Abstract
Membrane curvature can play a decisive role in demixing of membrane bound proteins, allowing for formation of fluid-like or gel-like proteo-lipid domains responsible of distinct shape (shape creators) and/or function (e.g. topological remodeling). We take advantage of the nanoconfinement offered by the lipid membrane tethers or lipid nanotubes to access such domains and reveal the fine details of their dynamic life. By combining conductance and fluorescence measurements on a lipid nanotube we are able to monitor the nucleation, stepwise growth and disassembly of individual dynamin1 nanodomains and observe reversible changes in membrane shape and topology produced by them. The sensitivity of this method relies on the nanoconfinement of the tube and the correlative analysis of the data, and gives the spatial and temporal resolution needed for the study of dynamic elasticity of non-homogeneous membranes at nanoscales.
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