ArticleProceedings of the National Academy of Sciences of the United States of America2024
Amino acids modulate liquid-liquid phase separation in vitro and in vivo by regulating protein-protein interactions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Seeing the Chemistry of Biomolecular Condensates: In Situ Mapping of Composition and Water Content.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Liquid-liquid phase separation in cancer therapy resistance.iScience · 2026Review
- Partition Coefficients Reveal Changes in Properties of Low-Contrast Biomolecular Condensates.bioRxiv : the preprint server for biology · 2026Article
- Harnessing Phase Separation in the Extracellular Matrix: From Mechanisms to Therapeutic Opportunities.BioMed research international · 2026Review
- The influence of proline on surface interactions in aqueous solutions.Biophysical journal · 2025Article
- Molecular drivers of RNA phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Liquid-Liquid Phase Separation: Mechanisms, Roles, and Implications in Cellular Function and Disease.FASEB bioAdvances · 2025Review
- Amino acids bind to phase-separating proteins and modulate biomolecular condensate stability and dynamics.Nature communications · 2025Article
- Article
- Crosstalk Between Phase-Separated Membraneless Condensates and Membrane-Bound Organelles in Cellular Function and Disease.Advances in experimental medicine and biology · 2025Review
- Amino acids modulate liquid-liquid phase separation in vitro and in vivo by regulating protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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Authors and funding
6 authors.
Funding
Abstract
Liquid-liquid phase separation (LLPS) is an intracellular process widely used by cells for many key biological functions. It occurs in complex and crowded environments, where amino acids (AAs) are vital components. We have found that AAs render the net interaction between proteins more repulsive. Here, we find that some AAs efficiently suppress LLPS in test tubes (in vitro). We then screen all the proteinogenic AAs and find that three specific AAs, including proline, glutamine, and glycine, significantly suppressed the formation of stress granules (SGs) in U2OS and HeLa cell lines (in vivo) irrespective of stress types. We also observe the effect in primary fibroblast cells, a viable cell model for neurodegenerative disorders. Kinetic studies by live-cell microscopy show that the presence of AAs not only slows down the formation but also decreases the saturating number and prevents the coalescence of SGs. We finally use sedimentation-diffusion equilibrium analytical ultracentrifuge (SE-AUC) to demonstrate that the suppression effects of AAs on LLPS may be due to their modulation in protein-protein and RNA-RNA interactions. Overall, this study reveals an underappreciated role of cellular AAs, which may find biomedical applications, especially in treating SG-associated diseases.
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