ArticleThe Journal of cell biology2012
An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component.
Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 49 citations in OpenAlex.
- Actually, what is a gain-of-function mutation?Genetics · 2026Article
- Novel insights into construct toxicity, strain optimization, and primary sequence design for producing recombinant silk fibroin and elastin-like peptide inMetabolic engineering communications · 2023Article
- [PRIONPathogens (Basel, Switzerland) · 2022Article
- Review
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Proteostasis collapse, a hallmark of aging, hinders the chaperone-Start network and arrests cells in G1.eLife · 2019Article
- Proteome-wide signatures of function in highly diverged intrinsically disordered regions.eLife · 2019Article
- More than Just a Phase: Prions at the Crossroads of Epigenetic Inheritance and Evolutionary Change.Journal of molecular biology · 2018Review
- Review
- Discovering Putative Prion-Like Proteins inFrontiers in microbiology · 2018Article
- The frequency of yeast [Microbial cell (Graz, Austria) · 2017Article
- Prions, Chaperones, and Proteostasis in Yeast.Cold Spring Harbor perspectives in biology · 2017Review
- CAMELOT: A machine learning approach for coarse-grained simulations of aggregation of block-copolymeric protein sequences.The Journal of chemical physics · 2015Article
- Autophagy protects against de novo formation of the [PSI+] prion in yeast.Molecular biology of the cell · 2015Article
- Quantitative nature of overexpression experiments.Molecular biology of the cell · 2015Article
- Polyglutamine toxicity in yeast induces metabolic alterations and mitochondrial defects.BMC genomics · 2015Article
- Dynamic droplets: the role of cytoplasmic inclusions in stress, function, and disease.Cellular and molecular life sciences : CMLS · 2015Review
- Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Molecular microbiology · 2014Article
- Dynamic JUNQ inclusion bodies are asymmetrically inherited in mammalian cell lines through the asymmetric partitioning of vimentin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Abstract
Intrinsically disordered proteins play causative roles in many human diseases. Their overexpression is toxic in many organisms, but the causes of toxicity are opaque. In this paper, we exploit yeast technologies to determine the root of toxicity for one such protein, the yeast prion Rnq1. This protein is profoundly toxic when overexpressed but only in cells carrying the endogenous Rnq1 protein in its [RNQ(+)] prion (amyloid) conformation. Surprisingly, toxicity was not caused by general proteotoxic stress. Rather, it involved a highly specific mitotic arrest mediated by the Mad2 cell cycle checkpoint. Monopolar spindles accumulated as a result of defective duplication of the yeast centrosome (spindle pole body [SPB]). This arose from selective Rnq1-mediated sequestration of the core SPB component Spc42 in the insoluble protein deposit (IPOD). Rnq1 does not normally participate in spindle pole dynamics, but it does assemble at the IPOD when aggregated. Our work illustrates how the promiscuous interactions of an intrinsically disordered protein can produce highly specific cellular toxicities through illicit, yet highly specific, interactions with the proteome.
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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.