ArticlePLoS genetics2014
Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.
Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 41 citations in OpenAlex.
- Mapping of Prion Structures in the Yeast Rnq1.International journal of molecular sciences · 2024Article
- How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023Review
- Article
- Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors.Nature communications · 2022Article
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Biochemical Principles in Prion-Based Inheritance.Epigenomes · 2022Review
- Critical Molecular and Cellular Contributors to Tau Pathology.Biomedicines · 2021Review
- Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.Nature structural & molecular biology · 2020Article
- Three J-proteins impact Hsp104-mediated variant-specific prion elimination: a new critical role for a low-complexity domain.Current genetics · 2020Review
- Molecular Chaperones: A Double-Edged Sword in Neurodegenerative Diseases.Frontiers in aging neuroscience · 2020Review
- Identifying Anti-prion Chemical Compounds Using a Newly Established Yeast High-Throughput Screening System.Cell chemical biology · 2019Article
- Review
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Variant-specific and reciprocal Hsp40 functions in Hsp104-mediated prion elimination.Molecular microbiology · 2018Article
- Chaperone functional specificity promotes yeast prion diversity.PLoS pathogens · 2018Article
- Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae.Scientific reports · 2017Article
- Prions, amyloids, and RNA: Pieces of a puzzle.Prion · 2016Review
- Prions and Protein Assemblies that Convey Biological Information in Health and Disease.Neuron · 2016Review
- Specific chaperones and regulatory domains in control of amyloid formation.The Journal of biological chemistry · 2015Review
- W8, a new Sup35 prion strain, transmits distinctive information with a conserved assembly scheme.Prion · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Amyloidogenic proteins associated with a variety of unrelated diseases are typically capable of forming several distinct self-templating conformers. In prion diseases, these different structures, called prion strains (or variants), confer dramatic variation in disease pathology and transmission. Aggregate stability has been found to be a key determinant of the diverse pathological consequences of different prion strains. Yet, it remains largely unclear what other factors might account for the widespread phenotypic variation seen with aggregation-prone proteins. Here, we examined a set of yeast prion variants of the [RNQ+] prion that differ in their ability to induce the formation of another yeast prion called [PSI+]. Remarkably, we found that the [RNQ+] variants require different, non-contiguous regions of the Rnq1 protein for both prion propagation and [PSI+] induction. This included regions outside of the canonical prion-forming domain of Rnq1. Remarkably, such differences did not result in variation in aggregate stability. Our analysis also revealed a striking difference in the ability of these [RNQ+] variants to interact with the chaperone Sis1. Thus, our work shows that the differential influence of various amyloidogenic regions and interactions with host cofactors are critical determinants of the phenotypic consequences of distinct aggregate structures. This helps reveal the complex interdependent factors that influence how a particular amyloid structure may dictate disease pathology and progression.
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