title: BAR domains as sensors of membrane curvature: the amphiphysin BAR structure.
abstract: The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module.
authors.affiliation: Medical Research Council (MRC) Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
authors.forename: Brian J
authors.initials: BJ
authors.lastname: Peter
authors.forename: Helen M
authors.initials: HM
authors.lastname: Kent
authors.forename: Ian G
authors.initials: IG
authors.lastname: Mills
authors.forename: Yvonne
authors.initials: Y
authors.lastname: Vallis
authors.forename: P Jonathan G
authors.initials: PJ
authors.lastname: Butler
authors.forename: Philip R
authors.initials: PR
authors.lastname: Evans
authors.forename: Harvey T
authors.initials: HT
authors.lastname: McMahon
mesh_terms: D020727:ADP-Ribosylation Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D048868:Adaptor Proteins, Signal Transducing; D000595:Amino Acid Sequence; D000818:Animals; D022181:COP-Coated Vesicles / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D002966:Clathrin / Q000378:metabolism; D022163:Clathrin-Coated Vesicles / Q000378:metabolism; D018699:Coated Vesicles / Q000737:chemistry / Q000378:metabolism*; D018360:Crystallography, X-Ray; D003598:Cytoskeletal Proteins; D019281:Dimerization; D004330:Drosophila / Q000737:chemistry; D029721:Drosophila Proteins / Q000737:chemistry* / Q000378:metabolism*; D020690:GTPase-Activating Proteins / Q000737:chemistry / Q000378:metabolism; D008081:Liposomes / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: C503237:ARFGAP1 protein, human; C503240:ARFGAP3 protein, human; C101158:ARFIP2 protein, human; C504466:ARHGAP17 protein, human; D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins; D002966:Clathrin; D003598:Cytoskeletal Proteins; D029721:Drosophila Proteins; D020690:GTPase-Activating Proteins; D008081:Liposomes; D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; D010750:Phosphoproteins; C075637:amphiphysin; D020727:ADP-Ribosylation Factors