Although calnexin is essential in S. pombe, its highly conserved central domain is dispensable for viability

Journal of Cell Science

Volumn 112, Issue 23, 1999, Pages 4449-4460

  Elagöz, Aram ^a   Callejo, Mario ^a   Armstrong, John ^b   Rokeach, Luis A ^a  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

^b UNIVERSITY OF SUSSEX   (United Kingdom)

Author keywords

BiP; Chaperone; Protein folding; Schizosaccharomyces pombe; Yeast genetics

Indexed keywords

CALCIUM; CALNEXIN; DITHIOTHREITOL;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL STRUCTURE; CELL VIABILITY; CELL WALL; CONTROLLED STUDY; FUNGUS GROWTH; GENETIC CONSERVATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; SCHIZOSACCHAROMYCES POMBE; TEMPERATURE;

AMINO ACID SEQUENCE; ANIMALS; CALCIUM-BINDING PROTEINS; CALNEXIN; CELL WALL; CONSERVED SEQUENCE; HAPLOIDY; HUMANS; INTRACELLULAR MEMBRANES; MEMBRANE POTENTIALS; MICROSOMES; MOLECULAR SEQUENCE DATA; MUTAGENESIS; POLYMERASE CHAIN REACTION; RECOMBINANT PROTEINS; SCHIZOSACCHAROMYCES; SEQUENCE DELETION; SPHEROPLASTS;

FUNGI; MAMMALIA; SCHIZOSACCHAROMYCES POMBE;

EID: 0033490333     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (51)

1. Bergeron, J. J. M., Brenner, M. B., Thomas, D. Y. and Williams, D. B. (1994). Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Trends Biochem. Sci. 19, 124-128.
2. Braakman, I., Helenius, J. and Helenius, A. (1992). Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J. 11, 1717-1722.
3. Brodsky, J. L., Werner, E. D., Dubas, M. E., Goeckeler, J. L., Kruse, K. B. and McCracken, A. A. (1999). The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J. Biol. Chem. 274, 3453-3460.
4. Burke, J. D. and Gould, K. L. (1994). Molecular cloning and characterization of the Schizosaccharomyces pombe his3 gene for use as a selectable marker. Mol. Gen. Genet. 242, 169-176.
5. Crofts, A., Lebrogne-Castel, N., Pesca, M., Vitale, A. and Denecke, J. (1998). BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress. Plant Cell 10, 813-823.
6. Dean, N. (1995). Yeast glycosylation mutants are sensitive to aminoglycosides. Proc. Natl. Acad. Sci. USA 92, 1287-1291.
7. Elliott, J. G., Oliver, J. D. and High, S. (1997). The thiol-dependent reductase ERp57 interacts specifically with A-glycosylated integral proteins. J. Biol. Chem. 272, 13849-13855.
8. Fanchiotti, S., Fernandez, F., D'Alessio, C. and Parodi, A. J. (1998) The UDP-Glc:Glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress. J. Cell Biol. 143, 625-635.
9. Fernandez, F., D'Alessio, C., Fanchiotti, S. and Parodi, A. J. (1998). A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J. 17, 5877-5886.
10. Fernández, F. S., Jannatipour, M., Hellman, U., Rokeath, L. A. and Parodi, A. J. (1996). A new stress protein: Synthesis of Schzosaccharomyces pombe UDP-Glc:glycoprotein glucosyltransferase mRNA is induced by stress conditions but the enzyme is not essential for cell viability. EMBO J. 15, 705-713.
11. Fernández, F. S., Trombetta, S. E., Hellman, U. and Parodi, A. J. (1994). Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae. J. Biol. Chem. 269, 30701-30706.
12. Fernández, J., Soto, T., Vicente-Soler, J., Cansado, J. and Gacto, M. (1997). Osmo-stress-induced changes in neutral trehalase activity of the fission yeast Schizosaccharomyces pombe. Biochim. Biophys. Acta 1357, 41-48.
13. Gekko, K. and Timasheff, S. N. (1981). Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochem. 20, 4667-4676.
14. Hammond, C. and Helenius, A. (1994). Folding of VSV protein: sequential interaction with BiP and calnexin. Science 266, 456-458.
15. Higuchi, R. and Krummel, B. S. R. K. (1988). A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res. 16, 7351-7367.
16. Ishiguro, J., Saitou, A., Duran, A. and Ribas, J. C. (1997) cps I a Schizosaccharomyces pombe gene homolog of Saccharomyces cerevisiae FKS genes whose mutation confers hypersensitivity to cyclosporin A and papulacandin B. J. Bacteriol. 1977, 7653-7662.
17. Jannatipour, M., Callejo, M., Parodi, A. J., Armstrong, J. and Rokeach, L. A. (1998). Calnexin and BiP interact with acid phophatase independently of glucose trimming and reglucosylation in S. pombe. Biochemistry 37, 17253-17261.
18. Jannatipour, M. and Rokeach, L. A. (1995). The Schizosaccharomyces pombe homologue of the chaperone calnexin is essential for viability. J. Biol. Chem. 270, 4845-4853.
19. Keller, S. H., Lindstrom, J. and Taylor, P. (1998). Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the α-subunit of the nicotinic acetylcholine receptor. J. Biol. Chem. 273, 17064-17072.
20. Kim, P. S. and Arvan, P. (1995). Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J. Cell Biol. 128, 29-38.
21. Kültz, D., Garcia-Perez, A., Ferraris, J. D. and Burg, M. B. (1997). Distinct regulation of osmoprotective genes in yeast and mammals. J. Biol. Chem. 272, 13165-13170.
22. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Mature 227, 680-685.
23. 1-antitrypsin. J. Biol. Chem. 269, 7514-7519.
24. Loo, T. W. and Clarke, D. M. (1994). Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis. J. Biol. Chem. 269, 28683-28689.
25. Maundrell, K. (1993). Thiamine-repressible expression vectors pREP and pRIP for fission yeast. Gene 123, 127-130.
26. Moreno, S., Klar, A. and Nurse, P. (1991). Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. Meth. Enzymol. 194, 795-823.
27. Oliver, J. D., van der Wal, F. J., Bulleid, N. J. and High, S. (1997). Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275, 86-88.
28. Orlean, P. (1997). Biogenesis of yeast wall and surface components. In Cell Cycle and Cell Biology (ed. J. R. Pringle, J. R. Broach and E. W. Jones), pp. 229-362. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
29. + in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain. EMBO J. 14, 3064-3072.
30. Parodi, A. J. (1998). Reglucosylation of glycoproteins and quality control of glycoprotein folding in the endoplasmic reticulum of yeast cells. Biochim. Biophys. Acta 1426, 287-295.
31. Peterson, J. R. and Helenius, A. (1999). In vitro reconstitution of calreticulin-substrate interactions. J. Cell Sci. 112, 2775-2784.
32. Pidoux, A. L. and Armstrong, J. (1992). Analysis of the BiP and identification of an ER retention signal in Schizosaccharomyces pombe. EMBO J. 11, 1583-1591.
33. Pidoux, A. L. and Armstrong, J. (1993). The BiP protein and the endoplasmic reticulum of Schizosaccharomyces pombe: fate of the nuclear envelope during cell division. J. Cell Sci. 105, 1115-1120.
34. Pipe, S. W., Morris, J. A., Shah, J. and Kaufman, R. J. (1998). Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J. Biol. Chem. 273, 8537-8544.
35. Robinow, C. F. and Hyams, J. S. (1989). General cytology of fission yeast. In Molecular Biology of the Fission Yeast (ed. A. Nasim, P. Young and B. F. Johnson), pp. 273-330. London: Academic Press Limited.
36. Sambrook, J., Fritsch, E. F. and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
37. Sato, S., Ward, C. L., Krouse, M. E., Wine, J. J. and Kopito, R. R. (1996). Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J. Biol. Chem. 271, 635-638.
38. Scott, J. E. and Dawson, J. R. (1995). MHC class 1 expression and transport in a calnexin-deficient cell line. J. Immunol. 155, 143-148.
39. Shahinian, S., Dijkgraaf, G. J., Sdicu, A.-M., Thomas, D. Y., Jakob, C. A., Aebi, M. and Bussey, H. (1998). Involvement of protein N-glycosylation and processing in the biosynthesis of cell wall β-1,6-glucan of Saccharomyces cerevisiae. Genetics 149, 843-856.
40. Silberstein, S., Schlenstedt, G., Silver, P. A. and Gilmore, R. (1998). A role tor the DnaJ homologue Scjlp in protein folding in the yeast endoplasmic reticulum. J. Cell Biol. 143, 921-933.
41. Simons, J. F., Ebersold, M. and Helenius, A. (1998). Cell wall 1,6-β-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II and the molecular chaperone BiP/Kar2p. EMBO J. 17, 396-405.
42. Sousa, M. and Parodi, A. J. (1995). The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J. 14, 4196-4203.
43. Tatu, U. and Helenius, A. (1997). Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J. Cell Biol. 136, 555-565.
44. Tjoelker, L. W., Seyfried, C. E., Eddy, R. L., Jr., Byers, M. G., Shows, T. B., Calderon, J., Scheiber, R. B. and Gray, P. W. (1994). Human, mouse, and rat calnexin cDNA cloning: Identification of potential calcium binding motifs and gene localization to human chromosome 5. Biochemistry 33 3229-3236.
45. Trombetta, E. S. and Helenius, A. (1998). Lectins as chaperones in glycoprotein folding. Curr. Opin. Struct. Biol. 8, 587-592.
46. Vassilakos, A., Cohen-Doyle, M. F., Peterson, P. A., Jackson, M. R. and Williams, D. B. (1996). The molecular chaperone calnexin facilitates folding and assembly of class 1 histocompatibility molecules. EMBO J. 15, 1495-1506.
47. Vassilakos, A., Michalak, M., Lehrman, M. A. and Williams, D. B. (1998). Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 37, 3480-3490.
48. Wada, I., Rindress, D., Cameron, P. H., Ou, W. J., Doherty II, J. J., Louvard, D., Bell, A. W., Dignard, D., Thomas, D. Y. and Bergeron, J. J. M. (1991). SSRgamma and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane. J. Biol. Chem. 266, 19599-19610.
49. 2 Oligosaccharide as an Initial Step in Recognizing Unfolded Glycoproteins. J. Biol. Chem. 270, 4697-4704.
50. Williams, D. B. (1995). The Merck Frosst award lecture 1994: Calnexin, a molecular chaperone with a taste for carbohydrate. Biochem. Cell Biol 73, 123-132.
51. Zapun, A., Darby, N. J., Tessier, D. C., Michalak, M., Bergeron, J. J. M. and Thomas, D. Y. (1998). Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 273, 6009-6012.