ArticleBiophysical journal2022
The physics of liquid-to-solid transitions in multi-domain protein condensates.
Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 52 citations in OpenAlex.
- Dynamic yet well-defined organization of the FUS RGG3 dense phase.Communications chemistry · 2026Article
- Droplet growth, Ostwald's rule, and emergence of order in Fused in Sarcoma.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Polo-Like Kinase 1 Phosphorylation Tunes the Functional Viscoelastic Properties of the Centrosome Scaffold.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Tunable metastability of condensates reconciles their dual roles in amyloid fibril formation.Molecular cell · 2025Article
- The mechanobiology of biomolecular condensates.Biophysics reviews · 2025Review
- Separation of sticker-spacer energetics governs the coalescence of metastable condensates.Biophysical journal · 2025Article
- Recent Progress in Modeling and Simulation of Biomolecular Crowding and Condensation Inside Cells.Journal of chemical information and modeling · 2024Review
- Sequence complexity and monomer rigidity control the morphologies and aging dynamics of protein aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Clustering of RNA Polymerase II C-Terminal Domain Models upon Phosphorylation.The journal of physical chemistry. B · 2024Article
- Sequence-specific interactions determine viscoelasticity and aging dynamics of protein condensates.Nature physics · 2024Article
- Ensemble structure of the N-terminal domain (1-267) of FUS in a biomolecular condensate.Biophysical journal · 2024Article
- Conformational fluctuations and phases in fused in sarcoma (FUS) low-complexity domain.Biopolymers · 2024Review
- Challenges in studying the liquid-to-solid phase transitions of proteins using computer simulations.Current opinion in chemical biology · 2023Review
- Modeling the effects of phosphorylation on phase separation of the FUS low-complexity domain.Biophysical journal · 2023Article
- Time-Dependent Material Properties of Aging Biomolecular Condensates from Different Viscoelasticity Measurements in Molecular Dynamics Simulations.The journal of physical chemistry. B · 2023Article
- Phosphorylation sites are evolutionary checkpoints against liquid-solid transition in protein condensates.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Developments in describing equilibrium phase transitions of multivalent associative macromolecules.Current opinion in structural biology · 2023Review
- Biophysics of biomolecular condensates.Biophysical journal · 2023Article
- Macromolecular Crowding Is Surprisingly Unable to Deform the Structure of a Model Biomolecular Condensate.Biology · 2023Article
- Formation of dissipative structures in microscopic models of mixtures with species interconversion.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
Many RNA-binding proteins (RBPs) that assemble into membraneless organelles have a common architecture including disordered prion-like domain (PLD) and folded RNA-binding domain (RBD). An enrichment of PLD within the condensed phase gives rise to formation, on longer time scales, of amyloid-like fibrils (aging). In this study, we employ coarse-grained Langevin dynamics simulations to explore the physical basis for the structural diversity in condensed phases of multi-domain RBPs. We discovered a highly cooperative first-order transition between disordered structures and an ordered phase whereby chains of PLD organize in fibrils with high nematic orientational order. An interplay between homodomain (PLD-PLD) and heterodomain (PLD-RBD) interactions results in variety of structures with distinct spatial architectures. Interestingly, the different structural phases also exhibit vastly different intracluster dynamics of proteins, with diffusion coefficients 5 times (disordered structures) to 50 times (ordered structures) lower than that of the dilute phase. Cooperativity of this liquid-solid transition makes fibril formation highly malleable to mutations or post-translational modifications. Our results provide a mechanistic understanding of how multi-domain RBPs could form assemblies with distinct structural and material properties.
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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.