Modulation of Prion Formation, Aggregation, and Toxicity by the Actin Cytoskeleton in Yeast

REFERENCES

• Allen, K. D., R. D. Wegrzyn, T. A. Chernova, S. Müller, G. P. Newnam, P. A. Winslett, K. B. Wittich, K. D. Wilkinson, and Y. O. Chernoff. 2005. Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics 169:1227–1242.
   PubMed Web of Science ®Google Scholar
• Ayscough, K. R. 2000. Endocytosis and the development of cell polarity in yeast require a dynamic F-actin cytoskeleton. Curr. Biol. 10:1587–1590.
   PubMedGoogle Scholar
• Ayscough, K. R., J. J. Eby, T. Lila, H. Dewar, K. G. Kozminski, and D. G. Drubin. 1999. Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology. Mol. Biol. Cell 10:1061–1075.
   PubMedGoogle Scholar
• Bailleul, P. A., G. P. Newnam, J. N. Steenbergen, and Y. O. Chernoff. 1999. Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. Genetics 153:81–94.
   PubMed Web of Science ®Google Scholar
• Bailleul-Winslett, P. A., G. P. Newnam, R. D. Wegrzyn, and Y. O. Chernoff. 2000. An antiprion effect of the anticytoskeletal drug latrunculin A in yeast. Gene Expr. 9:145–156.
   PubMed Web of Science ®Google Scholar
• Baron, G. S., K. Wehrly, D. W. Dorward, B. Chesebro, and B. Caughey. 2002. Conversion of raft associated prion protein to the protease-resistant state requires insertion of PrP-res (PrPSc) into contiguous membranes. EMBO J. 21:1031–1040.
   PubMed Web of Science ®Google Scholar
• Belmont, L. D., G. M. Patterson, and D. G. Drubin. 1999. New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites. J. Cell Sci. 112:1325–1336.
   PubMedGoogle Scholar
• Benedetti, H., S. Raths, F. Crausaz, and H. Riezman. 1994. The END3 gene encodes a protein that is required for the internalization step of endocytosis and for actin cytoskeleton organization in yeast. Mol. Biol. Cell 5:1023–1037.
   PubMed Web of Science ®Google Scholar
• Borchsenius, A. S., R. D. Wegrzyn, G. P. Newnam, S. G. Inge-Vechtomov, and Y. O. Chernoff. 2001. Yeast prion protein derivative defective in aggregate shearing and production of new seeds. EMBO J. 20:6683–6691.
   PubMed Web of Science ®Google Scholar
• Chernoff, Y. O. 2001. Mutation processes at the protein level: is Lamarck back? Mutat. Res. 488:39–64.
   PubMed Web of Science ®Google Scholar
• Chernoff, Y. O. 2004. Cellular control of prion formation and propagation in yeast, p. 257–303. In G. Telling (ed.), Prions and prion diseases: current perspectives. Horizon Scientific Press, Norfolk, United Kingdom.
   Google Scholar
• Chernoff, Y. O. 2004. Amyloidogenic domains, prions and structural inheritance: rudiments of early life or recent acquisition? Curr. Opin. Chem. Biol. 8:665–671.
   PubMed Web of Science ®Google Scholar
• Chernoff, Y. O., S. G. Inge-Vechtomov, I. L. Derkach, M. V. Ptyushkina, O. V. Tarunina, A. R. Dagkesamanskaya, and M. D. Ter-Avanesyan. 1992. Dosage-dependent translational suppression in yeast Saccharomyces cerevisiae. Yeast 8:489–499.
   PubMed Web of Science ®Google Scholar
• Chernoff, Y. O., I. L. Derkach, and S. G. Inge-Vechtomov. 1993. Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr. Genet. 24:268–270.
   PubMed Web of Science ®Google Scholar
• Chernoff, Y. O., G. P. Newnam, J. Kumar, K. Allen, and A. D. Zink. 1999. Evidence for a “protein mutator” in yeast: role of the Hsp70-related chaperone Ssb in formation, stability and toxicity of the [PSI] prion. Mol. Cell. Biol. 19:8103–8112.
   PubMed Web of Science ®Google Scholar
• Chernoff, Y. O., A. P. Galkin, E. Lewitin, T. A. Chernova, G. P. Newnam, and S. M. Belenkiy. 2000. Evolutionary conservation of prion-forming abilities of the yeast Sup35 protein. Mol. Microbiol. 35:865–876.
   PubMedGoogle Scholar
• Chernoff, Y. O., S. M. Uptain, and S. L. Lindquist. 2002. Analysis of prion factors in yeast. Methods Enzymol. 351:499–538.
   PubMed Web of Science ®Google Scholar
• Dagkesamanskaya, A. R., and M. D. Ter-Avanesyan. 1991. Interaction of the yeast omnipotent suppressors SUP1 (SUP45) and SUP2 (SUP35) with non-Mendelian factors. Genetics 128:513–520.
   PubMed Web of Science ®Google Scholar
• Derkatch, I. L., Y. O. Chernoff, V. V. Kushnirov, S. G. Inge-Vechtomov, and S. W. Liebman. 1996. Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 144:1375–1386.
   PubMed Web of Science ®Google Scholar
• Derkatch, I. L., M. E. Bradley, P. Zhou, Y. O. Chernoff, and S. W. Liebman. 1997. Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 147:507–519.
   PubMed Web of Science ®Google Scholar
• Derkatch, I. L., M. E. Bradley, P. Zhou, and S. W. Liebman. 1999. The PNM2 mutation in the prion protein domain of SUP35 has distinct effects on different variants of the [PSI+] prion in yeast. Curr. Genet. 35:59–67.
   PubMed Web of Science ®Google Scholar
• Derkatch, I. L., M. E. Bradley, J. Y. Hong, and S. W. Liebman. 2001. Prions affect the appearance of other prions: the story of [PIN+]. Cell 106:171–182.
   PubMed Web of Science ®Google Scholar
• Doel, S. M., S. J. McCready, C. R. Nierras, and B. S. Cox. 1994. The dominant PNM2 mutation which eliminates the psi factor of Saccharomyces cerevisiae is the result of a missense mutation in the SUP35 gene. Genetics 137:659–670.
   PubMed Web of Science ®Google Scholar
• Engqvist-Goldstein, A. E., and D. G. Drubin. 2003. Actin assembly and endocytosis: from yeast to mammals. Annu. Rev. Cell Dev. Biol. 19:287–332.
   PubMedGoogle Scholar
• Gokhale, K. C., G. P. Newnam, M. Y. Sherman, and Y. O. Chernoff. 2005. Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J. Biol. Chem. 280:22809–22818.
   PubMed Web of Science ®Google Scholar
• Holtzman, D. A., S. Yang, and D. G. Drubin. 1993. Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae. J. Cell Biol. 122:635–644.
   PubMed Web of Science ®Google Scholar
• James, P., J. Halladay, and E. A. Craig. 1996. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144:1425–1436.
   PubMed Web of Science ®Google Scholar
• Johnston, J. A., C. L. Ward, and R. R. Kopito. 1998. Aggresomes: a cellular response to misfolded proteins. J. Cell Biol. 28:1883–1898.
   Google Scholar
• Kalchman, M. A., H. B. Koide, K. McCutcheon, R. K. Graham, K. Nichol, K. Nishiyama, P. Kazemi-Esfarjani, F. C. Lynn, C. Wellington, M. Metzler, Y. P. Goldberg, I. Kanazawa, R. D. Gietz, and M. R. Hayden. 1997. HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain. Nat. Genet. 16:44–53.
   PubMed Web of Science ®Google Scholar
• Karpova, T. S., J. G. McNally, S. L. Moltz, and J. A. Cooper. 1998. Assembly and function of the actin cytoskeleton of yeast: relationships between cables and patches. J. Cell Biol. 142:1501–1517.
   PubMed Web of Science ®Google Scholar
• Kochneva-Pervukhova, N. V., S. V. Paushkin, V. V. Kushnirov, B. S. Cox, M. F. Tuite, and M. D. Ter-Avanesyan. 1998. Mechanism of inhibition of Psi+ prion determinant propagation by a mutation of the N terminus of the yeast Sup35 protein. EMBO J. 17:5805–5810.
   PubMed Web of Science ®Google Scholar
• Longtine, M. S., A. McKenzie, D. J. Demarini, N. G. Shah, A. Wach, A. Brachat, P. Philippsen, and J. R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14:953–961.
   PubMed Web of Science ®Google Scholar
• Meriin, A. B., X. Zhang, X. He, G. P. Newnam, Y. O. Chernoff, and M. Y. Sherman. 2002. Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J. Cell Biol. 157:997–1004.
   PubMed Web of Science ®Google Scholar
• Meriin, A. B., X. Zhang, N. B. Miliaras, A. Kazantsev, Y. O. Chernoff, J. M. McCaffery, B. Wendland, and M. Y. Sherman. 2003. Aggregation of expanded polyglutamine domain in yeast leads to defects in endocytosis. Mol. Cell. Biol. 23:7554–7565.
   PubMed Web of Science ®Google Scholar
• Michelitsch, M. D., and J. S. Weissman. 2000. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc. Natl. Acad. Sci. USA 97:11910–11915.
   PubMed Web of Science ®Google Scholar
• Muchowski, P. J., K. Ning, C. D'Souza-Schorey, and S. Fields. 2002. Requirement of an intact microtubule cytoskeleton for aggregation and inclusion body formation by a mutant huntingtin fragment. Proc. Natl. Acad. Sci. USA 99:727–732.
   PubMed Web of Science ®Google Scholar
• Munshi, R., K. A. Kandl, A. Carr-Schmid, J. L. Whitacre, A. E. Adams, and T. G. Kinzy. 2001. Overexpression of translation elongation factor 1A affects the organization and function of the actin cytoskeleton in yeast. Genetics 157:1425–1436.
   PubMed Web of Science ®Google Scholar
• Osherovich, L. Z., and J. S. Weissman. 2001. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI+] prion. Cell 106:183–194.
   PubMed Web of Science ®Google Scholar
• Osherovich, L. Z., B. S. Cox, M. F. Tuite, and J. S. Weissman. 2004. Dissection and design of yeast prions. PLoS Biol. 2:E86. [Online.] 10.1371/journal.pbio.0020086.
   PubMed Web of Science ®Google Scholar
• Perutz, M. F., R. Staden, L. Moens, and I. De Baere. 1993. Polar zippers. Curr. Biol. 3:249–253.
   PubMedGoogle Scholar
• Salnikova, A. B., D. S. Kryndushkin, V. N. Smirnov, V. V. Kushnirov, and M. D. Ter-Avanesyan. 2005. Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids. J. Biol. Chem. 280:8808–8812.
   PubMed Web of Science ®Google Scholar
• Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Serio, T. R., A. G. Cashikar, J. J. Moslehi, A. S. Kowal, and S. L. Lindquist. 1999. Yeast prion [psi+] and its determinant, Sup35p. Methods Enzymol. 309:649–673.
   PubMed Web of Science ®Google Scholar
• Sherman, F. 2002. Getting started with yeast. Methods Enzymol. 350:3–41.
   PubMed Web of Science ®Google Scholar
• Shorter, J., and S. Lindquist. 2004. Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304:1793–1797.
   PubMed Web of Science ®Google Scholar
• Shyng, S. L., M. T. Huber, and D. A. Harris. 1993. A prion protein cycles between the cell surface and an endocytic compartment in cultured neuroblastoma cells. J. Biol. Chem. 25:15922–15928.
   Google Scholar
• Tuite, M. F., and N. Koloteva-Levin. 2004. Propagating prions in fungi and mammals. Mol. Cell 14:541–552.
   PubMed Web of Science ®Google Scholar
• Uetz, P., L. Giot, G. Cagney, T. A. Mansfield, R. S. Judson, J. R. Knight, D. Lockshon, V. Narayan, M. Srinivasan, P. Pochart, A. Qureshi-Emili, Y. Li, B. Godwin, D. Conover, T. Kalbfleisch, G. Vijayadamodar, M. Yang, M. Johnston, S. Fields, and J. M. Rothberg. 2000. A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403:623–627.
   PubMed Web of Science ®Google Scholar
• Wegrzyn, R. D., K. Bapat, G. P. Newnam, A. D. Zink, and Y. O. Chernoff. 2001. Mechanism of prion loss after Hsp104 inactivation in yeast. Mol. Cell. Biol. 21:4656–4669.
   PubMed Web of Science ®Google Scholar
• Weissmann, C. 2004. The state of the prion. Nat. Rev. Microbiol. 2:861–871.
   PubMed Web of Science ®Google Scholar
• Yang, S., M. J. Cope, and D. G. Drubin. 1999. Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals. Mol. Biol. Cell 10:2265–2283.
   PubMedGoogle Scholar
• Zhou, P., I. L. Derkatch, and S. W. Liebman. 2001. The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI+] and [PIN+]. Mol. Microbiol. 39:37–46.
   PubMed Web of Science ®Google Scholar
• Zhouravleva, G. A., V. V. Alenin, S. G. Inge-Vechtomov, and Y. O. Chernoff. 2002. To stick or not to stick: prion domains from yeast to mammals, p. 185–218. In S. G. Pandalai (ed.), Recent research developments in molecular and cellular biology, vol. 3, part 1. Research Signpost, Kerala, India.
   Google Scholar