title: Nonlinear sorting, curvature generation, and crowding of endophilin N-BAR on tubular membranes.
abstract: The curvature of biological membranes is controlled by membrane-bound proteins. For example, during endocytosis, the sorting of membrane components, vesicle budding, and fission from the plasma membrane are mediated by adaptor and accessory proteins. Endophilin is a peripherally binding membrane protein that functions as an endocytic accessory protein. Endophilin's membrane tubulation capacity is well known. However, to understand the thermodynamic and mechanical aspects of endophilin function, experimental measurements need to be compared to quantitative theoretical models. We present measurements of curvature sorting and curvature generation of the endophilin A1 N-BAR domain on tubular membranes pulled from giant unilamellar vesicles. At low concentration, endophilin functions primarily as a membrane curvature sensor; at high concentrations, it also generates curvature. We determine the spontaneous curvature induced by endophilin and observe sigmoidal curvature/composition coupling isotherms that saturate at high membrane tensions and protein solution concentrations. The observation of saturation is supported by a strong dependence of lateral diffusion coefficients on protein density on the tether membrane. We develop a nonlinear curvature/composition coupling model that captures our experimental observations. Our model predicts a curvature-induced phase transition among two states with varying protein density and membrane curvature. This transition could act as a switch during endocytosis.
authors: Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
authors: Chen
authors: C
authors: Zhu
authors: Sovan L
authors: SL
authors: Das
authors: Tobias
authors: T
authors: Baumgart
mesh_terms: D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism*; D004058:Diffusion; D008954:Models, Biological; D017711:Nonlinear Dynamics; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D051381:Rats; D013816:Thermodynamics; D053835:Unilamellar Liposomes / Q000737:chemistry / Q000378:metabolism
chemical_list: D053835:Unilamellar Liposomes; D000217:Acyltransferases; C018764:2-acylglycerophosphate acyltransferase