Davis Lydia, Abdi Khadar, Machius Mischa, Brautigam Chad, Tomchick Diana R, Bennett Vann, Michaely Peter
Department of Cell Biology and Howard Hughes Medical Institute, Duke University Medical Center, Durham, North Carolina 27710, USA.
J Biol Chem. 2009 Mar 13;284(11):6982-7. doi: 10.1074/jbc.M809245200. Epub 2008 Dec 20.
Spectrins are tetrameric actin-cross-linking proteins that form an elastic network, termed the membrane skeleton, on the cytoplasmic surface of cellular membranes. At the plasma membrane, the membrane skeleton provides essential support, preventing loss of membrane material to environmental shear stresses. The skeleton also controls the location, abundance, and activity of membrane proteins that are critical to cell and tissue function. The ability of the skeleton to modulate membrane stability and function requires adaptor proteins that bind the skeleton to membranes. The principal adaptors are the ankyrin proteins, which bind to the beta-subunit of spectrin and to the cytoplasmic domains of numerous integral membrane proteins. Here, we present the crystal structure of the ankyrin-binding domain of human beta2-spectrin at 1.95 A resolution together with mutagenesis data identifying the binding surface for ankyrins on beta2-spectrin.
血影蛋白是一种四聚体肌动蛋白交联蛋白，在细胞膜的细胞质表面形成一个弹性网络，称为膜骨架。在质膜上，膜骨架提供必要的支撑，防止膜材料因环境剪切应力而损失。该骨架还控制着对细胞和组织功能至关重要的膜蛋白的位置、丰度和活性。骨架调节膜稳定性和功能的能力需要衔接蛋白将骨架与膜结合。主要的衔接蛋白是锚蛋白，它与血影蛋白的β亚基以及众多整合膜蛋白的细胞质结构域结合。在这里，我们展示了人β2-血影蛋白锚蛋白结合结构域的晶体结构，分辨率为1.95埃，同时还展示了诱变数据，确定了β2-血影蛋白上锚蛋白的结合表面。
