ReviewCell cycle (Georgetown, Tex.)2018
Reversible, functional amyloids: towards an understanding of their regulation in yeast and humans.
Review in Cell cycle (Georgetown, Tex.), 2018. 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
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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.
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Who cites it
25 citing papers in PubMed, 61 citations in OpenAlex.
- Functional amyloids as molecular switches: emerging roles in diverse signalling pathways.Biochemical Society transactions · 2026Review
- Uncovering a previously unknown function of polyphosphate in polyadenylated RNA-induced amyloidogenesis of Hfq.The FEBS journal · 2026Article
- Neuronal Death and Biomolecular Condensates: Are There Any New Treatment Options for Alzheimer's Disease?Cells · 2025Review
- How does protein aggregate structure affect mechanisms of disaggregation?Biochemical Society transactions · 2025Review
- Systematic Comparison of Commercial Uranyl-Alternative Stains for Negative- and Positive-Staining Transmission Electron Microscopy of Organic Specimens.Advanced healthcare materials · 2025Article
- On the reversibility of amyloid fibril formation.Biophysics reviews · 2025Review
- The Promising Role of Selenium and Yeast in the Fight Against Protein Amyloidosis.Biological trace element research · 2025Review
- A structural rationale for reversible vs irreversible amyloid fibril formation from a single protein.Nature communications · 2024Article
- Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Assembly and function of the amyloid-like translational repressor Rim4 is coupled with nutrient conditions.The EMBO journal · 2023Article
- Fibril structures of TFG protein mutants validate the identification of TFG as a disease-related amyloid protein by the IMPAcT method.PNAS nexus · 2023Article
- The Effect of Calorie Restriction on Protein Quality Control in Yeast.Biomolecules · 2023Review
- Article
- Molecular Insights into the Self-Assembly of Block Copolymer Suckerin Polypeptides into Nanoconfined β-Sheets.Small (Weinheim an der Bergstrasse, Germany) · 2022Article
- Condensate Formation by Metabolic Enzymes inMicroorganisms · 2022Review
- Reversible amyloids of pyruvate kinase couple cell metabolism and stress granule disassembly.Nature cell biology · 2021Article
- A thiol-based intramolecular redox switch in four-repeat tau controls fibril assembly and disassembly.The Journal of biological chemistry · 2021Article
- The less conserved metal-binding site in human CRISP1 remains sensitive to zinc ions to permit protein oligomerization.Scientific reports · 2021Article
- Functional amyloids of eukaryotes: criteria, classification, and biological significance.Current genetics · 2020Review
- Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein aggregates, and in particular amyloids, are generally considered to be inherently irreversible aberrant clumps, and are often associated with pathologies, such as Alzheimer's disease, Parkinson's disease, or systemic amyloidosis. However, recent evidence demonstrates that some aggregates are not only fully reversible, but also perform essential physiological functions. Despite these new findings, very little is known about how these functional protein aggregates are regulated in a physiological context. Here, we take the yeast pyruvate kinase Cdc19 as an example of a protein forming functional, reversible, solid, amyloid-like aggregates in response to stress conditions. Cdc19 aggregation is regulated via an aggregation-prone low complexity region (LCR). In favorable growth conditions, this LCR is prevented from aggregating by phosphorylation or oligomerization, while upon glucose starvation it becomes exposed and allows aggregation. We suggest that LCR phosphorylation, oligomerization or partner-binding may be general and widespread mechanisms regulating LCR-mediated reversible protein aggregation. Moreover, we show that, as predicted by computational tools, Cdc19 forms amyloid-like aggregates in vitro. Interestingly, we also observe striking similarities between Cdc19 and its mammalian counterpart, PKM2. Indeed, also PKM2 harbors a LCR and contains several peptides with high amyloidogenic propensity, which coincide with known phosphorylation sites. Thus, we speculate that the formation of reversible, amyloid-like aggregates may be a general physiological mechanism for cells to adapt to stress conditions, and that the underlying regulatory mechanisms may be conserved from yeast to humans.
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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.