ArticlePrion
Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Amyloid Fragmentation and Disaggregation in Yeast and Animals.Biomolecules · 2021Review
- Huntingtin Polyglutamine Fragments Are a Substrate for Hsp104 in Saccharomyces cerevisiae.Molecular and cellular biology · 2021Article
- The Pub1 and Upf1 Proteins Act in Concert to Protect Yeast from Toxicity of the [PSI⁺] Prion.International journal of molecular sciences · 2018Article
- Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.International journal of molecular sciences · 2018Review
- Screening for amyloid proteins in the yeast proteome.Current genetics · 2018Article
- Prions, amyloids, and RNA: Pieces of a puzzle.Prion · 2016Review
- Article
- A protein polymerization cascade mediates toxicity of non-pathological human huntingtin in yeast.Scientific reports · 2015Article
- Functional role of Tia1/Pub1 and Sup35 prion domains: directing protein synthesis machinery to the tubulin cytoskeleton.Molecular cell · 2014Article
- Proteomic screening for amyloid proteins.PloS one · 2014Article
- Non-targeted identification of prions and amyloid-forming proteins from yeast and mammalian cells.The Journal of biological chemistry · 2013Article
- Erythrocytic stage-dependent regulation of oligomerization of Plasmodium ribosomal protein P2.The Journal of biological chemistry · 2012Article
- An aggregation sensing reporter identifies leflunomide and teriflunomide as polyglutamine aggregate inhibitors.Human molecular genetics · 2012Article
- Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast.PloS one · 2012Article
- Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast.PLoS genetics · 2012Article
- Ordered assembly of heat shock proteins, Hsp26, Hsp70, Hsp90, and Hsp104, on expanded polyglutamine fragments revealed by chemical probes.The Journal of biological chemistry · 2011Article
- Molecular basis for transmission barrier and interference between closely related prion proteins in yeast.The Journal of biological chemistry · 2011Article
- Non-Mendelian determinant [ISP+] in yeast is a nuclear-residing prion form of the global transcriptional regulator Sfp1.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Defining the limits: Protein aggregation and toxicity in vivo.Critical reviews in biochemistry and molecular biologyReview
- Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
In eukaryotic cells amyloid aggregates may incorporate various functionally unrelated proteins. In mammalian diseases this may cause amyloid toxicity, while in yeast this could contribute to prion phenotypes. Insolubility of amyloids in the presence of strong ionic detergents, such as SDS or sarcosyl, allows discrimination between amorphous and amyloid aggregates. Here, we used this property of amyloids to study the interdependence of their formation in yeast. We observed that SDS-resistant polymers of proteins with extended polyglutamine domains caused the appearance of SDS or sarcosyl-insoluble polymers of three tested chromosomally-encoded Q/N-rich proteins, Sup35, Rnq1 and Pub1. These polymers were non-heritable, since they could not propagate in the absence of polyglutamine polymers. Sup35 prion polymers caused the appearance of non-heritable sarcosyl-resistant polymers of Pub1. Since eukaryotic genomes encode hundreds of proteins with long Q/N-rich regions, polymer interdependence suggests that conversion of a single protein into polymer form may significantly affect cell physiology by causing partial transfer of other Q/N-rich proteins into a non-functional polymer state.
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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.