ERp28, a human endoplasmic-reticulum-lumineal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif

European Journal of Biochemistry

Volumn 255, Issue 3, 1998, Pages 570-579

  Ferrari, David M ^a   Van Nguyen, Phuc ^a   Kratzin, Hartmut D ^b   Söling, Hans Dieter ^a,c  

^a UNIVERSITY OF GÖTTINGEN   (Germany)

^b MAX PLANCK INSTITUTE OF EXPERIMENTAL MEDICINE   (Germany)

^c MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

Endoplasmic reticulum; ERp28; ERp29; Protein disulfide isomerse; Thioredoxin

Indexed keywords

PROTEIN DISULFIDE ISOMERASE;

AMINO ACID SEQUENCE; ARTICLE; CELL FRACTIONATION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; HUMAN; HUMAN TISSUE; NORMAL HUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FAMILY; PROTEIN ISOLATION; SEQUENCE ANALYSIS;

EID: 0032146759     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2550570.x     Document Type: Article

References (48)

1. Fischer, G., Bang, H. & Mech, C. (1984) Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides, Biomed. Biochim. Acta 43, 1101-1111.
2. Haas, I. G. & Wabl, M. (1983) Immunoglobulin heavy chain binding protein, Nature 306, 387-389.
3. Rothman, J. E. (1989) Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells, Cell 59, 591-601.
4. Goldberger, R. F., Epstein, C. J. & Anfinsen, C. B. (1963) Acceleration of reactivation of reduced bovine pancreatic ribonuclease by a microsomal system from rat liver, J. Biol. Chem. 238, 628-635.
5. Edman, J., Ellis, L., Blacher, R., Rorh, R. & Rutter, W. (1985) Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin, Nature 317, 267-270.
6. Freedman, R. B., Hirst, T. & Tuite, M. (1994) Protein disulfide isomerase: building bridges in protein folding, TIBS 19, 331-336.
7. Noiva, R. & Lennarz, W. J. (1992) Protein disulfide isomerase, J. Biol. Chem. 267, 3553-3556.
8. Freedman, R. B. (1995) The formation of disulfide bonds, Curr. Opin. Struct. Biol. 5, 85-91.
9. Holmgren, A. (1985) Thioredoxin, Annu. Rev. Biochem. 54, 237-271.
10. Urade, R. & Kito, M. (1992) Inhibition by acidic phospholipids of protein degradation by ER-60 protease, a novel cysteine protease, of the endoplasmic reticulum, FEBS Lett. 312, 83-86.
11. Chauduri, M., Tonin, P., Lewis, W. & Srinivasan, P. (1992) The geneton a novel protein, a member of the protein disulfide isomerase/ form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells, Biochem. J. 281, 645-650.
12. Nguyen Van, P., Peter, F. & Söling, H.-D. (1989) Four intracisternal calcium-binding glycoproteins from rat liver microsomes with high affinity for calcium, J. Biol. Chem. 264, 17494-17501.
13. Füllekrug, J., Sönnischen, B., Wünsch, U., Arseven, K., Nguyen Van, P., Söling, H.-D. & Mieskes, G. (1994) 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, 2719-2727.
14. Mazzarella, R., Srinivasan, M., Haugejorden, M. & Green, M. (1990) ERp72, an abundant lumenal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase, J. Biol. Chem. 265, 1094-1101.
15. Nguyen Van, P., Rupp, K., Lampen, A. & Söling, H.-D. (1993) CaBP2 is a rat homologue of ERp72 with protein disulfide isomerase activity, Eur J. Biochem. 213, 789-795.
16. Noiva, R., Freedman, R. B. & Lennarz, W. J. (1993) Peptide binding to protein disulphide isomerase occurs at a site distinct from the active sites, J. Biol. Chem. 268, 19210-19217.
17. LaMantia, M. L. & Lennarz, W. J. (1993) The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity, Cell 74, 899-908.
18. Cai, H., Wang, C. C. & Tsou, C.-L. (1994) Chaperone-like activity of protein disulfide isomerase in the refolding of a protein with no disulfide bonds, J. Biol. Chem. 269, 24550-24552.
19. Yaou, Y., Zhou, Y. & Wang, C.-C. (1997) Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2, EMBO J. 16, 651-658.
20. Reddy, P., Sparvoli, A., Fagioli, C., Fassina, G. & Sitia, R. (1996) Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains, EMBO J. 15, 2077-2085.
21. Demmer, J., Zhou, M. C. & Hubbard, M. J. (1997) Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum, FEBS Lett. 402, 145-150.
22. Mkrtchian, S., Fang, C., Hellman, U. & Ingelman-Sundberg, M. (1998) A stress-inducible rat liver endoplasmic reticulum protein. Erp29, Eur. J. Biochem. 251, 304-313.
23. Kemmink, J., Darby, J., Dijkstra, K., Nilges, M. & Creighton, T. E. (1997) The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules, Curr. Biol. 7, 239-245.
24. Vaux, D., Tooze, J. & Fuller, S. (1990) Identification by anti-idiotype antibodies of an intracellular membrane protein that recognizes a mammalian endoplasmic reticulum retention signal, Nature 345, 495-502.
25. Majoul, I. V., Bastiaens, P. I. H. & Söling, H.-D. (1996) Transport of an external Lys-Asp-Glu-Leu (KDEL) protein from the plasma membrane to the endoplasmic reticulum: studies with cholera toxin in Vero cells. Cell Biol. 133, 777-789.
26. Steinbuch, M. & Audran, R. (1969) The isolation of IgG from mammalian sera with the aid of caprylic acid, Arch. Biochem. Biophys. 134, 279-284.
27. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989) Molecular cloning: a laboratory manual, 2nd edn, Cold Spring Harbour Laboratory, Cold Spring Harbour NY.
28. Anderson, S., Davis, D. L., Dahlbaeck, H., Jörnvall, H. & Russell, D. W. (1989) Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme, J. Biol. Chem. 264, 8222-8229.
29. Hennecke, J., Spleiss, C. & Glockshuber, R. (1997) Influence of acidic residues and the kink in the active-site helix on the properties of the disulfide oxidoreductase DsbA, J. Biol. Chem. 272, 189-195.
30. Fleischer, S. & Kervina, M. (1974) Subcellular fractionation of rat liver, Methods Enzymol. 31, 6-41.
31. Tagaya, M., Wilson, D. W., Brunner, M., Arango, N. & Rothman, J. E. (1993) Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport, J. Biol. Chem. 268, 2662-2666.
32. Kassenbrock, C. K. & Kelly, R. B. (1989) Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides, EMBO J. 8, 1461-1467.
33. Gaut, J. R. & Hendershot, L. M. (1993) Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain, J. Biol. Chem. 268, 7248-7255.
34. Gribskov, M. & Burgess, R. R. (1986) Sigma factors from E. coli, B. subtilis, phage SP01, and phage T4 are homologous proteins, Nucleic Acids Res. 14, 6745-63.
35. Kozutsumi, Y., Segal, M., Normington, K., Gething, M.-J. & Sambrook, J. (1988) The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins, Nature 332, 462-464.
36. Kim, Y. K., Kim, K. S. & Lee, A. S. (1987) Regulation of the glucose-regulated protein genes by beta-mercaptoethanol requires de nova protein synthesis and correlates with inhibition of protein glycosylation, J. Cell Physiol. 133, 553-559.
37. Dorner, A. J., Wasley, L. C., Raney, P., Haugejorden, S., Green, M. & Kaufman, R. J. (1990) The stress response in Chinese hamster ovary cells. Regulation of ERp72 and protein disulfide isomerase expression and secretion, J. Biol. Chem. 265, 22029-22034.
38. Volkmer, J., Guth, S., Nastainczyk, W., Knippel, P., Klappa, P., Gnau, V. & Zimmermann, R. (1997) Pancreas specific protein disulfide isomerase, PDIp, is in transient contact with secretory proteins during late stages of translocation, FEBS Lett. 406, 291-295.
39. Oliver, J. D., van der Wal, F., Bulleid, N. J. & High, S. (1997) Interaction of thiol-dependent reductase ERp57 with nascent glycoproteins, Science 275, 86-88.
40. Kuznetsov, G., Chen, L. B. & Nigam, S. K. (1997) Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum, J. Biol. Chem. 272, 3057-3063.
41. Hammond, C. & Helenius, A. (1995) Quality control in the secretory pathway, Curr. Opin. Cell Biol. 7, 523-529.
42. Tatu, U., Hammond, C. & Helenius, A. (1995) Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment, EMBO J. 14, 1340-1348.
43. Katti, S. K., LeMaster, D. M. & Eklund, H. (1990) Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution, J. Mol. Biol. 212, 167-184.
44. Martin, J. L., Bardwell, J. C. & Kuriyan, J. (1993) Crystal structure of the DsbA protein required for disulphide bond formation in vivo, Nature 365, 464-468.
45. Eklund, H., Gleason, F. K. & Holmgren, A. (1991) Structural and functional relations among thioredoxins of different species, Proteins Struct. Funct. Genet. 11, 13-28.
46. Rodan, A. R., Simons, J. F., Trombetta, E. S. & Helenius, A. (1996) N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin, EMBO J. 15, 6921-6930.
47. Zapun, A., Petrescu, S. M., Rudd, P. M., Dwek, R. A., Thomas, D. Y. & Bergeron, J. J. (1997) Conformation-independent binding of monoglucosylated ribonuclease B to calnexin, Cell 88, 29-38.
48. Allen, S. & Bulleid, N. J. (1997) Calnexin and calreticulin bind to enzymatically active tissue-type plasminogen activator during biosynthesis and are not required for folding to the native state, Biochem. J. 328, 113-119.