ArticleThe Journal of biological chemistry2013
Non-targeted identification of prions and amyloid-forming proteins from yeast and mammalian cells.
Article in The Journal of biological chemistry, 2013. 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, 67 citations in OpenAlex.
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- Tissue-specific landscape of protein aggregation and quality control in an aging vertebrate.Developmental cell · 2024Article
- Identification of protein aggregates in the aging vertebrate brain with prion-like and phase-separation properties.Cell reports · 2024Article
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- Protein aggregation and the evolution of stress resistance in clinical yeast.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021Article
- Cell-free reconstitution of multi-condensate assemblies.Methods in enzymology · 2021Article
- Functional amyloids of eukaryotes: criteria, classification, and biological significance.Current genetics · 2020Review
- Detection of Protein Aggregation in LiveAntimicrobial agents and chemotherapy · 2020Article
- A complete catalog of wild-type Sup35 prion variants and their protein-only propagation.Current genetics · 2020Article
- RNA-binding protein FXR1 is presented in rat brain in amyloid form.Scientific reports · 2019Article
- An extensively glycosylated archaeal pilus survives extreme conditions.Nature microbiology · 2019Article
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Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The formation of amyloid aggregates is implicated both as a primary cause of cellular degeneration in multiple human diseases and as a functional mechanism for providing extraordinary strength to large protein assemblies. The recent identification and characterization of several amyloid proteins from diverse organisms argues that the amyloid phenomenon is widespread in nature. Yet identifying new amyloid-forming proteins usually requires a priori knowledge of specific candidates. Amyloid fibers can resist heat, pressure, proteolysis, and denaturation by reagents such as urea or sodium dodecyl sulfate. Here we show that these properties can be exploited to identify naturally occurring amyloid-forming proteins directly from cell lysates. This proteomic-based approach utilizes a novel purification of amyloid aggregates followed by identification by mass spectrometry without the requirement for special genetic tools. We have validated this technique by blind identification of three amyloid-based yeast prions from laboratory and wild strains and disease-related polyglutamine proteins expressed in both yeast and mammalian cells. Furthermore, we found that polyglutamine aggregates specifically recruit some stress granule components, revealing a possible mechanism of toxicity. Therefore, core amyloid-forming proteins as well as strongly associated proteins can be identified directly from cells of diverse origin.
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