title: New insights into BAR domain-induced membrane remodeling.
abstract: Mesoscopic simulations and electron microscopy of N-BAR domain-induced liposome remodeling are used to characterize the process of liposome tubulation and vesiculation. The overall process of membrane remodeling is found to involve complex couplings among the N-BAR protein density, the degree of N-BAR oligomerization, and the membrane density. A comparison of complex remodeled liposome structures from mesoscopic simulations with those measured by electron microscopy experiments suggests that the process of membrane remodeling can be described via an appropriate mesoscopic free energy framework. Liposome remodeling more representative of F-BAR domains is also presented within the mesoscopic simulation framework.
authors.affiliation: Center for Biophysical Modeling and Simulation, University of Utah, Salt Lake City, Utah, USA.
authors.forename: Gary S
authors.initials: GS
authors.lastname: Ayton
authors.forename: Edward
authors.initials: E
authors.lastname: Lyman
authors.forename: Vinod
authors.initials: V
authors.lastname: Krishna
authors.forename: Richard D
authors.initials: RD
authors.lastname: Swenson
authors.forename: Carsten
authors.initials: C
authors.lastname: Mim
authors.forename: Vinzenz M
authors.initials: VM
authors.lastname: Unger
authors.forename: Gregory A
authors.initials: GA
authors.lastname: Voth
mesh_terms: D000217:Acyltransferases / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D004548:Elasticity; D008081:Liposomes / Q000737:chemistry* / Q000378:metabolism*; D008854:Microscopy, Electron; D008954:Models, Biological; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D051381:Rats
chemical_list: D008081:Liposomes; D009419:Nerve Tissue Proteins; C075637:amphiphysin; D000217:Acyltransferases; C018764:2-acylglycerophosphate acyltransferase