ArticleBiophysical journal2025
Formation of multicompartment structures through aging of protein-RNA condensates.
Article in Biophysical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Melatonin Targets Mitochondrial Redox Homeostasis: Optimizing the Intracellular Microenvironment.International journal of molecular sciences · 2026Review
- Competition between protein-RNA clustering and phase separation drives re-entrant phase behavior of hnRNPA1.Nature communications · 2026Article
- Determination of Nucleotide-Nucleotide and Nucleotide-Amino Acid Binding Interactions from All-Atom Potential-of-Mean-Force Calculations.ACS physical chemistry Au · 2026Article
- Transient pH changes drive vacuole formation in enzyme-polymer condensates.Nature chemical engineering · 2026Article
- Immiscible proteins compete for RNA binding to order condensate layers.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Microscopy-based techniques for studying the material properties of biomolecular condensates in the cellular environment.Biophysical reviews · 2025Review
- The role of RNA in the nanoscale organization of α-synuclein phase separation.NAR molecular medicine · 2025Article
- Aging of biomolecular condensates reveals complexity-Through diffusion dynamics.Biophysical journal · 2025Article
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Authors and funding
6 authors.
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Abstract
Cells can dynamically organize reactions through the formation of biomolecular condensates. These viscoelastic networks exhibit complex material properties and mesoscale architectures, including the ability to form multiphase assemblies. It was shown previously that condensates with complex architectures may arise at equilibrium in multicomponent systems or in condensates that were driven out of equilibrium by changes in external parameters such as temperature. In this study, we demonstrate that the aging of initially homogeneous protein-RNA condensates can spontaneously lead to the formation of kinetically arrested double-emulsion and core-shell structures without changes in external variables such as temperature or solution conditions. By combining time-resolved fluorescence-based experimental techniques with simulations based on the Cahn-Hilliard theory, we show that, as the protein-RNA condensates age, the decrease of the relative strength of protein-RNA interactions induces the release of RNA molecules from the dense phase. In condensates exceeding a critical size, aging combined with slow diffusion of the macromolecules trigger nucleation of dilute phase inside the condensates, which leads to the formation of double-emulsion structures. These findings illustrate a new mechanism of formation of multicompartment condensates.
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