title: A sub-nanometre view of how membrane curvature and composition modulate lipid packing and protein recruitment.
abstract: Two parameters of biological membranes, curvature and lipid composition, direct the recruitment of many peripheral proteins to cellular organelles. Although these traits are often studied independently, it is their combination that generates the unique interfacial properties of cellular membranes. Here, we use a combination of in vivo, in vitro and in silico approaches to provide a comprehensive map of how these parameters modulate membrane adhesive properties. The correlation between the membrane partitioning of model amphipathic helices and the distribution of lipid-packing defects in membranes of different shape and composition explains how macroscopic membrane properties modulate protein recruitment by changing the molecular topography of the membrane interfacial region. Furthermore, our results suggest that the range of conditions that can be obtained in a cellular context is remarkably large because lipid composition and curvature have, under most circumstances, cumulative effects.
authors.affiliation: 1] Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and Centre National de la Recherche Scientifique, UMR 7275, 660 route des Lucioles, 06560 Valbonne, France [2].
authors.forename: Stefano
authors.initials: S
authors.lastname: Vanni
authors.affiliation: 1] Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and Centre National de la Recherche Scientifique, UMR 7275, 660 route des Lucioles, 06560 Valbonne, France [2].
authors.forename: Hisaaki
authors.initials: H
authors.lastname: Hirose
authors.affiliation: Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and Centre National de la Recherche Scientifique, UMR 7275, 660 route des Lucioles, 06560 Valbonne, France.
authors.forename: Hélène
authors.initials: H
authors.lastname: Barelli
authors.affiliation: Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and Centre National de la Recherche Scientifique, UMR 7275, 660 route des Lucioles, 06560 Valbonne, France.
authors.forename: Bruno
authors.initials: B
authors.lastname: Antonny
authors.affiliation: Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and Centre National de la Recherche Scientifique, UMR 7275, 660 route des Lucioles, 06560 Valbonne, France.
authors.forename: Romain
authors.initials: R
authors.lastname: Gautier
mesh_terms: D002448:Cell Adhesion; D002461:Cell Line, Transformed; D002462:Cell Membrane / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D048430:Cell Shape; D004134:Dimyristoylphosphatidylcholine / Q000737:chemistry; D004847:Epithelial Cells / Q000378:metabolism* / Q000648:ultrastructure; D005227:Fatty Acids / Q000737:chemistry; D020690:GTPase-Activating Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D049452:Green Fluorescent Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D010713:Phosphatidylcholines / Q000737:chemistry; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D055213:Retinal Pigment Epithelium / Q000378:metabolism / Q000648:ultrastructure
chemical_list: C503237:ARFGAP1 protein, human; D005227:Fatty Acids; D020690:GTPase-Activating Proteins; D008051:Lipid Bilayers; D010713:Phosphatidylcholines; D011993:Recombinant Fusion Proteins; C485184:enhanced green fluorescent protein; D049452:Green Fluorescent Proteins; C017251:1,2-oleoylphosphatidylcholine; C028694:1-palmitoyl-2-oleoylphosphatidylcholine; D004134:Dimyristoylphosphatidylcholine