ArticleScience advances2022
Biomolecular condensates can both accelerate and suppress aggregation of α-synuclein.
Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed, 118 citations in OpenAlex.
- α-Synuclein Forms Distinct Micelle-Like Assemblies at Low Ionic Strengths.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Liquid-liquid phase-separated tau colocalizes with and stabilizes Aβ oligomers.Communications chemistry · 2026Article
- Inhibition and Formation of Amyloid Fibrils in the Bulk and at the Interface of Biomolecular Condensates.Angewandte Chemie (International ed. in English) · 2026Review
- Cell-specific Cahn-Hilliard models predict condensed fates of the chromosomal passenger complex.PLoS computational biology · 2026Article
- Divergent effects of pathological α-synuclein truncations and mutations on phase separation.Nature communications · 2026Article
- Liquid-liquid phase separation and the formation of amyloid fibrils from DcpS scavenger enzymes.Scientific reports · 2026Article
- De novo design of peptides localizing at the interface of biomolecular condensates.Nature communications · 2026Article
- An ALS-associated mutation in the C-terminal α-helix of TDP-43 uncouples condensate formation and amyloid assembly.Protein science : a publication of the Protein Society · 2026Article
- Differential effects of α-Synuclein monomers and seeds on the material properties of Tau condensates.bioRxiv : the preprint server for biology · 2026Article
- Folded domains impose structural heterogeneity and attenuated dynamics in biomolecular condensates.Nature communications · 2026Article
- Condensate State as Determinant of Amyloid Pathology in Neurodegeneration.Biomolecules · 2026Review
- Density transitions in the regulation of transcription.Molecular cell · 2026Review
- Decoupling phase separation and fibrillization preserves activity of biomolecular condensates.Nature communications · 2026Article
- A global thermodynamic-kinetic model capturing the hallmarks of liquid-liquid phase separation and amyloid aggregation.Cell reports. Physical science · 2026Article
- The regulatory principles, physiological functions, and phase transition of biomolecular condensates.Frontiers in cell and developmental biology · 2026Review
- Protein codes and mobility together shape cellular function and disease.Trends in biochemical sciences · 2026Review
- Viscoelasticity and interface properties of multi-component condensates govern protein sequestration and suppression of amyloid formation.bioRxiv : the preprint server for biology · 2025Article
- Control of encounter kinetics by chemically active droplets.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- APOE Genotype Difference in the Biphasic Modulation of Amyloid-β Aggregation by Direct Binding and Lowering the Nucleation Barrier.Biomacromolecules · 2025Article
- Cardiolipin and mitochondrial membrane integrity in neurodegeneration: insights from α-synuclein-driven Parkinson's disease.Acta neuropathologica communications · 2025Review
11 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biomolecular condensates present in cells can fundamentally affect the aggregation of amyloidogenic proteins and play a role in the regulation of this process. While liquid-liquid phase separation of amyloidogenic proteins by themselves can act as an alternative nucleation pathway, interaction of partly disordered aggregation-prone proteins with preexisting condensates that act as localization centers could be a far more general mechanism of altering their aggregation behavior. Here, we show that so-called host biomolecular condensates can both accelerate and slow down amyloid formation. We study the amyloidogenic protein α-synuclein and two truncated α-synuclein variants in the presence of three types of condensates composed of nonaggregating peptides, RNA, or ATP. Our results demonstrate that condensates can markedly speed up amyloid formation when proteins localize to their interface. However, condensates can also significantly suppress aggregation by sequestering and stabilizing amyloidogenic proteins, thereby providing living cells with a possible protection mechanism against amyloid formation.
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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.