Defining the limits: Protein aggregation and toxicity in vivo

References

• Aguzzi A. (2009). Cell biology: beyond the prion principle. Nature 459:924–5
   PubMed Web of Science ®Google Scholar
• Aigle M, Lacroute F. (1975). Genetical aspects of [URE3], a non-mitochondrial, cytoplasmically inherited mutation in yeast. Mol Gen Genet 136:327–35
   PubMedGoogle Scholar
• Alberti S, Halfmann R, King O, et al. (2009). A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. Cell 137:146–58
   PubMed Web of Science ®Google Scholar
• Alkalaeva EZ, Pisarev AV, Frolova LY, et al. (2006). In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell 125:1125–36
   PubMed Web of Science ®Google Scholar
• Anfinsen CB. (1967). The formation of the tertiary structure of proteins. Harvey Lect 61:95–116
   Google Scholar
• Arispe N, Rojas E, Pollard HB. (1993). Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc Natl Acad Sci USA 90:567–71
   PubMed Web of Science ®Google Scholar
• Arrasate M, Mitra S, Schweitzer ES, et al. (2004). Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431:805–10
   PubMed Web of Science ®Google Scholar
• Bagriantsev SN, Gracheva EO, Richmond JE, Liebman SW. (2008). Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition. Mol Biol Cell 9:2433–43
   Google Scholar
• Balch WE, Morimoto RI, Dillin A, Kelly JW. (2008). Adapting proteostasis for disease intervention. Science 319:916–19
   PubMed Web of Science ®Google Scholar
• Bence NF, Sampat RM, Kopito RR. (2001). Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292:1552–5
   PubMed Web of Science ®Google Scholar
• Berson JF, Theos AC, Harper DC, et al. (2003). Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J Cell Biol 161:521–33
   Google Scholar
• Broadley SA, Hartl FU. (2009). The role of molecular chaperones in human misfolding diseases. FEBS Lett 583:2647–53
   PubMed Web of Science ®Google Scholar
• Brown JC, Lindquist S. (2009). A heritable switch in carbon source utilization driven by an unusual yeast prion. Genes Dev 23:2320–32
   PubMed Web of Science ®Google Scholar
• Brundin P, Melki R, Kopito R. (2010). Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat Rev Mol Cell Biol 11:301–7
   PubMed Web of Science ®Google Scholar
• Bullitt E, Rout MP, Kilmartin JV, Akey CW. (1997). The yeast spindle pole body is assembled around a central crystal of Spc42p. Cell 89:1077–86
   Google Scholar
• Cao F, Levine JJ, Li SH, Li XJ. (2001). Nuclear aggregation of huntingtin is not prevented by deletion of chaperone Hsp104. Biochim Biophys Acta 1537:158–66
   PubMed Web of Science ®Google Scholar
• Cascarina SM, Ross ED. (2014). Yeast prions and human prion-like proteins: sequence features and prediction methods. Cell Mol Life Sci. [Epub ahead of print]. doi: http://dx.doi.org/10.1007/s00018-013-1543-6
   Google Scholar
• Cashikar AG, Duennwald M, Lindquist SL. (2005). A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem 280:23869–75
   PubMed Web of Science ®Google Scholar
• Caughey B, Lansbury PT. (2003). Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu Rev Neurosci 26:267–98
   PubMed Web of Science ®Google Scholar
• Chai Y, Shao J, Miller VM, et al. (2002). Live-cell imaging reveals divergent intracellular dynamics of polyglutamine disease proteins and supports a sequestration model of pathogenesis. Proc Natl Acad Sci USA 99:9310–15
   PubMedGoogle Scholar
• Chernoff YO, Derkach IL, Inge-Vechtomov SG. (1993). Multicopy SUP35 gene induces de-novo appearance of psi-like factors in the yeast Saccharomyces cerevisiae. Curr Genet 24:268–70
   PubMed Web of Science ®Google Scholar
• Chernoff YO, Inge-Vechtomov SG, Derkach IL, et al. (1992). Dosage-dependent translational suppression in yeast Saccharomyces cerevisiae. Yeast 8:489–99
   PubMed Web of Science ®Google Scholar
• Chernoff YO, Lindquist SL, Ono B, et al. (1995). Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [PSI+]. Science 268:880–4
   PubMed Web of Science ®Google Scholar
• Chesebro B, Trifilo M, Race R, et al. (2005). Anchorless prion protein results in infectious amyloid disease without clinical scrapie. Science 308:1435–9
   PubMed Web of Science ®Google Scholar
• Chiti F, Dobson CM. (2006). Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333–66
   PubMed Web of Science ®Google Scholar
• Cohen E, Bieschke J, Perciavalle RM, et al. (2006). Opposing activities protect against age-onset proteotoxicity. Science 313:1604–10
   PubMed Web of Science ®Google Scholar
• Cox B. (1965). [PSI], a cytoplasmic suppressor of super-suppression in yeast. Heredity 20:505–21
   Web of Science ®Google Scholar
• Czaplinski K, Ruiz-Echevarria MJ, Paushkin SV, et al. (1998). The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs. Genes Dev 12:1665–77
   PubMedGoogle Scholar
• Dagkesamanskaya AR, Ter-Avanesyan MD. (1991). Interaction of the yeast omnipotent suppressors SUP1(SUP45) and SUP2(SUP35) with non-Mendelian factors. Genetics 128:513–20
   PubMed Web of Science ®Google Scholar
• David DC, Ollikainen N, Trinidad JC, et al. (2010). Widespread protein aggregation as an inherent part of aging in C. elegans. PLoS Biol 8:e1000450
   PubMed Web of Science ®Google Scholar
• Dehay B, Bertolotti A. (2006). Critical role of the proline-rich region in Huntingtin for aggregation and cytotoxicity in yeast. J Biol Chem 281:35608–15
   PubMed Web of Science ®Google Scholar
• Derdowski A, Sindi SS, Klaips CL, et al. (2010). A size threshold limits prion transmission and establishes phenotypic diversity. Science 330:680–3
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Bradley ME, Hong JY, Liebman SW. (2001). Prions affect the appearance of other prions: the story of [PIN+]. Cell 106:171–82
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Bradley ME, Liebman SW. (1998). Overexpression of the SUP45 gene encoding a Sup35p-binding protein inhibits the induction of the de novo appearance of the [PSI+] prion. Proc Natl Acad Sci USA 95:2400–5
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Bradley ME, Zhou P, et al. (1997). Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae. Genetics 147:507–19
   PubMed Web of Science ®Google Scholar
• Derkatch IL, Chernoff YO, Kushnirov VV, et al. (1996). Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae. Genetics 144:1375–86
   PubMed Web of Science ®Google Scholar
• DiSalvo S, Derdowski A, Pezza JA, Serio TR. (2011). Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation. Nat Struct Mol Biol 18:486–92
   PubMed Web of Science ®Google Scholar
• Douglas PM, Summers DW, Ren HY, Cyr DM. (2009). Reciprocal efficiency of RNQ1 and polyglutamine detoxification in the cytosol and nucleus. Mol Biol Cell 20:4162–73
   PubMedGoogle Scholar
• Douglas PM, Treusch S, Ren HY, et al. (2008). Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proc Natl Acad Sci USA 105:7206–11
   PubMed Web of Science ®Google Scholar
• Du Z, Park KW, Yu H, et al. (2008). Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae. Nat Genet 40:460–5
   PubMed Web of Science ®Google Scholar
• Duennwald ML, Jagadish S, Giorgini F, et al. (2006a). A network of protein interactions determines polyglutamine toxicity. Proc Natl Acad Sci USA 103:11051–6
   PubMed Web of Science ®Google Scholar
• Duennwald ML, Jagadish S, Muchowski PJ, Lindquist S. (2006b). Flanking sequences profoundly alter polyglutamine toxicity in yeast. Proc Natl Acad Sci USA 103:11045–50
   PubMed Web of Science ®Google Scholar
• Duennwald ML, Lindquist S. (2008). Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev 22:3308–19
   PubMed Web of Science ®Google Scholar
• Eisenberg D, Jucker M. (2012). The amyloid state of proteins in human diseases. Cell 148:1188–203
   PubMed Web of Science ®Google Scholar
• Eyler DE, Wehner KA, Green R. (2013). Eukaryotic release factor 3 is required for multiple turnovers of peptide release catalysis by eukaryotic release factor 1. J Biol Chem 288:29530–8
   Google Scholar
• Fowler DM, Koulov AV, Alory-Jost C, et al. (2006). Functional amyloid formation within mammalian tissue. PLoS Biol 4:e6
   PubMed Web of Science ®Google Scholar
• Garcia W, De Araujo AP, Lara F, et al. (2007). An intermediate structure in the thermal unfolding of the GTPase domain of human septin 4 (SEPT4/Bradeion-beta) forms amyloid-like filaments in vitro. Biochemistry 46:11101–9
   Google Scholar
• Gidalevitz T, Ben-Zvi A, Ho KH, et al. (2006). Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311:1471–4
   PubMed Web of Science ®Google Scholar
• Giorgini F, Guidetti P, Nguyen Q, et al. (2005). A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease. Nat Genet 37:526–31
   PubMed Web of Science ®Google Scholar
• Gokhale KC, Newnam GP, Sherman MY, Chernoff YO. (2005). Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J Biol Chem 280:22809–18
   PubMed Web of Science ®Google Scholar
• Gong H, Romanova NV, Allen KD, et al. (2012). Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast. PLoS Genet 8:e1002634
   Google Scholar
• Haass C, Selkoe DJ. (2007). Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat Rev Mol Cell Biol 8:101–12
   PubMed Web of Science ®Google Scholar
• Halfmann R, Alberti S, Lindquist S. (2010). Prions, protein homeostasis, and phenotypic diversity. Trends Cell Biol 20:125–33
   PubMed Web of Science ®Google Scholar
• Halfmann R, Wright JR, Alberti S, et al. (2012). Prion formation by a yeast GLFG nucleoporin. Prion 6:391–9
   PubMed Web of Science ®Google Scholar
• Hartl FU, Bracher A, Hayer-Hartl M. (2011). Molecular chaperones in protein folding and proteostasis. Nature 475:324–32
   PubMed Web of Science ®Google Scholar
• Higurashi T, Hines JK, Sahi C, et al. (2008). Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proc Natl Acad Sci USA 105:16596–601
   PubMed Web of Science ®Google Scholar
• Ihara M, Tomimoto H, Kitayama H, et al. (2003). Association of the cytoskeletal GTP-binding protein Sept4/H5 with cytoplasmic inclusions found in Parkinson's disease and other synucleinopathies. J Biol Chem 278:24095–102
   PubMed Web of Science ®Google Scholar
• Ito K, Ebihara K, Nakamura Y. (1998). The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast. RNA 4:958–72
   PubMed Web of Science ®Google Scholar
• Jahn TR, Radford SE. (2008). Folding versus aggregation: polypeptide conformations on competing pathways. Arch Biochem Biophys 469:100–17
   PubMed Web of Science ®Google Scholar
• Jean-Jean O, Le Goff X, Philippe M. (1996). Is there a human [psi]? Comptes Rendus de l Academie des Sciences – Serie Iii. Sciences de la Vie 319:487–92
   PubMed Web of Science ®Google Scholar
• Jiang H, Poirier MA, Liang Y, et al. (2006). Depletion of CBP is directly linked with cellular toxicity caused by mutant huntingtin. Neurobiol Dis 23:543–51
   PubMed Web of Science ®Google Scholar
• Johnston JA, Ward CL, Kopito RR. (1998). Aggresomes: a cellular response to misfolded proteins. J Cell Biol 143:1883–98
   PubMed Web of Science ®Google Scholar
• Kaganovich D, Kopito R, Frydman J. (2008). Misfolded proteins partition between two distinct quality control compartments. Nature 454:1088–95
   PubMed Web of Science ®Google Scholar
• Kaiser CJ, Grotzinger SW, Eckl JM, et al. (2013). A network of genes connects polyglutamine toxicity to ploidy control in yeast. Nat Commun 4:1571
   Google Scholar
• Kaltenbach LS, Romero E, Becklin RR, et al. (2007). Huntingtin interacting proteins are genetic modifiers of neurodegeneration. PLoS Genet 3:e82
   PubMed Web of Science ®Google Scholar
• Kim S, Nollen EA, Kitagawa K, et al. (2002). Polyglutamine protein aggregates are dynamic. Nat Cell Biol 4:826–31
   PubMedGoogle Scholar
• Kim YE, Hipp MS, Bracher A, et al. (2013). Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem 82:323–55
   PubMed Web of Science ®Google Scholar
• Kimura Y, Koitabashi S, Kakizuka A, Fujita T. (2004). The role of pre-existing aggregates in Hsp104-dependent polyglutamine aggregate formation and epigenetic change of yeast prions. Genes Cells 9:685–96
   Google Scholar
• Kinoshita A, Kinoshita M, Akiyama H, et al. (1998). Identification of septins in neurofibrillary tangles in Alzheimer's disease. Am J Pathol 153:1551–60
   PubMed Web of Science ®Google Scholar
• Kirstein-Miles J, Scior A, Deuerling E, Morimoto RI. (2013). The nascent polypeptide-associated complex is a key regulator of proteostasis. EMBO J 32:1451–68
   Google Scholar
• Kobayashi Y, Sobue G. (2001). Protective effect of chaperones on polyglutamine diseases. Brain Res Bull 56:165–8
   PubMed Web of Science ®Google Scholar
• Kochneva-Pervukhova NV, Alexandrov AI, Ter-Avanesyan MD. (2012). Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast. PLoS One 7:e29832
   Google Scholar
• Kremer JJ, Sklansky DJ, Murphy RM. (2001). Profile of changes in lipid bilayer structure caused by beta-amyloid peptide. Biochemistry 40:8563–71
   PubMed Web of Science ®Google Scholar
• Krobitsch S, Lindquist S. (2000). Aggregation of huntingtin in yeast varies with the length of the polyglutamine expansion and the expression of chaperone proteins. Proc Natl Acad Sci USA 97:1589–94
   PubMed Web of Science ®Google Scholar
• Kryndushkin DS, Alexandrov IM, Ter-Avanesyan MD, Kushnirov VV. (2003). Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104. J Biol Chem 278:49636–43
   PubMed Web of Science ®Google Scholar
• Li JY, Englund E, Holton JL, et al. (2008). Lewy bodies in grafted neurons in subjects with Parkinson's disease suggest host-to-graft disease propagation. Nat Med 14:501–3
   PubMed Web of Science ®Google Scholar
• Liebman SW, Sherman F. (1979). Extrachromosomal psi+ determinant suppresses nonsense mutations in yeast. J Bacteriol 139:1068–71
   PubMed Web of Science ®Google Scholar
• Lindquist SL, Kelly JW. (2011). Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harb Perspect Biol 3:pii:a004507
   Google Scholar
• Lopez N, Aron R, Craig EA. (2003). Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+]. Mol Biol Cell 14:1172–81
   PubMed Web of Science ®Google Scholar
• Lum R, Tkach JM, Vierling E, Glover JR. (2004). Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J Biol Chem 279:29139–46
   PubMed Web of Science ®Google Scholar
• Maji SK, Perrin MH, Sawaya MR, et al. (2009). Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 325:328–32
   PubMed Web of Science ®Google Scholar
• Malinovska L, Kroschwald S, Munder MC, et al. (2012). Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates. Mol Biol Cell 23:3041–56
   Google Scholar
• Masison DC, Wickner RB. (1995). Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270:93–5
   PubMed Web of Science ®Google Scholar
• Mason RP, Casu M, Butler N, et al. (2013). Glutathione peroxidase activity is neuroprotective in models of Huntington's disease. Nat Genet 45:1249–54
   PubMedGoogle Scholar
• McCampbell A, Taylor JP, Taye AA, et al. (2000). CREB-binding protein sequestration by expanded polyglutamine. Hum Mol Genet 9:2197–202
   PubMed Web of Science ®Google Scholar
• McGlinchey RP, Kryndushkin D, Wickner RB. (2011). Suicidal [PSI+] is a lethal yeast prion. Proc Natl Acad Sci USA 108:5337–41
   PubMed Web of Science ®Google Scholar
• Meriin AB, Zhang X, He X, et al. (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 AB, Zhang X, Miliaras NB, et al. (2003). Aggregation of expanded polyglutamine domain in yeast leads to defects in endocytosis. Mol Cell Biol 23:7554–65
   PubMed Web of Science ®Google Scholar
• Meyer-Luehmann M, Coomaraswamy J, Bolmont T, et al. (2006). Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host. Science 313:1781–4
   PubMed Web of Science ®Google Scholar
• Muchowski PJ, Schaffar G, Sittler A, et al. (2000). Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. Proc Natl Acad Sci USA 97:7841–6
   PubMed Web of Science ®Google Scholar
• Muchowski PJ, Wacker JL. (2005). Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 6:11–22
   PubMed Web of Science ®Google Scholar
• Ness F, Ferreira P, Cox BS, Tuite MF. (2002). Guanidine hydrochloride inhibits the generation of prion “seeds” but not prion protein aggregation in yeast. Mol Cell Biol 22:5593–605
   PubMed Web of Science ®Google Scholar
• Nucifora FC Jr, Sasaki M, Peters MF, et al. (2001). Interference by huntingtin and atrophin-1 with cbp-mediated transcription leading to cellular toxicity. Science 291:2423–8
   PubMed Web of Science ®Google Scholar
• Olzscha H, Schermann SM, Woerner AC, et al. (2011). Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144:67–78
   PubMed Web of Science ®Google Scholar
• Osherovich LZ, Weissman JS. (2001). Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI+] prion. Cell 106:183–94
   PubMed Web of Science ®Google Scholar
• Park SH, Kukushkin Y, Gupta R, et al. (2013). PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell 154:134–45
   PubMed Web of Science ®Google Scholar
• Park YN, Morales D, Rubinson EH, et al. (2012). Differences in the curing of [PSI+] prion by various methods of Hsp104 inactivation. PLoS One 7:e37692
   PubMedGoogle Scholar
• Patel BK, Gavin-Smyth J, Liebman SW. (2009). The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion. Nat Cell Biol 11:344–9
   PubMed Web of Science ®Google Scholar
• Patino MM, Liu JJ, Glover JR, Lindquist S. (1996). Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273:622–6
   PubMed Web of Science ®Google Scholar
• Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD. (1996). Propagation of the yeast prion-like [PSI+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J 15:3127–34
   PubMed Web of Science ®Google Scholar
• Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD. (1997). Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation. Mol Cell Biol 17:2798–805
   PubMed Web of Science ®Google Scholar
• Perez MK, Paulson HL, Pendse SJ, et al. (1998). Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J Cell Biol 143:1457–70
   PubMed Web of Science ®Google Scholar
• Pezza JA, Langseth SX, Raupp Yamamoto R, et al. (2009). The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype. Mol Biol Cell 20:1068–80
   Google Scholar
• Piccardo P, Manson JC, King D, et al. (2007). Accumulation of prion protein in the brain that is not associated with transmissible disease. Proc Natl Acad Sci USA 104:4712–17
   PubMed Web of Science ®Google Scholar
• Pissuti Damalio JC, Garcia W, Alves Macedo JN, et al. (2012). Self assembly of human septin 2 into amyloid filaments. Biochimie 94:628–36
   Google Scholar
• Ren PH, Lauckner JE, Kachirskaia I, et al. (2009). Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates. Nat Cell Biol 11:219–25
   PubMed Web of Science ®Google Scholar
• Rogoza T, Goginashvili A, Rodionova S, et al. (2010). Non-Mendelian determinant [ISP+] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1. Proc Natl Acad Sci USA 107:10573–7
   PubMed Web of Science ®Google Scholar
• Satpute-Krishnan P, Langseth SX, Serio TR. (2007). Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance. PLoS Biol 5:e24
   PubMed Web of Science ®Google Scholar
• Satpute-Krishnan P, Serio TR. (2005). Prion protein remodelling confers an immediate phenotypic switch. Nature 437:262–5
   PubMed Web of Science ®Google Scholar
• Saudou F, Finkbeiner S, Devys D, Greenberg ME. (1998). Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95:55–66
   PubMed Web of Science ®Google Scholar
• Schaffar G, Breuer P, Boteva R, et al. (2004). Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Mol Cell 15:95–105
   PubMed Web of Science ®Google Scholar
• Serio TR, Cashikar AG, Kowal AS, et al. (2000). Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289:1317–21
   PubMed Web of Science ®Google Scholar
• Shiber A, Breuer W, Brandeis M, Ravid T. (2013). Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting. Mol Biol Cell 24:2076–87
   Google Scholar
• Si K, Choi YB, White-Grindley E, et al. (2010). Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation. Cell 140:421–35
   PubMed Web of Science ®Google Scholar
• Sindi SS, Serio TR. (2009). Prion dynamics and the quest for the genetic determinant in protein-only inheritance. Curr Opin Microbiol 12:623–30
   PubMed Web of Science ®Google Scholar
• Sondheimer N, Lindquist S. (2000). Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell 5:163–72
   PubMed Web of Science ®Google Scholar
• Sondheimer N, Lopez N, Craig EA, Lindquist S. (2001). The role of Sis1 in the maintenance of the [RNQ+] prion. EMBO J 20:2435–42
   PubMed Web of Science ®Google Scholar
• Stansfield I, Jones KM, Kushnirov VV, et al. (1995). The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae. EMBO J 14:4365–73
   PubMed Web of Science ®Google Scholar
• Steffan JS, Kazantsev A, Spasic-Boskovic O, et al. (2000). The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription. Proc Natl Acad Sci USA 97:6763–8
   PubMed Web of Science ®Google Scholar
• Strawn LA, True HL. (2006). Deletion of RNQ1 gene reveals novel functional relationship between divergently transcribed Bik1p/CLIP-170 and Sfi1p in spindle pole body separation. Curr Genet 50:347–66
   Google Scholar
• Stryer L. (1965). The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J Mol Biol 13:482–95
   PubMedGoogle Scholar
• Summers DW, Douglas PM, Cyr DM. (2009a). Prion propagation by Hsp40 molecular chaperones. Prion 3:59–64
   PubMed Web of Science ®Google Scholar
• Summers DW, Douglas PM, Ren HY, Cyr DM. (2009b). The type I Hsp40 Ydj1 utilizes a farnesyl moiety and zinc finger-like region to suppress prion toxicity. J Biol Chem 284:3628–39
   PubMed Web of Science ®Google Scholar
• Summers DW, Wolfe KJ, Ren HY, Cyr DM. (2013). The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein. PLoS One 8:e52099
   PubMed Web of Science ®Google Scholar
• Suzuki G, Shimazu N, Tanaka M. (2012). A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress. Science 336:355–9
   PubMed Web of Science ®Google Scholar
• Tanaka M, Collins SR, Toyama BH, Weissman JS. (2006). The physical basis of how prion conformations determine strain phenotypes. Nature 442:585–9
   PubMed Web of Science ®Google Scholar
• Tank EM, True HL. (2009). Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates. PLoS Genet 5:e1000382
   PubMedGoogle Scholar
• Ter-Avanesyan MD, Dagkesamanskaya AR, Kushnirov VV, Smirnov VN. (1994). The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [PSI+] in the yeast Saccharomyces cerevisiae. Genetics 137:671–6
   PubMed Web of Science ®Google Scholar
• Ter-avanesyan MD, Kushnirov VV, Dagkesamanskaya AR, et al. (1993). Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein. Mol Microbiol 7:683–92
   PubMed Web of Science ®Google Scholar
• Tessarz P, Mogk A, Bukau B. (2008). Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol Microbiol 68:87–97
   PubMed Web of Science ®Google Scholar
• The Huntington's Disease Collaborative Research Group. (1993). A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72:971–83
   PubMed Web of Science ®Google Scholar
• Tipton KA, Verges KJ, Weissman JS. (2008). In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104. Mol Cell 32:584–91
   PubMed Web of Science ®Google Scholar
• Treusch S, Lindquist S. (2012). An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component. J Cell Biol 197:369–79
   Google Scholar
• Tuite MF, Serio TR. (2010). The prion hypothesis: from biological anomaly to basic regulatory mechanism. Nat Rev Mol Cell Biol 11:823–33
   PubMed Web of Science ®Google Scholar
• Urakov VN, Vishnevskaya AB, Alexandrov IM, et al. (2010). Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions. Prion 4:45–52
   PubMed Web of Science ®Google Scholar
• Valouev IA, Kushnirov VV, Ter-Avanesyan MD. (2002). Yeast polypeptide chain release factors eRF1 and eRF3 are involved in cytoskeleton organization and cell cycle regulation. Cell Motil Cytoskeleton 52:161–73
   PubMed Web of Science ®Google Scholar
• Vavouri T, Semple JI, Garcia-Verdugo R, Lehner B. (2009). Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity. Cell 138:198–208
   PubMed Web of Science ®Google Scholar
• Vishveshwara N, Bradley ME, Liebman SW. (2009). Sequestration of essential proteins causes prion associated toxicity in yeast. Mol Microbiol 73:1101–14
   PubMed Web of Science ®Google Scholar
• Voisine C, Pedersen JS, Morimoto RI. (2010). Chaperone networks: tipping the balance in protein folding diseases. Neurobiol Dis 40:12–20
   PubMed Web of Science ®Google Scholar
• Volles MJ, Lee SJ, Rochet JC, et al. (2001). Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40:7812–19
   PubMed Web of Science ®Google Scholar
• Wang Y, Meriin AB, Zaarur N, et al. (2009). Abnormal proteins can form aggresome in yeast: aggresome-targeting signals and components of the machinery. FASEB J 23:451–63
   PubMed Web of Science ®Google Scholar
• Wickner RB. (1994). [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264:566–9
   PubMed Web of Science ®Google Scholar
• Wolfe KJ, Ren HY, Trepte P, Cyr DM. (2013). The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins. Mol Biol Cell 24:3588–602
   PubMed Web of Science ®Google Scholar
• Zhao X, Park YN, Todor H, et al. (2012). Sequestration of Sup35 by aggregates of huntingtin fragments causes toxicity of [PSI+] yeast. J Biol Chem 287:23346–55
   Google Scholar
• Zhou P, Derkatch IL, Uptain SM, et al. (1999). The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion- like form of release factor eRF3. EMBO J 18:1182–91
   PubMed Web of Science ®Google Scholar
• Zhouravleva G, Frolova L, Le Goff X, et al. (1995). Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J 14:4065–72
   PubMed Web of Science ®Google Scholar