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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.

Original publication

DOI

10.1126/science.1092586

Type

Journal article

Journal

Science

Publication Date

23/01/2004

Volume

303

Pages

495 - 499

Keywords

ADP-Ribosylation Factors, Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, COP-Coated Vesicles, Carrier Proteins, Cell Membrane, Clathrin, Clathrin-Coated Vesicles, Coated Vesicles, Crystallography, X-Ray, Cytoskeletal Proteins, Dimerization, Drosophila, Drosophila Proteins, GTPase-Activating Proteins, Liposomes, Models, Molecular, Molecular Sequence Data, Mutation, Nerve Tissue Proteins, Nuclear Proteins, Phosphoproteins, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary