Salzer Ulrich, Kostan Julius, Djinović-Carugo Kristina
Max F. Perutz Laboratories, Department of Medical Biochemistry, Medical University of Vienna, Dr. Bohr-Gasse 9, 1030, Vienna, Austria.
Max F. Perutz Laboratories, Department of Structural and Computational Biology, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria.
Cell Mol Life Sci. 2017 Jul;74(13):2413-2438. doi: 10.1007/s00018-017-2478-0. Epub 2017 Feb 27.
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.
BAR结构域是“BAR结构域蛋白超家族”的同名结构域,该超家族由大量多样的多结构域蛋白组成,这些蛋白在膜细胞骨架界面发挥着重要作用。BAR结构域同源二聚体是与脂质膜外周结合并参与膜塑形活动的功能单元。它们内在曲率和脂质结合特性的差异导致了膜调节特性的多样性。BAR结构域的膜活性还受到分子内或亚基间结构域、分子间蛋白质相互作用以及翻译后修饰的进一步修饰和调节。本综述并非提供关于该超家族单个成员的详细细胞生物学信息,而是聚焦于生化、生物物理和结构方面,以及最近的研究发现,这些发现典型地促进了我们对由BAR结构域驱动和调节的过程的理解。