title: A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins.
abstract: The discovery of proteins that recognize membrane curvature created a paradigm shift by suggesting that membrane shape may act as a cue for protein localization that is independent of lipid or protein composition. Here we review recent data on membrane curvature sensing by three structurally unrelated motifs: BAR domains, amphipathic helices and membrane-anchored proteins. We discuss the conclusion that the curvature of the BAR dimer is not responsible for sensing and that the sensing properties of all three motifs can be rationalized by the physicochemical properties of the curved membrane itself. We thus anticipate that membrane curvature will promote the redistribution of proteins that are anchored in membranes through any type of hydrophobic moiety, a thesis that broadens tremendously the implications of membrane curvature for protein sorting, trafficking and signaling in cell biology.
authors.affiliation: Bio-Nanotechnology Laboratory, Department of Neuroscience and Pharmacology, University of Copenhagen, 2100 Copenhagen, Denmark.
authors.forename: Vikram Kjøller
authors.initials: VK
authors.lastname: Bhatia
authors.forename: Nikos S
authors.initials: NS
authors.lastname: Hatzakis
authors.forename: Dimitrios
authors.initials: D
authors.lastname: Stamou
mesh_terms: D002462:Cell Membrane / Q000737:chemistry / Q000648:ultrastructure; D008081:Liposomes / Q000737:chemistry / Q000648:ultrastructure; D008560:Membrane Fluidity; D008563:Membrane Lipids / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013499:Surface Properties
chemical_list: D008081:Liposomes; D008563:Membrane Lipids; D008565:Membrane Proteins