Accumulation of misfolded protein aggregates leads to the formation of russell body-like dilated endoplasmic reticulum in yeast

Yeast

Volumn 13, Issue 11, 1997, Pages 1009-1020

  Umebayashi, Kyohei ^a   Hirata, Aiko ^a   Fukuda, Ryouichi ^a   Horiuchi, Hiroyuki ^a   Ohta, Akinori ^a   Takagi, Masamichi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

Chaperone; Endoplasmic reticulum; Saccharomyces cerevisiae; Unfolded protein response

Indexed keywords

ASPARTIC PROTEINASE; CHAPERONE; FUNGAL PROTEIN; FUNGAL RNA; GLUCOSE REGULATED PROTEIN; PROTEIN DISULFIDE ISOMERASE; RNAP 1; UNCLASSIFIED DRUG;

ARTICLE; CELL NUCLEUS MEMBRANE; CONTROLLED STUDY; ELECTRON MICROSCOPY; ENDOPLASMIC RETICULUM; IMMUNOFLUORESCENCE MICROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN SECRETION; PROTEIN SYNTHESIS; SACCHAROMYCES CEREVISIAE;

AMINO ACID SEQUENCE; ASPARTIC ENDOPEPTIDASES; CELL NUCLEUS; ENDOPLASMIC RETICULUM; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; FUNGAL PROTEINS; HSP70 HEAT-SHOCK PROTEINS; IMMUNOBLOTTING; MICROSCOPY, IMMUNOELECTRON; MOLECULAR CHAPERONES; PLASMIDS; PROTEIN CONFORMATION; PROTEIN DISULFIDE-ISOMERASE; RNA; SACCHAROMYCES CEREVISIAE; TRANSFORMATION, GENETIC;

FUNGI; RHIZOPUS NIVEUS; SACCHAROMYCES CEREVISIAE;

EID: 0030820146     PISSN: 0749503X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0061(19970915)13:11<1009::AID-YEA157>3.0.CO;2-K     Document Type: Article

References (42)

1. 2+ function independently in a cell-free protein transport reaction. Proc. Natl. Acad. Sci. USA 87, 355-359.
2. Blond-Elguindi, S., Cwirla, S. E., Dower, W. J., et al. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP. Cell 75, 717-728.
3. Cai, H., Wang, C.-C. and 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.
4. Cox, J. S., Shamu, C. E. and Walter, P. (1993). Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73, 1197-1206.
5. Dorner, A. J., Wasley, L. C., Raney, P., Haugejorden, S., Green, M. and Kaufman, R. J. (1990). The stress response in Chinese Hamster Ovary cells. J. Biol. Chem. 265, 22029-22034.
6. Franzusoff, A., Rothblatt, J. and Schekman, R. (1991). Analysis of polypeptide transit through yeast secretory pathway. Guide to yeast genetics and molecular biology. Methods Enzymol. 194, 662-674.
7. Fukuda, R., Horiuchi, H., Ohta, A. and Takagi, M. (1994). The prosequence of Rhizopus niveus aspartic proteinase-I supports correct folding and secretion of its mature part in Saccharomyces cerevisiae. J. Biol. Chem. 269, 9556-9561.
8. Fukuda, R., Umebayashi, K., Horiuchi, H., Ohta, A. and Takagi, M. (1996). Degradation of Rhizopus niveus aspartic proteinase-I with mutated prosequences occurs in the endoplasmic reticulum of Saccharomyces cerevisiae. J. Biol. Chem. 271, 14252-14255.
9. Gething, M.-J. and Sambrook, J. (1992). Protein folding in the cell. Nature 355, 33-45.
10. Helenius, A., Marquardt, T. and Braakman, I. (1992). The endoplasmic reticulum as a protein-folding compartment. Trends Cell Biol. 2, 227-231.
11. Horiuchi, H., Yanai, K., Okazaki, T., Takagi, M. and Yano, K. (1988). Isolation and sequencing of a genomic clone encoding aspartic proteinase of Rhizopus niveus. J. Bacteriol. 170, 272-278.
12. Horiuchi, H., Ashikari, T., Amachi, T., Yoshizumi, H., Takagi, M. and Yano, K. (1990). High-level secretion of a Rhizopus niveus aspartic proteinase in Saccharomyces cerevisiae. Agric. Biol. Chem. 54, 1771-1779.
13. Ito, H., Fukuda, Y., Murata, K. and Kimura, A. (1983). Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
14. Kohno, K., Normington, K., Sambrook, J., Gething, M.-J. and Mori, K. (1993). The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol. Cell Biol. 13, 877-890.
15. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
16. LaMantia, M. L., Miura, T., Tachikawa, H., Kaplan, H. A., Lennarz, W. J. and Mizunaga, T. (1991). Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast. Proc. Natl. Acad. Sci. USA 88, 4453-4457.
17. Lee, A. S. (1987). Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells. Trends Biochem. Sci. 12, 20-23.
18. Lin, H., Masso-Welch, P., Di, Y.-P., Cai, J., Shen, J. and Subjeck, J. R. (1993). The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin. Mol. Biol. Cell 4, 1109-1119.
19. Maniatis, T., Fritsch, E. F. and Sambrook, J. (1982). Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
20. Mori, K., Sant, A., Kohno, K., Normington, K., Gething, M.-J. and Sambrook, J. (1992). A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J. 11, 2583-2593.
21. 2+/ CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74, 743-756.
22. Nikawa, J.-I. and Yamashita, S. (1992). IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol prototrophy in Saccharomyces cerevisiae. Mol. Microbiol. 6, 1441-1446.
23. Nishikawa, S. and Nakano, A. (1991). The GTP-binding Sarl protein is localized to the early compartment of the yeast secretory pathway. Biochim. Biophys. Acta 1093, 135-143.
24. Nishikawa, S., Hirata, A. and Nakano, A. (1994). Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies. Mol. Biol. Cell 5, 1129-1143.
25. Normington, K., Kohno, K., Kozutsumi, Y., Gething, M.-J. and Sambrook, J. (1989). S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57, 1223-1236.
26. Ohkuma, M., Park, S. M., Zimmer, T., et al. (1995). Proliferation of intracellular membrane structures upon homologous overproduction of cytochrome P-450 in Candida maltosa. Biochim. Biophys. Acta 1236, 163-169.
27. Preuss, D., Mulholland, J., Kaiser, C. A., et al. (1991). Structure of the yeast endoplasmic reticulum: localization of ER proteins using immunofluorescence and immunoelectron microscopy. Yeast 7, 891-911.
28. Rose, M. D., Misra, L. M. and Vogel, J. P. (1989). KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57, 1211-1221.
29. Schlenstedt, G., Harris, S., Risse, B., Lill, R. and Silver, P. A. (1995). A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J. Cell Biol. 129, 979-988.
30. Schmitt, M. E., Brown, T. A. and Trumpower, B. L. (1990). A rapid and simple method for preparation of RNA from Saccharomyces cerevisiae. Nucl. Acids Res. 18, 3091.
31. Schunck, W.-H., Vogel, F., Gross, B., et al. (1991). Comparison of two cytochromes P-450 from Candida maltosa: primary structures, substrate specificities and effects of their expression in Saccharomyces cerevisiae on the proliferation of the endoplasmic reticulum. Eur. J. Cell Biol. 55, 336-345.
32. Shamu, C. E. and Walter, P. (1996). Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15, 3028-3039.
33. Sitia, R. and Meldolesi, J. (1992). Endoplasmic reticulum: a dynamic patchwork of specialized subregions. Mol. Biol. Cell 3, 1067-1072.
34. Strambio-de-Castillia, C., Blobel, G. and Rout, M. P. (1995). Isolation and characterization of nuclear envelopes from the yeast Saccharomyces. J. Cell Biol. 131, 19-31.
35. Sun, G.-H., Hirata, A., Ohya, Y. and Anraku, Y. (1992). Mutations in yeast calmodulin cause defects in spindle pole body functions and nuclear integrity. J. Cell Biol. 119, 1625-1639.
36. Tachibana, C. and Stevens, T. H. (1992). The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell Biol. 12, 4601-4611.
37. Tokunaga, M., Kawamura, A. and Kohno, K. (1992). Purification and characterization of BiP/Kar2 protein from Saccharomyces cerevisiae. J. Biol. Chem. 267, 17553-17559.
38. Tooze, J., Kern, H. F., Fuller, S. D. and Howell, K. E. (1989). Condensation-sorting events in the rough endoplasmic reticulum of exocrine pancreatic cells J. Cell Biol. 109, 35-50.
39. Tooze, J., Hollinshead, M., Ludwig, T., Howell, K., Hoflack, B. and Kern, H. (1990). In exocrine pancreas, the basolateral endocytic pathway converges with the autophagic pathway immediately after the early endosome. J. Cell Biol. 111, 329-345.
40. Valetti, C., Grossi, C. E., Milstein, C. and Sitia, R. (1991). Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum. J. Cell Biol. 115, 983-994.
41. 5 in yeast results in marked proliferation of the intracellular membrane. J. Cell Sci. 106, 249-259.
42. Wright, R., Basson, M., D'Ari, L. and Rine, J. (1988). Increased amounts of HMG-CoA reductase induce "karmellae": a proliferation of stacked membrane pairs surrounding the yeast nucleus. J. Cell Biol. 107, 101-114.