Hug C, Jay P Y, Reddy I, McNally J G, Bridgman P C, Elson E L, Cooper J A
Department of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110, USA.
Cell. 1995 May 19;81(4):591-600. doi: 10.1016/0092-8674(95)90080-2.
Actin assembly is important for cell motility, but the mechanism of assembly and how it relates to motility in vivo is largely unknown. In vitro, actin assembly can be controlled by proteins, such as capping protein, that bind filament ends. To investigate the function of actin assembly in vivo, we altered the levels of capping protein in Dictyostelium cells and found changes in resting and chemoattractant-induced actin assembly that were consistent with the in vitro properties of capping protein in capping but not nucleation. Significantly, overexpressers moved faster and underexpressers moved slower than control cells. Mutants also exhibited changes in cytoskeleton architecture. These results provide insights into in vivo actin assembly and the role of the actin cytoskeleton in motility.
肌动蛋白组装对于细胞运动很重要,但组装机制以及它在体内如何与运动相关在很大程度上尚不清楚。在体外,肌动蛋白组装可由诸如封端蛋白等结合丝末端的蛋白质控制。为了研究肌动蛋白组装在体内的功能,我们改变了盘基网柄菌细胞中封端蛋白的水平,发现静息状态和趋化因子诱导的肌动蛋白组装变化与封端蛋白在体外封端而非成核的特性一致。值得注意的是,过表达细胞比对照细胞移动得更快,而低表达细胞移动得更慢。突变体还表现出细胞骨架结构的变化。这些结果为体内肌动蛋白组装以及肌动蛋白细胞骨架在运动中的作用提供了见解。