kaiser, C. A. (2007) Modulation of cellular disulfide-bond formation and the ER redox environment by feedback regulation of Ero1. Cell 129, 333-344 CrossRef PubMed (Pubitemid 46574965)
10. Kim, S., Sideris, D. P., Sevier, C. S. and Kaiser, C. A. (2012) Balanced Ero1 activation and inactivation establishes ER redox homeostasis. J. Cell Biol. 196, 713-725 CrossRef PubMed
11. Heldman, N., Vonshak, O., Sevier, C. S., Vitu, E., Mehlman, T. and Fass, D. (2010) Steps in reductive activation of the disulfide-generating enzyme Ero1p. Protein Sci. 19, 1863-1876 CrossRef PubMed
12. Tu, B. P., Ho-Schleyer, S. C., Travers, K. J. and Weissman, J. S. (2000) Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290, 1571-1574 CrossRef PubMed
13. Araki, K., Iemura, S., Kamiya, Y., Ron, D., Kato, K., Natsume, T. and Nagata, K. (2013) Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases. J. Cell Biol. 202, 861-874 CrossRef PubMed
14. Araki, K. and Nagata, K. (2011) Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway. J. Biol. Chem. 286, 32705-32712 CrossRef PubMed
15. Nguyen, V. D., Wallis, K., Howard, M. J., Haapalainen, A. M., Salo, K. E., Saaranen, M. J., Sidhu, A., Wierenga, R. K., Freedman, R. B., Ruddock, L. W. and Williamson, R. A. (2008) Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b′ domain. J. Mol. Biol. 383, 1144-1155 CrossRef PubMed
16. Masui, S., Vavassori, S., Fagioli, C., Sitia, R. and Inaba, K. (2011) Molecular bases of cyclic and specific disulfide interchange between human ERO1α protein and protein-disulfide isomerase (PDI). J. Biol. Chem. 286, 16261-16271 CrossRef PubMed
17. Gross, E., Sevier, C. S., Heldman, N., Vitu, E., Bentzur, M., Kaiser, C. A., Thorpe, C. and Fass, D. (2006) Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc. Natl. Acad. Sci. U.S.A. 103, 299-304 CrossRef PubMed (Pubitemid 43122395)
18. 2-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol. Cell 10, 983-994 CrossRef PubMed
19. Tavender, T. J., Sheppard, A. M. and Bulleid, N. J. (2008) Peroxiredoxin IV is an endoplasmic reticulum-localized enzyme forming oligomeric complexes in human cells. Biochem. J. 411, 191-199 CrossRef PubMed (Pubitemid 351482361)
20. Nguyen, V. D., Saaranen, M. J., Karala, A. R., Lappi, A. K., Wang, L., Raykhel, I. B., Alanen, H. I., Salo, K. E., Wang, C. C. and Ruddock, L. W. (2011) Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation. J. Mol. Biol. 406, 503-515 CrossRef PubMed