ArticleScience advances2022
Lipid-driven condensation and interfacial ordering of FUS.
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 9 papers.
What it found
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The trial behind it
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Who cites it
9 citing papers in PubMed.
- Insights into de-mixing and morphology modulation in coacervate-membrane interactions from integrating experiments and simulations.Communications chemistry · 2025Article
- Article
- Viral fusion proteins of classes II and III recognize and reorganize complex biological membranes.Communications biology · 2025Article
- Interplay between membranes and biomolecular condensates in the regulation of membrane-associated cellular processes.Experimental & molecular medicine · 2024Review
- The molecular basis for the increased stability of the FUS-LC fibril at the anionic membrane- and air-water interfaces.Chemical science · 2024Article
- Lipid droplets as substrates for protein phase separation.Biophysical journal · 2024Article
- Fibril formation and ordering of disordered FUS LC driven by hydrophobic interactions.Nature chemistry · 2023Article
- Role of condensates in modulating DNA repair pathways and its implication for chemoresistance.The Journal of biological chemistry · 2023Review
- Remodeling of yeast vacuole membrane lipidomes from the log (one phase) to stationary stage (two phases).Biophysical journal · 2023Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein condensation into liquid-like structures is critical for cellular compartmentalization, RNA processing, and stress response. Research on protein condensation has primarily focused on membraneless organelles in the absence of lipids. However, the cellular cytoplasm is full of lipid interfaces, yet comparatively little is known about how lipids affect protein condensation. Here, we show that nonspecific interactions between lipids and the disordered fused in sarcoma low-complexity (FUS LC) domain strongly affect protein condensation. In the presence of anionic lipids, FUS LC formed lipid-protein clusters at concentrations more than 30-fold lower than required for pure FUS LC. Lipid-triggered FUS LC clusters showed less dynamic protein organization than canonical, lipid-free FUS LC condensates. Lastly, we found that phosphatidylserine membranes promoted FUS LC condensates having β sheet structures, while phosphatidylglycerol membranes initiated unstructured condensates. Our results show that lipids strongly influence FUS LC condensation, suggesting that protein-lipid interactions modulate condensate formation in cells.
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Registered trials
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