ArticleProceedings of the National Academy of Sciences of the United States of America2006
Lateral mobility of proteins in liquid membranes revisited.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers.
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156 citing papers in PubMed.
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- Long-range viscosity of the plasma membrane of a living cell measured by a shear-driven flow method.Biophysical journal · 2025Article
- Polymer sailing on rafts within lipid membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Antigen mobility regulates the dynamics and precision of antigen capture in the B cell immune synapse.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Temperature dependence of membrane viscosity of ternary lipid GUV with LBiophysical journal · 2025Article
- Receptor clustering tunes and sharpens the selectivity of multivalent binding.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Monitoring GPCR conformation with GFP-inspired dyes.iScience · 2024Article
- Reciprocal effect on lateral diffusion of receptor for advanced glycation endproducts and toll-like receptor 4 in the HEK293 cell membrane.European biophysics journal : EBJ · 2024Article
- Rapid Enrichment of a Native Multipass Transmembrane Protein via Cell Membrane Electrophoresis through Buffer pH and Ionic Strength Adjustment.Journal of the American Chemical Society · 2024Article
- Effects of grafted polymers on the lipid membrane fluidity.Biophysical journal · 2024Article
- Nanoporous Membranes of Densely Packed Carbon Nanotubes Formed by Lipid-Mediated Self-Assembly.ACS applied bio materials · 2024Review
- Kinetic study of membrane protein interactions: from three to two dimensions.Scientific reports · 2024Article
- Super-resolution microscopy to study membrane nanodomains and transport mechanisms in the plasma membrane.Frontiers in molecular biosciences · 2024Review
- Membrane homeostasis beyond fluidity: control of membrane compressibility.Trends in biochemical sciences · 2023Review
- A perspective of fluorescence microscopy for cellular structural biology with EGFR as witness.Journal of microscopy · 2023Article
- Evolution of the Concepts of Architecture and Supramolecular Dynamics of the Plasma Membrane.Membranes · 2023Review
- Field model for multistate lateral diffusion of various transmembrane proteins observed in living Dictyostelium cells.Journal of cell science · 2023Article
- Hetero-pentamerization determines mobility and conductance of Glycine receptor α3 splice variants.Cellular and molecular life sciences : CMLS · 2022Article
- Modeling Receptor Motility along Advecting Lipid Membranes.Membranes · 2022Review
96 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The biological function of transmembrane proteins is closely related to their insertion, which has most often been studied through their lateral mobility. For >30 years, it has been thought that hardly any information on the size of the diffusing object can be extracted from such experiments. Indeed, the hydrodynamic model developed by Saffman and Delbrück predicts a weak, logarithmic dependence of the diffusion coefficient D with the radius R of the protein. Despite widespread use, its validity has never been thoroughly investigated. To check this model, we measured the diffusion coefficients of various peptides and transmembrane proteins, incorporated into giant unilamellar vesicles of 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine (SOPC) or in model bilayers of tunable thickness. We show in this work that, for several integral proteins spanning a large range of sizes, the diffusion coefficient is strongly linked to the protein dimensions. A heuristic model results in a Stokes-like expression for D, (D proportional, variant 1/R), which fits literature data as well as ours. Diffusion measurement is then a fast and fruitful method; it allows determining the oligomerization degree of proteins or studying lipid-protein and protein-protein interactions within bilayers.
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