ArticleJournal of lipid research2020
Nanodomains can persist at physiologic temperature in plasma membrane vesicles and be modulated by altering cell lipids.
Article in Journal of lipid research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 43 citations in OpenAlex.
- Nanodomain formation in lipid bilayers II: The influence of mixed-chain saturated lipids.Biochimica et biophysica acta. Biomembranes · 2026Article
- Nanodomain formation in lipid bilayers I: Quantifying the nanoscopic miscibility transition with FRET.Biochimica et biophysica acta. Biomembranes · 2026Article
- Nanodomain formation in lipid bilayers I: Quantifying the nanoscopic miscibility transition with FRET.bioRxiv : the preprint server for biology · 2026Article
- Nanodomain formation in lipid bilayers II: The influence of mixed-chain saturated lipids.bioRxiv : the preprint server for biology · 2026Article
- PROTEIN-PROTEIN INTERACTION NETWORKS CAN BE HIGHLY SENSITIVE TO THE MEMBRANE PHASE TRANSITION.bioRxiv : the preprint server for biology · 2025Article
- Protein-protein interaction networks can be highly sensitive to the membrane phase transition.ArXiv · 2025Article
- Xanthohumol Sensitizes Melanoma Cells to Vemurafenib by Lowering Membrane Cholesterol and Increasing Membrane Fluidity.International journal of molecular sciences · 2025Article
- Lipid Peroxidation Drives Liquid-Liquid Phase Separation and Disrupts Raft Protein Partitioning in Biological Membranes.Journal of the American Chemical Society · 2024Article
- The Membrane Phase Transition Gives Rise to Responsive Plasma Membrane Structure and Function.Cold Spring Harbor perspectives in biology · 2023Review
- Investigation of nano- and microdomains formed by ceramide 1 phosphate in lipid bilayers.Scientific reports · 2023Article
- Heterogeneous biological membranes regulate protein partitioning via fluctuating diffusivity.PNAS nexus · 2023Article
- Membrane phase separation drives responsive assembly of receptor signaling domains.Nature chemical biology · 2023Article
- The plasma membrane as an adaptable fluid mosaic.Biochimica et biophysica acta. Biomembranes · 2023Review
- Ordered Domain (Raft) Formation in Asymmetric Vesicles and Its Induction upon Loss of Lipid Asymmetry in Artificial and Natural Membranes.Membranes · 2022Article
- The Role of Sphingomyelin and Ceramide in Motor Neuron Diseases.Journal of personalized medicine · 2022Review
- Transbilayer Coupling of Lipids in Cells Investigated by Imaging Fluorescence Correlation Spectroscopy.The journal of physical chemistry. B · 2022Article
- Using cyclodextrin-induced lipid substitution to study membrane lipid and ordered membrane domain (raft) function in cells.Biochimica et biophysica acta. Biomembranes · 2022Review
- Loss of plasma membrane lipid asymmetry can induce ordered domain (raft) formation.Journal of lipid research · 2022Article
- Cholesterol and sphingomyelin are critical for Fcγ receptor-mediated phagocytosis of Cryptococcus neoformans by macrophages.The Journal of biological chemistry · 2021Article
- EPA and DHA differentially modulate membrane elasticity in the presence of cholesterol.Biophysical journal · 2021Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
The formation and properties of liquid-ordered (Lo) lipid domains (rafts) in the plasma membrane are still poorly understood. This limits our ability to manipulate ordered lipid domain-dependent biological functions. Giant plasma membrane vesicles (GPMVs) undergo large-scale phase separations into coexisting Lo and liquid-disordered lipid domains. However, large-scale phase separation in GPMVs detected by light microscopy is observed only at low temperatures. Comparing Förster resonance energy transfer-detected versus light microscopy-detected domain formation, we found that nanodomains, domains of nanometer size, persist at temperatures up to 20°C higher than large-scale phases, up to physiologic temperature. The persistence of nanodomains at higher temperatures is consistent with previously reported theoretical calculations. To investigate the sensitivity of nanodomains to lipid composition, GPMVs were prepared from mammalian cells in which sterol, phospholipid, or sphingolipid composition in the plasma membrane outer leaflet had been altered by cyclodextrin-catalyzed lipid exchange. Lipid substitutions that stabilize or destabilize ordered domain formation in artificial lipid vesicles had a similar effect on the thermal stability of nanodomains and large-scale phase separation in GPMVs, with nanodomains persisting at higher temperatures than large-scale phases for a wide range of lipid compositions. This indicates that it is likely that plasma membrane nanodomains can form under physiologic conditions more readily than large-scale phase separation. We also conclude that membrane lipid substitutions carried out in intact cells are able to modulate the propensity of plasma membranes to form ordered domains. This implies lipid substitutions can be used to alter biological processes dependent upon ordered domains.
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