ArticleMolecular microbiology2014
Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Inactive Proteasomes Routed to Autophagic Turnover Are Confined within the Soluble Fraction of the Cell.Biomolecules · 2022Article
- Review
- Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022Review
- Article
- Prions and the concept of polyprionic inheritance.Current genetics · 2017Review
- Prion-based memory of heat stress in yeast.Prion · 2017Article
- Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.PLoS genetics · 2017Article
- Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress.Cell reports · 2017Article
- Interaction of Prions Causes Heritable Traits in Saccharomyces cerevisiae.PLoS genetics · 2016Article
- Heterologous aggregates promote de novo prion appearance via more than one mechanism.PLoS genetics · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Many neurodegenerative diseases are associated with conversion of a soluble protein into amyloid deposits, but how this is connected to toxicity remains largely unknown. Here, we explore mechanisms of amyloid associated toxicity using yeast. [PIN(+)], the prion form of the Q/N-rich Rnq1 protein, was known to enhance aggregation of heterologous proteins, including the overexpressed Q/N-rich amyloid forming domain of Pin4 (Pin4C), and Pin4C aggregates were known to attract chaperones, including Sis1. Here we show that in [PIN(+)] but not [pin(-)] cells, overexpression of Pin4C is deadly and linked to hyperphosphorylation of aggregated Pin4C. Furthermore, Pin4C aggregation, hyperphosphorylation and toxicity are simultaneously reversed by Sis1 overexpression. Toxicity may result from proteasome overload because hyperphosphorylated Pin4C aggregation is associated with reduced degradation of a ubiquitin-protein degradation reporter. Finally, hyperphosphorylation of endogenous full-length Pin4 was also facilitated by [PIN(+)], revealing that a prion can regulate post-translational modification of another protein.
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Registered trials
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