ArticlePLoS genetics2013
Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability.
Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association.International journal of molecular sciences · 2020Article
- Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.Nature structural & molecular biology · 2020Article
- Calcium-responsive transactivator (CREST) toxicity is rescued by loss of PBP1/ATXN2 function in a novel yeast proteinopathy model and in transgenic flies.PLoS genetics · 2019Article
- [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
- Q-Rich Yeast Prion [Frontiers in molecular neuroscience · 2018Article
- Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.PLoS genetics · 2017Article
- Prions, Chaperones, and Proteostasis in Yeast.Cold Spring Harbor perspectives in biology · 2017Review
- Article
- The Yeast Prion [SWI(+)] Abolishes Multicellular Growth by Triggering Conformational Changes of Multiple Regulators Required for Flocculin Gene Expression.Cell reports · 2015Article
- Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.The Journal of cell biology · 2015Article
- Heterologous aggregates promote de novo prion appearance via more than one mechanism.PLoS genetics · 2015Article
- Hsp40 function in yeast prion propagation: Amyloid diversity necessitates chaperone functional complexity.Prion · 2015Article
- Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.eLife · 2014Article
- Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Molecular microbiology · 2014Article
- Structural variants of yeast prions show conformer-specific requirements for chaperone activity.Molecular microbiology · 2014Article
- Functional diversification of hsp40: distinct j-protein functional requirements for two prions allow for chaperone-dependent prion selection.PLoS genetics · 2014Article
- Article
Corrections and comments
- Commented on by
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Prions are self-propagating conformations of proteins that can cause heritable phenotypic traits. Most yeast prions contain glutamine (Q)/asparagine (N)-rich domains that facilitate the accumulation of the protein into amyloid-like aggregates. Efficient transmission of these infectious aggregates to daughter cells requires that chaperones, including Hsp104 and Sis1, continually sever the aggregates into smaller "seeds." We previously identified 11 proteins with Q/N-rich domains that, when overproduced, facilitate the de novo aggregation of the Sup35 protein into the [PSI(+)] prion state. Here, we show that overexpression of many of the same 11 Q/N-rich proteins can also destabilize pre-existing [PSI(+)] or [URE3] prions. We explore in detail the events leading to the loss (curing) of [PSI(+)] by the overexpression of one of these proteins, the Q/N-rich domain of Pin4, which causes Sup35 aggregates to increase in size and decrease in transmissibility to daughter cells. We show that the Pin4 Q/N-rich domain sequesters Hsp104 and Sis1 chaperones away from the diffuse cytoplasmic pool. Thus, a mechanism by which heterologous Q/N-rich proteins impair prion propagation appears to be the loss of cytoplasmic Hsp104 and Sis1 available to sever [PSI(+)].
Indexed as
Identifiers
What OpenQuestion holds
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.