ArticleProceedings of the National Academy of Sciences of the United States of America2008
Tuning lipid mixtures to induce or suppress domain formation across leaflets of unsupported asymmetric bilayers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.
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Who cites it
120 citing papers in PubMed.
- Quantifying interleaflet coupling of phase behavior and observing anti-registered phases in asymmetric lipid bilayers.Biophysical journal · 2026Article
- A Spectroelectrochemical Study of the Effect of Asymmetry on the Electrochemical Response of Lipid Bilayers.The journal of physical chemistry. B · 2026Article
- Quantifying interleaflet coupling of phase behavior and observing anti-registered phases in asymmetric lipid bilayers.bioRxiv : the preprint server for biology · 2026Article
- Review
- Effect of a scramblase activator upon lipid and probe scrambling and membrane domain formation in HEK 293T cells.Faraday discussions · 2025Article
- The Importance of Bilayer Asymmetry in Biological Membranes: Insights from Model Membranes.Membranes · 2025Review
- Disruption of liquid/liquid phase separation in asymmetric GUVs prepared by hemifusion.bioRxiv : the preprint server for biology · 2024Article
- Coupling liquid phases in 3D condensates and 2D membranes: Successes, challenges, and tools.Biophysical journal · 2024Review
- Methyl-β-cyclodextrin asymmetrically extracts phospholipid from bilayers, granting tunable control over differential stress in lipid vesicles.Soft matter · 2024Article
- Multispherical shapes of vesicles with intramembrane domains.The European physical journal. E, Soft matter · 2024Article
- Biomimetic Lipid Raft: Domain Stability and Interaction with Physiologically Active Molecules.Advances in experimental medicine and biology · 2024Review
- Transmembrane coupling of liquid-like protein condensates.Nature communications · 2023Article
- Seeing the Membrane from Both Sides Now: Lipid Asymmetry and Its Strange Consequences.Cold Spring Harbor perspectives in biology · 2023Review
- Experimentally determined leaflet-leaflet phase diagram of an asymmetric lipid bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- Building Asymmetric Lipid Bilayers for Molecular Dynamics Simulations: What Methods Exist and How to Choose One?Membranes · 2023Review
- Dynamics of asymmetric membranes and interleaflet coupling as intermediates in membrane fusion.Biophysical journal · 2023Article
- Remodeling of yeast vacuole membrane lipidomes from the log (one phase) to stationary stage (two phases).Biophysical journal · 2023Article
- Insights into Asymmetric Liposomes as a Potential Intervention for Drug Delivery Including Pulmonary Nanotherapeutics.Pharmaceutics · 2023Review
- A Theoretical Basis for Nanodomains.The Journal of membrane biology · 2022Review
60 more citing papers are in PubMed but not listed here.
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2 authors.
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Abstract
Plasma membranes of cells are asymmetric in both lipid and protein composition. The mechanism by which proteins on both sides of the membrane colocalize during signaling events is unknown but may be due to the induction of inner leaflet domains by the outer leaflet. Here we show that liquid domains form in asymmetric Montal-Mueller planar bilayers in which one leaflet's composition would phase-separate in a symmetric bilayer and the other's would not. Equally important, by tuning the lipid composition of the second leaflet, we are able to suppress domains in the first leaflet. When domains are present in asymmetric membranes, each leaflet contains regions of three distinct lipid compositions, implying strong interleaflet interactions. Our results show that mechanisms of domain induction between the outer and inner leaflets of cell plasma membranes do not necessarily require the participation of membrane proteins. Based on these findings, we suggest mechanisms by which cells could actively regulate protein function by modulating local lipid composition or interleaflet interactions.
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