Structural interaction of cytoskeletal components.
Structural interaction of cytoskeletal components.
复制标题
细胞骨架成分的结构相互作用。
DOI：
10.1083/jcb.90.1.222
复制
发表时间：
1981-07
影响因子：
7.8
通讯作者：
van Blerkom, J
中科院分区：
文献类型：
--
作者：
Schliwa, M;van Blerkom, J
在高压电子显微镜下观察了经去污剂处理的非洲绿色猴肾上皮细胞（BSC-1）和鸡胚成纤维细胞的三维细胞骨架组织。立体图像生成在低和高放大率，以揭示整体细胞骨架形态和不同的细丝类型的结构连续性的细节。通过使用一种改进的提取程序结合重meromyosin亚片段1装饰的肌动蛋白丝，揭示了丝组织的几个新的功能，这表明细胞骨架是一个高度互连的结构单元。除了肌动蛋白丝，中间丝和微管，一类新的丝2- 3纳米直径和30- 300纳米的长度，不结合重merymyosin被证明。它们与其他细胞骨架丝形成端对侧接触，从而充当各种纤维之间的接头，两者都像（例如，肌动蛋白-肌动蛋白）和不同的（例如，肌动蛋白-中间丝，中间肌动蛋白-微管）。其性质不明。除了2至3纳米的细丝，肌动蛋白细丝被证明形成端到侧与其他丝接触。Y形肌动蛋白丝“分支”在细胞周边靠近皱褶和更中央的细胞区域也被大量的中间丝和微管占据。由肌动蛋白丝的亚片段1装饰形成的箭头复合物指向接触位点。肌动蛋白丝也与微管和中间丝形成端侧接触。仔细检查大量肌动蛋白微管接触表明，微管经常改变他们的路线在网站的接触。各种实验诱导的肌动蛋白微管接触的频率的修改可以被证明影响微管的过程。我们的结论是，弯曲微管的结构相互作用与其他细胞骨架元素。对整个细胞和细胞骨架的结构和生化比较表明，前者比后者显示出更紧密的三维网络和更复杂的生化组成。去污剂提取的时间过程的分析强烈地表明，细胞骨架形成结构骨架，细胞质基质的大量蛋白质以有序的方式与该结构骨架缔合以形成“微小梁网络”的特征图像（J. J. Wolosewick和K.R.波特1979. 82：114-139）。
Three-dimensional cytoskeletal organization of detergent-treated epithelial African green monkey kidney cells (BSC-1) and chick embryo fibroblasts was studied in whole-mount preparations visualized in a high voltage electron microscope. Stereo images are generated at both low and high magnification to reveal both overall cytoskeletal morphology and details of the structural continuity of different filament types. By the use of an improved extraction procedure in combination with heavy meromyosin subfragment 1 decoration of actin filaments, several new features of filament organization are revealed that suggest that the cytoskeleton is a highly interconnected structural unit. In addition to actin filaments, intermediate filaments, and microtubules, a new class of filaments of 2- to 3-nm diameter and 30- to 300-nm length that do not bind heavy merymyosin is demonstrated. They form end-to-side contacts with other cytoskeletal filaments, thereby acting as linkers between various fibers, both like (e.g., actin- actin) and unlike (e.g., actin-intermediate filament, intermediate filament-microtubule). Their nature is unknown. In addition to 2- to 3-nm filaments, actin filaments are demonstrated to form end-to-side contacts with other filaments. Y-shaped actin filament “branches” are observed both in the cell periphery close to ruffles and in more central cell areas also populated by abundant intermediate filaments and microtubules. Arrowhead complexes formed by subfragment 1 decoration of actin filaments point towards the contact site. Actin filaments also form end-to-side contacts with microtubules and intermediate filaments. Careful inspection of numerous actin-microtubule contacts shows that microtubules frequently change their course at sites of contact. A variety of experimentally induced modifications of the frequency of actin-microtubule contacts can be shown to influence the course of microtubules. We conclude that bends in microtubules are imposed by structural interactions with other cytoskeletal elements. A structural and biochemical comparison of whole cells and cytoskeletons demonstrates that the former show a more inticate three-dimensional network and a more complex biochemical composition than the latter. An analysis of the time course of detergent extraction strongly suggests that the cytoskeleton forms a structural backbone with which a large number of proteins of the cytoplasmic ground substance associate in an ordered fashion to form the characteristic image of the “microtrabecular network” (J.J. Wolosewick and K.R. Porter. 1979. J. Cell Biol. 82: 114-139).