Bogusławska Dżamila M, Machnicka Beata, Hryniewicz-Jankowska Anita, Czogalla Aleksander
Faculty of Biological Sciences, University of Zielona Góra, Zielona Góra, Poland.
Cell Mol Biol Lett. 2014 Mar;19(1):158-79. doi: 10.2478/s11658-014-0185-5. Epub 2014 Feb 25.
The spectrin-based membrane skeleton is crucial for the mechanical stability and resilience of erythrocytes. It mainly contributes to membrane integrity, protein organization and trafficking. Two transmembrane protein macro-complexes that are linked together by spectrin tetramers play a crucial role in attaching the membrane skeleton to the cell membrane, but they are not exclusive. Considerable experimental data have shown that direct interactions between spectrin and membrane lipids are important for cell membrane cohesion. Spectrin is a multidomain, multifunctional protein with several distinctive structural regions, including lipid-binding sites within CH tandem domains, a PH domain, and triple helical segments, which are excellent examples of ligand specificity hidden in a regular repetitive structure, as recently shown for the ankyrin-sensitive lipid-binding domain of beta spectrin. In this review, we summarize the state of knowledge about interactions between spectrin and membrane lipids.
基于血影蛋白的膜骨架对于红细胞的机械稳定性和弹性至关重要。它主要有助于膜的完整性、蛋白质组织和运输。由血影蛋白四聚体连接在一起的两个跨膜蛋白大复合体在将膜骨架附着到细胞膜上起着关键作用，但并非唯一作用。大量实验数据表明，血影蛋白与膜脂之间的直接相互作用对于细胞膜黏附很重要。血影蛋白是一种多结构域、多功能的蛋白质，具有几个独特的结构区域，包括CH串联结构域内的脂质结合位点、一个PH结构域和三螺旋片段，这些都是隐藏在规则重复结构中的配体特异性的极佳例子，最近在β血影蛋白的锚蛋白敏感脂质结合结构域中也有体现。在这篇综述中，我们总结了关于血影蛋白与膜脂相互作用的知识现状。
