title: Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis.
abstract: Endocytosis is an important way for cells to take up liquids and particles from their environment. It requires membrane bending to be coupled with membrane fission, and the actin cytoskeleton has an active role in membrane remodelling. Here, we review recent research into the function of Bin-Amphiphysin-Rvs (BAR) domain proteins, which can sense membrane curvature and recruit actin to membranes. BAR proteins interact with the endocytic and cytoskeletal machinery, including the GTPase dynamin (which mediates vesicle fission), N-WASP (an Arp2/3 complex regulator) and synaptojanin (a phosphoinositide phosphatase). We describe three classes of BAR domains, BAR, N-BAR and F-BAR, providing examples of each discussing and how they function in linking membranes to the actin cytoskeleton in endocytosis.
authors.affiliation: School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK.
authors.forename: John C
authors.initials: JC
authors.lastname: Dawson
authors.forename: John A
authors.initials: JA
authors.lastname: Legg
authors.forename: Laura M
authors.initials: LM
authors.lastname: Machesky
mesh_terms: D000199:Actins / Q000502:physiology*; D000818:Animals; D002352:Carrier Proteins / Q000502:physiology*; D002455:Cell Division / Q000502:physiology; D002462:Cell Membrane / Q000502:physiology*; D002966:Clathrin / Q000502:physiology*; D003034:Coated Pits, Cell-Membrane / Q000502:physiology; D003599:Cytoskeleton / Q000502:physiology; D034281:Dynamins / Q000378:metabolism; D004705:Endocytosis / Q000502:physiology*; D006801:Humans; D008563:Membrane Lipids / Q000502:physiology; D008565:Membrane Proteins / Q000502:physiology*
chemical_list: D000199:Actins; D002352:Carrier Proteins; D002966:Clathrin; D008563:Membrane Lipids; D008565:Membrane Proteins; D034281:Dynamins