title: Structural characteristics of BAR domain superfamily to sculpt the membrane.
abstract: Membrane dynamics is an essential process for cell locomotion, cytokinesis, vesicular transport and organelle morphogenesis. Formation of tubes or buds from a nearly flat membrane is a widely spread feature of the membrane shape changes. The BAR (Bin/Amphiphysin/Rvs-homology) domain dimers exhibit long extended curved shapes and appear to be outstandingly suitable modules for this purpose. So far, crystal structures of 18 independent BAR domains including inverse-BAR domains and FCH-BAR domains have been reported. These atomic models show a vast variation of dimer shapes on a common and simple basic framework. Comparison of the structural variations with respect to differences in membrane sculpting properties provide useful clues about the mechanisms for modifying the framework into a particular dimer that generates and/or senses a distinct curvature set of the membrane.
authors.affiliation: Department of Structural Analysis, National Cardiovascular Center Research Institute, 5-7-1 Fujishiro-dai, Suita, Osaka 565-0865, Japan. masuda61@ri.ncvc.go.jp
authors.forename: Michitaka
authors.initials: M
authors.lastname: Masuda
authors.forename: Naoki
authors.initials: N
authors.lastname: Mochizuki
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry* / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000648:ultrastructure; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000235:genetics; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D009419:Nerve Tissue Proteins; C075637:amphiphysin