Ungewickell E, Bennett P M, Calvert R, Ohanian V, Gratzer W B
Nature. 1979 Aug 30;280(5725):811-4. doi: 10.1038/280811a0.
The formation of a high-molecular weight complex between spectrin and F-actin depends on the presence of a third cytoskeletal constituent, protein 4.1. Electron microscopy shows that in this ternary complex the actin filaments are linked by bridges, which have the appearance of spectrin. The spectrin must be in the tetrameric state for such bridges to form: the dimer is evidently univalent, for it binds but forms no cross-links. G-actin also fails to form extended complexes. It is inferred that in the native cytoskeleton the spectrin is tetrameric and associated with 4.1 and probably oligomers of actin.
血影蛋白与F-肌动蛋白之间高分子量复合物的形成取决于第三种细胞骨架成分——蛋白4.1的存在。电子显微镜显示，在这种三元复合物中，肌动蛋白丝通过具有血影蛋白外观的桥相连。血影蛋白必须处于四聚体状态才能形成这样的桥：二聚体显然是单价的，因为它能结合但不形成交联。G-肌动蛋白也不能形成延伸复合物。据推测，在天然细胞骨架中，血影蛋白是四聚体，并与4.1以及可能的肌动蛋白寡聚体相关联。
