title: Amphipathic helices and membrane curvature.
abstract: Numerous data have been collected on lipid-binding amphipathic helices involved in membrane-remodeling machineries and vesicular transport. Here we describe how, with regard to lipid composition, the physicochemical features of some amphipathic helices explain their ability to recognize membrane curvature or to participate in membrane remodeling. We propose that sensing highly-curved membranes requires that the polar and hydrophobic faces of the helix do not cooperate in lipid binding. A more detailed description of the interaction between amphipathic helices and lipids is however needed; notably to explain how new helices contribute to detection of modest changes in curvature or even negative curvature.
authors.affiliation: Université de Nice-Sophia Antipolis and CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, Valbonne, France. drin@ipmc.cnrs.fr
authors.forename: Guillaume
authors.initials: G
authors.lastname: Drin
authors.forename: Bruno
authors.initials: B
authors.lastname: Antonny
mesh_terms: D000595:Amino Acid Sequence / Q000502:physiology; D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000502:physiology* / Q000648:ultrastructure; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008560:Membrane Fluidity / Q000502:physiology*; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000502:physiology; D008954:Models, Biological; D008958:Models, Molecular; D017510:Protein Folding; D017433:Protein Structure, Secondary / Q000502:physiology*
chemical_list: D008563:Membrane Lipids; D008565:Membrane Proteins