Actin, spectrin, and associated proteins form a periodic cytoskeletal structure in axons.
Actin, spectrin, and associated proteins form a periodic cytoskeletal structure in axons.
复制标题
DOI：
10.1126/science.1232251
复制
发表时间：
2013-01-25
期刊：
影响因子：
--
通讯作者：
Zhuang X
中科院分区：
文献类型：
--
作者：
Xu K;Zhong G;Zhuang X
肌动蛋白和血影蛋白在神经元中起着重要作用，但它们在轴突和树突中的组织尚不清楚。我们使用随机光学重建显微镜（STORM）研究肌动蛋白，血影蛋白和相关蛋白在神经元中的组织。肌动蛋白形成环状结构，环绕轴突的圆周，并沿轴向沿着均匀分布，周期约为180-190 nm。这种周期性结构在树突中没有观察到，而是含有沿着树突轴延伸的长肌动蛋白丝。内收蛋白是一种肌动蛋白加帽蛋白，与肌动蛋白环共定位。Spectrin表现出周期性的结构交替与肌动蛋白和内收蛋白，和相邻的肌动蛋白-内收蛋白环之间的距离是可比的spectrin四聚体的长度。轴突中的钠通道以周期性模式分布，与基于肌动蛋白的细胞骨架相协调。
Actin and spectrin play important roles in neurons, but their organization in axons and dendrites remains unclear. We used stochastic optical reconstruction microscopy (STORM) to study the organization of actin, spectrin and associated proteins in neurons. Actin formed ring-like structures that wrapped around the circumference of axons and evenly spaced along axonal shafts with a periodicity of ~180–190 nm. This periodic structure was not observed in dendrites, which instead contained long actin filaments running along dendritic shafts. Adducin, an actin-capping protein, colocalized with the actin rings. Spectrin exhibited periodic structures alternating with those of actin and adducin, and the distance between adjacent actin-adducin rings was comparable to the length of a spectrin tetramer. Sodium channels in axons were distributed in a periodic pattern coordinated with the underlying actin-spectrin-based cytoskeleton.