ArticleeLife2014
Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 34 papers.
What it found
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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.
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
34 citing papers in PubMed.
- [PSI]-CIC: A Deep-Learning Pipeline for the Annotation of Sectored Saccharomyces cerevisiae Colonies.Bulletin of mathematical biology · 2024Article
- The middle domain of Hsp104 can ensure substrates are functional after processing.PLoS genetics · 2024Article
- Overexpression of Hsp104 by Causing Dissolution of the Prion Seeds Cures the Yeast [International journal of molecular sciences · 2023Article
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
- Article
- AAA+ proteins: one motor, multiple ways to work.Biochemical Society transactions · 2022Review
- The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors.Journal of neuropathology and experimental neurology · 2021Review
- Sis1 potentiates the stress response to protein aggregation and elevated temperature.Nature communications · 2020Article
- The actin cytoskeletal network plays a role in yeast prion transmission and contributes to prion stability.Molecular microbiology · 2020Article
- The clinical trial landscape in amyotrophic lateral sclerosis-Past, present, and future.Medicinal research reviews · 2020Review
- How and why to build a mathematical model: A case study using prion aggregation.The Journal of biological chemistry · 2020Review
- Article
- The huntingtin inclusion is a dynamic phase-separated compartment.Life science alliance · 2019Article
- Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.Molecules (Basel, Switzerland) · 2019Review
- Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.Cold Spring Harbor perspectives in biology · 2019Review
- Engineered protein disaggregases mitigate toxicity of aberrant prion-like fusion proteins underlying sarcoma.The Journal of biological chemistry · 2019Article
- Role of the Cell Asymmetry Apparatus and Ribosome-Associated Chaperones in the Destabilization of aGenetics · 2019Article
- AAA+ Protein-Based Technologies to Counter Neurodegenerative Disease.Biophysical journal · 2019Review
- Potentiating Hsp104 activity via phosphomimetic mutations in the middle domain.FEMS yeast research · 2018Article
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
Abstract
The proteostasis network has evolved to support protein folding under normal conditions and to expand this capacity in response to proteotoxic stresses. Nevertheless, many pathogenic states are associated with protein misfolding, revealing in vivo limitations on quality control mechanisms. One contributor to these limitations is the physical characteristics of misfolded proteins, as exemplified by amyloids, which are largely resistant to clearance. However, other limitations imposed by the cellular environment are poorly understood. To identify cell-based restrictions on proteostasis capacity, we determined the mechanism by which thermal stress cures the [PSI(+)]/Sup35 prion. Remarkably, Sup35 amyloid is disassembled at elevated temperatures by the molecular chaperone Hsp104. This process requires Hsp104 engagement with heat-induced non-prion aggregates in late cell-cycle stage cells, which promotes its asymmetric retention and thereby effective activity. Thus, cell division imposes a potent limitation on proteostasis capacity that can be bypassed by the spatial engagement of a quality control factor.
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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.