ArticlePloS one2012
Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Human J-Domain Protein DnaJB6 Protects Yeast from [Biology · 2022Article
- Review
- A Novel Method of Magnetic Nanoparticles Functionalized with Anti-Folate Receptor Antibody and Methotrexate for Antibody Mediated Targeted Drug Delivery.Molecules (Basel, Switzerland) · 2022Article
- Huntingtin Polyglutamine Fragments Are a Substrate for Hsp104 in Saccharomyces cerevisiae.Molecular and cellular biology · 2021Article
- Article
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Candida albicans Is Resistant to Polyglutamine Aggregation and Toxicity.G3 (Bethesda, Md.) · 2017Article
- The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation.Prion · 2016Article
- Article
- A protein polymerization cascade mediates toxicity of non-pathological human huntingtin in yeast.Scientific reports · 2015Article
- Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Physiological and environmental control of yeast prions.FEMS microbiology reviews · 2014Review
- Proteomic screening for amyloid proteins.PloS one · 2014Article
- Prions in yeast.Genetics · 2012Review
- Contribution of yeast models to neurodegeneration research.Journal of biomedicine & biotechnology · 2012Review
- Defining the limits: Protein aggregation and toxicity in vivo.Critical reviews in biochemistry and molecular biologyReview
- Article
- Article
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3 authors.
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Abstract
backgroundPolyglutamine expansion is responsible for several neurodegenerative disorders, among which Huntington disease is the most well-known. Studies in the yeast model demonstrated that both aggregation and toxicity of a huntingtin (htt) protein with an expanded polyglutamine region strictly depend on the presence of the prion form of Rnq1 protein ([PIN+]), which has a glutamine/asparagine-rich domain. PRINCIPAL
findingsHere, we showed that aggregation and toxicity of mutant htt depended on [PIN+] only quantitatively: the presence of [PIN+] elevated the toxicity and the levels of htt detergent-insoluble polymers. In cells lacking [PIN+], toxicity of mutant htt was due to the polymerization and inactivation of the essential glutamine/asparagine-rich Sup35 protein and related inactivation of another essential protein, Sup45, most probably via its sequestration into Sup35 aggregates. However, inhibition of growth of [PIN+] cells depended on Sup35/Sup45 depletion only partially, suggesting that there are other sources of mutant htt toxicity in yeast.
conclusionsThe obtained data suggest that induced polymerization of essential glutamine/asparagine-rich proteins and related sequestration of other proteins which interact with these polymers represent an essential source of htt toxicity.
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