title: Mechanisms of membrane deformation by lipid-binding domains.
abstract: Among an increasing number of lipid-binding domains, a group that not only binds to membrane lipids but also changes the shape of the membrane has been found. These domains are characterized by their strong ability to transform globular liposomes as well as flat plasma membranes into elongated membrane tubules both in vitro and in vivo. Biochemical studies on the structures of these proteins have revealed the importance of the amphipathic helix, which potentially intercalates into the lipid bilayer to induce and/or sense membrane curvature. Among such membrane-deforming domains, BAR and F-BAR/EFC domains form crescent-shaped dimers, suggesting a preference for a curved membrane, which is important for curvature sensing. Bioinformatics in combination with structural analyses has been identifying an increasing number of novel families of lipid-binding domains. This review attempts to summarize the evidence obtained by recent studies in order to gain general insights into the roles of membrane-deforming domains in a variety of biological events.
authors.affiliation: Department of Biochemistry and Molecular Biology, Kobe University Graduate School of Medicine, Kusunoki-cho, Chuo-ku, Japan. titoh@med.kobe-u.ac.jp
authors.forename: Toshiki
authors.initials: T
authors.lastname: Itoh
authors.forename: Tadaomi
authors.initials: T
authors.lastname: Takenawa
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D005110:Extracellular Space / Q000378:metabolism; D006801:Humans; D008563:Membrane Lipids / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D008563:Membrane Lipids; D011506:Proteins