ArticlePLoS genetics2012
Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast.
Article in PLoS genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 55 citations in OpenAlex.
- Maturation and detoxification of synphilin-1 inclusion bodies regulated by sphingolipids.eLife · 2025Article
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- Human J-Domain Protein DnaJB6 Protects Yeast from [Biology · 2022Article
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- Review
- Gene Amplification as a Mechanism of Yeast Adaptation to Nonsense Mutations in Release Factor Genes.Genes · 2021Article
- Huntingtin Polyglutamine Fragments Are a Substrate for Hsp104 in Saccharomyces cerevisiae.Molecular and cellular biology · 2021Article
- Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association.International journal of molecular sciences · 2020Article
- Article
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.Molecules (Basel, Switzerland) · 2019Review
- An aggregation-prone mutant of eIF3a forms reversible assemblies escaping spatial control in exponentially growing yeast cells.Current genetics · 2019Article
- Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species.Scientific reports · 2018Article
- A Liquid to Solid Phase Transition Underlying Pathological Huntingtin Exon1 Aggregation.Molecular cell · 2018Article
- Article
- Prions, Chaperones, and Proteostasis in Yeast.Cold Spring Harbor perspectives in biology · 2017Review
- Haploid yeast cells undergo a reversible phenotypic switch associated with chromosome II copy number.BMC genetics · 2016Article
- Multiple discrete soluble aggregates influence polyglutamine toxicity in a Huntington's disease model system.Scientific reports · 2016Article
- Strain conformation controls the specificity of cross-species prion transmission in the yeast model.Prion · 2016Article
- Ubiquilin/Dsk2 promotes inclusion body formation and vacuole (lysosome)-mediated disposal of mutated huntingtin.Molecular biology of the cell · 2016Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Polyglutamine expansion causes diseases in humans and other mammals. One example is Huntington's disease. Fragments of human huntingtin protein having an expanded polyglutamine stretch form aggregates and cause cytotoxicity in yeast cells bearing endogenous QN-rich proteins in the aggregated (prion) form. Attachment of the proline(P)-rich region targets polyglutamines to the large perinuclear deposit (aggresome). Aggresome formation ameliorates polyglutamine cytotoxicity in cells containing only the prion form of Rnq1 protein. Here we show that expanded polyglutamines both with (poly-QP) or without (poly-Q) a P-rich stretch remain toxic in the presence of the prion form of translation termination (release) factor Sup35 (eRF3). A Sup35 derivative that lacks the QN-rich domain and is unable to be incorporated into aggregates counteracts cytotoxicity, suggesting that toxicity is due to Sup35 sequestration. Increase in the levels of another release factor, Sup45 (eRF1), due to either disomy by chromosome II containing the SUP45 gene or to introduction of the SUP45-bearing plasmid counteracts poly-Q or poly-QP toxicity in the presence of the Sup35 prion. Protein analysis confirms that polyglutamines alter aggregation patterns of Sup35 and promote aggregation of Sup45, while excess Sup45 counteracts these effects. Our data show that one and the same mode of polyglutamine aggregation could be cytoprotective or cytotoxic, depending on the composition of other aggregates in a eukaryotic cell, and demonstrate that other aggregates expand the range of proteins that are susceptible to sequestration by polyglutamines.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.