Sjöblom B, Salmazo A, Djinović-Carugo K
Department for Biomolecular Structural Chemistry, Max F. Perutz Laboratories, University of Vienna, Campus Vienna Biocenter 5, 1030 Vienna, Austria.
Cell Mol Life Sci. 2008 Sep;65(17):2688-701. doi: 10.1007/s00018-008-8080-8.
Alpha-actinin is a cytoskeletal actin-binding protein and a member of the spectrin superfamily, which comprises spectrin, dystrophin and their homologues and isoforms. It forms an anti-parallel rod-shaped dimer with one actin-binding domain at each end of the rod and bundles actin filaments in multiple cell-type and cytoskeleton frameworks. In non-muscle cells, alpha-actinin is found along the actin filaments and in adhesion sites. In striated, cardiac and smooth muscle cells, it is localized at the Z-disk and analogous dense bodies, where it forms a lattice-like structure and stabilizes the muscle contractile apparatus. Besides binding to actin filaments alpha-actinin associates with a number of cytoskeletal and signaling molecules, cytoplasmic domains of transmembrane receptors and ion channels, rendering it important structural and regulatory roles in cytoskeleton organization and muscle contraction. This review reports on the current knowledge on structure and regulation of alpha-actinin.
α-辅肌动蛋白是一种细胞骨架肌动蛋白结合蛋白，属于血影蛋白超家族成员，该超家族包括血影蛋白、肌营养不良蛋白及其同源物和异构体。它形成一个反平行的杆状二聚体，在杆的两端各有一个肌动蛋白结合结构域，并在多种细胞类型和细胞骨架框架中捆绑肌动蛋白丝。在非肌肉细胞中，α-辅肌动蛋白存在于肌动蛋白丝沿线和黏附位点。在横纹肌、心肌和平滑肌细胞中，它定位于Z盘和类似的致密体，在那里它形成晶格状结构并稳定肌肉收缩装置。除了与肌动蛋白丝结合外，α-辅肌动蛋白还与许多细胞骨架和信号分子、跨膜受体和离子通道的细胞质结构域相关联，使其在细胞骨架组织和肌肉收缩中发挥重要的结构和调节作用。本综述报道了关于α-辅肌动蛋白结构和调节的当前知识。
