title: Deciphering the BAR code of membrane modulators.
abstract: The BAR domain is the eponymous domain of the "BAR-domain protein superfamily", a large and diverse set of mostly multi-domain proteins that play eminent roles at the membrane cytoskeleton interface. BAR domain homodimers are the functional units that peripherally associate with lipid membranes and are involved in membrane sculpting activities. Differences in their intrinsic curvatures and lipid-binding properties account for a large variety in membrane modulating properties. Membrane activities of BAR domains are further modified and regulated by intramolecular or inter-subunit domains, by intermolecular protein interactions, and by posttranslational modifications. Rather than providing detailed cell biological information on single members of this superfamily, this review focuses on biochemical, biophysical, and structural aspects and on recent findings that paradigmatically promote our understanding of processes driven and modulated by BAR domains.
authors.affiliation: Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, Dr. Bohr-Gasse 9, 1030, Vienna, Austria.
authors.forename: Ulrich
authors.initials: U
authors.lastname: Salzer
authors.affiliation: Max F. Perutz Laboratories, Department of Structural and Computational Biology, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria.
authors.forename: Julius
authors.initials: J
authors.lastname: Kostan
authors.affiliation: Max F. Perutz Laboratories, Department of Structural and Computational Biology, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria. kristina.djinovic@univie.ac.at.|Department of Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Večna pot 119, 1000, Ljubljana, Slovenia. kristina.djinovic@univie.ac.at.
authors.forename: Kristina
authors.identifier: 0000-0003-0252-2972
authors.initials: K
authors.lastname: Djinović-Carugo
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D010766:Phosphorylation; D011485:Protein Binding; D000072417:Protein Domains; D025941:Protein Interaction Mapping
chemical_list: D008565:Membrane Proteins
keywords: F-BAR domain; I-BAR domain; Membrane curvature; Membrane remodelling; N-BAR domain; lipid binding