ArticleMolecular and cellular biology2012
Localization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity.
Article in Molecular and cellular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 45 citations in OpenAlex.
- A Story Between s and S: [Het-s] Prion of the FungusMycobiology · 2024Review
- Emergence of the fungal immune system.iScience · 2023Review
- What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022Review
- Molecular Mechanisms and Evolutionary Consequences of Spore Killers in Ascomycetes.Microbiology and molecular biology reviews : MMBR · 2021Review
- The expanding scope of amyloid signalling.Prion · 2021Article
- Article
- Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019Review
- Diversity of Amyloid Motifs in NLR Signaling in Fungi.Biomolecules · 2017Review
- Prion-Like Polymerization in Immunity and Inflammation.Cold Spring Harbor perspectives in biology · 2017Review
- Molecular Mechanisms Regulating Cell Fusion and Heterokaryon Formation in Filamentous Fungi.Microbiology spectrum · 2017Review
- The HET-S/s Prion Motif in the Control of Programmed Cell Death.Cold Spring Harbor perspectives in biology · 2016Review
- Identification of a novel cell death-inducing domain reveals that fungal amyloid-controlled programmed cell death is related to necroptosis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Overlapping Podospora anserina Transcriptional Responses to Bacterial and Fungal Non Self Indicate a Multilayered Innate Immune Response.Frontiers in microbiology · 2016Article
- Key Points Concerning Amyloid Infectivity and Prion-Like Neuronal Invasion.Frontiers in molecular neuroscience · 2016Article
- Theme and variations: evolutionary diversification of the HET-s functional amyloid motif.Scientific reports · 2015Article
- Signal transduction by a fungal NOD-like receptor based on propagation of a prion amyloid fold.PLoS biology · 2015Article
- As a toxin dies a prion comes to life: A tentative natural history of the [Het-s] prion.Prion · 2015Review
- Diversity and variability of NOD-like receptors in fungi.Genome biology and evolution · 2014Article
- Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Molecular microbiology · 2014Article
- Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.PLoS pathogens · 2014Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Prion diseases are associated with accumulation of the amyloid form of the prion protein, but the mechanisms of toxicity are unknown. Amyloid toxicity is also associated with fungal prions. In Podospora anserina, the simultaneous presence of [Het-s] prion and its allelic protein HET-S causes cell death in a self-/nonself-discrimination process. Here, using the prion form of a fragment of HET-s ([PrD(157)(+)]), we show that [Het-s]-HET-S toxicity can be faithfully recapitulated in yeast. Overexpression of Hsp40 chaperone, Sis1, rescues this toxicity by curing cells of [PrD(157)(+)]. We find no evidence for toxic [PrD(157)(+)] conformers in the presence of HET-S. Instead, [PrD(157)(+)] appears to seed HET-S to accumulate at the cell periphery and to form aggregates distinct from visible [PrD(157)(+)] aggregates. Furthermore, HET-S mutants that cause HET-S to be sequestered into [PrD(157)(+)] prion aggregates are not toxic. The localization of HET-S at the cell periphery and its association with cell death was also observed in the native host Podospora anserina. Thus, upon interaction with [Het-s], HET-S localizes to the cell periphery, and this relocalization, rather than the formation of mixed HET-s/HET-S aggregates, is associated with toxicity.
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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.