Ervasti J M, Campbell K P
University of Wisconsin, Department of Physiology, Madison 53706.
Curr Opin Cell Biol. 1993 Feb;5(1):82-7. doi: 10.1016/s0955-0674(05)80012-2.
Recent studies have confirmed several predictions concerning the structure and possible function of dystrophin, including a direct interaction with F-actin and an indirect interaction with laminin via linkage through a transmembrane protein complex. The results of the past year support a role for dystrophin in linking the actin cytoskeleton with the extracellular matrix in striated muscle, but they have not explained its function in other tissues.
最近的研究证实了关于肌营养不良蛋白结构和可能功能的几个预测,包括与F-肌动蛋白的直接相互作用以及通过跨膜蛋白复合物与层粘连蛋白的间接相互作用。过去一年的研究结果支持肌营养不良蛋白在横纹肌中将肌动蛋白细胞骨架与细胞外基质连接起来的作用,但尚未解释其在其他组织中的功能。