ArticleNature chemical biology2026
Molecular basis for the regulation of membrane proteins through preferential lipid solvation.
Article in Nature chemical biology, 2026. 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.
- Folding and Oligomerization of CLC Channels and Transporters.Chemical reviews · 2026Review
- When membrane proteins prefer lipids.Nature chemical biology · 2026Article
- Hydrophobic mismatch induces lipid sorting based on tail unsaturation.bioRxiv : the preprint server for biology · 2026Article
- Membrane Phase, Charge, and Curvature Regulate α-Synuclein Binding Dynamics.bioRxiv : the preprint server for biology · 2026Article
- Why Do Cells Contain Thousands of Lipid Species? Toward an Integrated Framework for Lipid Diversity in Biological Membranes.International journal of molecular sciences · 2026Review
- GlueFinder: A Data-Driven Framework for the Rational Discovery of Molecular Glues.Journal of chemical information and modeling · 2026Article
- Integrated multi-omics analysis reveals distinct microbiota-metabolite signatures and a novel HCN2-2-hydroxybutyric acid interaction in inflammatory bowel disease.Frontiers in nutrition · 2026Article
- Membrane-forming phospholipids allosterically modulate native-state prolyl isomerization in a CNG channel.Protein science : a publication of the Protein Society · 2025Article
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Authors and funding
8 authors.
Funding
Abstract
The mechanism by which lipids regulate membrane proteins remains an open question. While many protein structures reveal associated lipids, neither binding nor regulatory mechanisms can be gleaned from frozen static snapshots, as these processes occur in the context of a dynamic membrane at equilibrium. In this study, we combine single-molecule experiments with computational analyses of lipid dynamics and lipid-solvation energetics to understand how changes in the lipid composition of the membrane influence the dimerization of the CLC-ec1 chloride/proton antiporter. We find this influence does not result from long-lived lipid binding at specific sites, but instead from an inherently dynamic effect known as preferential lipid solvation, which ultimately determines the relative thermodynamic stability of associated and dissociated dimers. This study provides a foundation for linking lipid composition to the modulation of membrane protein conformational equilibria and a framework for discriminating among different lipid regulation mechanisms in membranes.
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