Abstract
The protein epsin is believed to be involved in generating the high membrane curvature necessary for vesicle formation in clathrin-mediated endocytosis. To assess the hypothesis that membrane curvature-dependent binding underlies this function, we quantify the curvature dependence of the area density of the epsin ENTH domain bound to cylindrical membranes of adjustable curvature. By fluorescence microscopy, we observe curvature-induced repartitioning of membrane-bound ENTH between flat and highly curved membranes, in cylindrical tethers pulled from micropipette-aspirated giant unilamellar vesicles. We analyze our measurements using a thermodynamic theory and determine the first Leibler curvature-composition coupling coefficient to be reported for an endocytic accessory protein. Thus our results clearly demonstrate and quantify the curvature sensing of epsin. We believe our method will prove useful generally in relating molecular interactions to macroscopic cell membrane remodeling.
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