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- W2079465089 abstract "A long matter of debate in membrane traffic biology is how proteins can create or sense membrane curvature. Recent studies have associated either ability of proteins involved in membrane traffic with their structure and the specific physico-chemistry that dictates their binding to the lipid membrane. By using a micromanipulation set-up combining a micropipette used to aspirate Giant Unilamellar Vesicles (GUV) and optical tweezers to extract a tubule out of them, we can precisely control and measure the size of the tubule, and the force needed to hold it (tube force). We studied the binding of both dynamin and its partner amphiphysin, a BAR domain protein. We show that both proteins are able to lower the tube force at high concentration (several micromolar). At these concentrations, both dynamin and amphiphysin are able to tubulate membranes. At much lower concentrations (nanomolar) however, both proteins interacts with the membrane in a curvature coupled manner. Dynamin polymerizes around tubules less than 20nm only, and the amount of amphiphysin bound is linear with increasing curvature. By estimating the coupling coefficient (in the range of 1000) between the amount bound and the curvature, we found that it is the highest value measured for endocytic protein. No modification of the tubule force is observed, indicating that the protein works in these conditions as a membrane curvature sensor.Importantly, we show that proteins that transiently interact with membranes in a curvature-coupled manner can work both as curvature generator or curvature sensor, depending on the conditions. We will compare our in vitro results to the in vivo situation and give some clues about how to discriminate the function of these proteins in vivo.Figure 1: Experimental set-up for the study of dynamin and amphiphysin polymerization." @default.
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- W2079465089 date "2011-02-01" @default.
- W2079465089 modified "2023-09-30" @default.
- W2079465089 title "How Dynamin and Amphiphysin Sense and Generate Membrane Curvature" @default.
- W2079465089 doi "https://doi.org/10.1016/j.bpj.2010.12.368" @default.
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