The human protein disulphide isomerase family: Substrate interactions and functional properties

EMBO Reports

Volumn 6, Issue 1, 2005, Pages 28-32

  Ellgaard, Lars ^a   Ruddock, Lloyd W ^b  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF OULU   (Finland)

Author keywords

Disulphide bond formation; Endoplasmic reticulum; Protein disulphide isomerase; Protein folding; Thiol disulphide oxidoreductase

Indexed keywords

ALPHA 1 ANTITRYPSIN; CALRETICULIN; CELL PROTEIN; CYSTEINE; MEMBRANE PROTEIN; PROTEIN DISULFIDE ISOMERASE; SOMATOSTATIN; THIOREDOXIN;

AMINO ACID SEQUENCE; DISULFIDE BOND; ENZYME SUBSTRATE COMPLEX; HUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN INTERACTION; REVIEW; SEQUENCE ALIGNMENT; CHEMISTRY; CLASSIFICATION; ENZYME SPECIFICITY; METABOLISM; MOLECULAR GENETICS;

EUKARYOTA;

AMINO ACID SEQUENCE; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN DISULFIDE-ISOMERASE; SUBSTRATE SPECIFICITY; THIOREDOXIN;

EID: 14044271131     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/sj.embor.7400311     Document Type: Review

References (36)

1. Alanen HI, Williamson RA, Howard MJ, Lappi AK, Jäntti HP, Rautio SM, Kellokumpu S, Ruddock LW (2003) Functional characterisation of ERp18, a new endoplasmic reticulum located thioredoxin superfamily member. J Biol Chem 278: 28912-28920
2. Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R (2002) ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J 21: 835-844
3. Anelli T, Alessio M, Bachi A, Bergamelli L, Bertoli G, Camerini S, Mezghrani A, Ruffato E, Simmen T, Sitia R (2003) Thiol-mediated protein retention in the endoplasmic reticulum: the role of Erp44. EMBO J 22: 5015-5022
4. Barnewitz K, Guo C, Sewana M, Ma Q, Sheldrick GM, Söling H-D, Ferrari DM (2004) Mapping of a substrate-binding site in the protein disulfide isomerase-related chaperone Wind based on protein function and crystal structure. J Biol Chem 279: 39829-39837
5. Cunnea PM et al (2003) ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress. J Biol Chem 278: 1059-1066
6. Darby NJ, Penka E, Vincentelli R (1998) The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency. J Mol Biol 276: 239-247
7. Dyson HJ, Jeng MF, Tennant LL, Slaby I, Lindell M, Cui DS, Kuprin S, Holmgren A (1997) Effects of buried charged groups on cysteine thiol ionization and reactivity in Escherichia coli thioredoxin: structural and functional characterization of mutants of Asp 26 and Lys 57. Biochemistry 36: 2622-2636
8. Ellgaard L, Riek R, Herrmann T, Güntert P, Braun D, Helenius A, Wuthrich K (2001) NMR structure of the calreticulin P-domain. Proc Natl Acad Sci USA 98: 3133-3138
9. Ferrari DM, Söling HD (1999) The protein disulphide-isomerase family: unraveling a string of folds. Biochem J 339: 1-10
10. Freedman RB, Klappa P, Ruddock LW (2002) Catalytic and binding domains in the mechanism and specificty of protein disulphide isomerases: a theme with variations. EMBO Rep 3: 136-140
11. Frickel E-M, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L (2002) TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc Natl Acad Sci USA 99: 1954-1959
12. Frickel E-M et al (2004) ERp57 is a multifunctional thiol-disulfide oxidoreductase. J Biol Chem 279: 18277-18287
13. Horibe T, Gomi M, Iguchi D, Ito H, Kitamura Y, Masuoka T, Tsujimoto I, Kimura T, Kikuchi M (2004) Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding. J Biol Chem 279: 4604-4611
14. Hosoda A, Kimata Y, Tsuru A, Kohno K (2003) JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs. J Biol Chem 278: 2669-2676
15. Kemmink J, Darby ND, Dijkstra K, Nilges M, Creighton TE (1996) Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy. Biochemistry 35: 7684-7691
16. Kemmink J, Darby ND, Dijkstra K, Nilges M, Creighton TE (1997) The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules. Curr Biol 7: 239-245
17. Klappa P, Ruddock LW, Darby NJ, Freedman RB (1998) 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: 927-935
18. Knoblach B, Keller BO, Groenendyk J, Aldred S, Zheng J, Lemire BD, Li L, Michalak M (2003) ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins. Mol Cell Proteomics 2: 1104-1119
19. Lappi AK, Lensink M, Alanen HI, Salo KEH, Lobell M, Juffer A, Ruddock LW (2004). A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases. J Mol Biol 335: 283-295
20. Matsuo Y, Akiyama N, Nakamura H, Yodoi J, Noda M, Kizaka-Kondoh S (2001) Identification of a novel thioredoxin-related transmembrane protein. J Biol Chem 276: 10032-10038
21. Meng X, Zhang C, Chen J, Peng S, Cao Y, Ying K, Xie Y, Mao Y (2003) Cloning and identification of a novel cDNA coding thioredoxin-related transmembrane protein 2. Biochem Genet 41: 99-106
22. Meunier L, Usherwood Y-K, Chung KT, Hendershot LM (2002). A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13: 4456-4469
23. Oliver JD, van der Wal FJ, Bulleid NJ, High S (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275: 86-88
24. Pirneskoski A, Klappa P, Lobell M, Williamson RA, Byrne L, Alanen HI, Salo KE, Kivirikko KI, Freedman RB, Ruddock LW (2004) Molecular characterisation of the principal substrate binding site of the ubiquitous folding catalyst protein disulphide isomerase. J Biol Chem 279: 10374-10381
25. Pollock S, Kozlov G, Pelletier M-F, Trempe J-F, Jansen G, Sitnikov D, Bergeron JJ, Gehring K, Ekiel I, Thomas DY (2004) Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system. EMBO J 23: 1020-1029
26. Ruddock LW, Freedman RB, Klappa P (2000) Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp. Protein Sci 9: 758-764
27. Rupp K, Birnbach U, Lundström J, Van Nguyen P, Soling H-D (1994) Effects of CaBP2, the rat analog of ERp72, and of CaBP1 on the refolding of denatured proteins: comparison with protein disulfide isomerase. J Biol Chem 269: 2501-2507
28. Russell SJ, Ruddock LW, Salo KEH, Oliver JD, Roebuck QP, Llewellyn DH, Roderick HL, Koivunen P, Myllyharju J, High S (2004) The primary substrate binding site in the b′ domain of ERp57 is adapted for ER lectin association. J Biol Chem 279: 18861-18869
29. Schwaller M, Wilkinson B, Gilbert HF (2003) Reduction-reoxidation cycles contribute to catalysis of disulfide isomerisation by protein-disulfide isomerase. J Biol Chem 278: 7154-7159
30. Silvennoinen L, Myllyharju J, Ruoppolo M, Orrù S, Caterino M, Kivirikko KI, Koivunen P (2004) Identification and characterisation of structural domains of human Erp57. Association with calreticulin requires several domains. J Biol Chem 279: 13607-13615
31. Sullivan DC, Huminiecki L, Moore JW, Boyle JJ, Poulsom R, Creamer D, Barker J, Bicknell R (2003) EndoPDI, a novel protein-disulfide isomerase-like protein that is preferentially expressed in endothelial cells acts as a stress survival factor. J Biol Chem 278: 47079-47088
32. Tu BP, Weissman JS (2004) Oxidative protein folding in eukaryotes: mechanisms and consequences. J Cell Biol 164: 341-346
33. Turano C, Coppari S, Altieri F, Ferraro A (2002) Proteins of the PDI family: unpredicted non-ER locations and functions. J Cell Physiol 193: 154-163
34. Urade R, Okudo H, Kato H, Moriyama T, Arakaki Y (2004) ER-60 domains responsible for interaction with calnexin and calreticulin. Biochemistry 43: 8858-8868
35. van Lith M, Hartigan N, Hatch J, Benham AM (2004) PDILT: a divergent testis-specific PDI with a non-classical SXXC motif that engages in disulfide dependent interactions in the endoplasmic reticulum. J Biol Chem [Epub ahead of print]
36. Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJM, Thomas DY (1998) Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with Erp57. J Biol Chem 273: 6009-6012