Max-Delbrück-Centrum for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 Berlin, Germany.
Structure. 2012 Oct 10;20(10):1621-8. doi: 10.1016/j.str.2012.08.028.
Dynamin is a multidomain mechanochemical guanine triphosphatase that catalyzes membrane scission, most notably of clathrin-coated endocytic vesicles. A number of recent publications have provided structural and mechanistic insights into the formation of helical dynamin filaments assembled by dynamic interactions of multiple domains within dynamin. As a prerequisite for membrane scission, this oligomer undergoes nucleotide-triggered large scale dynamic rearrangements. Here, we review these structural findings and discuss how the architecture of dynamin is poised for the assembly into right-handed helical filaments. Based on these data, we propose a structure-based model for dynamin-mediated scission of membranes.
动力蛋白是一种具有多个结构域的机械化学鸟苷三磷酸酶，能催化膜的断裂，尤其是网格蛋白包被的内吞小泡的膜断裂。最近的一些出版物提供了结构和机制方面的见解，揭示了动力蛋白内多个结构域之间的动态相互作用组装成螺旋状动力蛋白丝的过程。作为膜断裂的前提条件，这种寡聚体发生核苷酸触发的大规模动态重排。在这里，我们回顾这些结构发现，并讨论动力蛋白的结构如何为组装成右手螺旋丝做好准备。基于这些数据，我们提出了一个基于结构的模型，用于动力蛋白介导的膜断裂。
