Tsuchida Mark A, Theriot Julie A
Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305, USA.
ACS Chem Biol. 2007 Apr 24;2(4):221-4. doi: 10.1021/cb700071d.
Actin filament polymerization provides the driving force for several kinds of actin-based motility, propelling loads such as the plasma membrane at the leading edge of a crawling cell, an endosomal vesicle, or an intracellular bacterial pathogen. In these systems, branched filament networks continuously grow while simultaneously remaining attached to the load. Previous experiments have suggested an important role in both actin filament nucleation and filament attachment for a family of proteins called nucleation-promoting factors (NPFs) that stimulate actin branch formation and nucleation by the Arp2/3 complex. A recent report demonstrates that N-WASP, an NPF, uses distinct domains to mediate nucleation and attachment during motility. The surprising details of the biochemical mechanism necessitate reconsideration of the biophysical models proposed for actin-based motility.
肌动蛋白丝聚合作用为多种基于肌动蛋白的运动提供驱动力,推动诸如爬行细胞前缘的质膜、内体囊泡或细胞内细菌病原体等负载。在这些系统中,分支丝网络持续生长,同时保持与负载相连。先前的实验表明,一类称为成核促进因子(NPFs)的蛋白质在肌动蛋白丝成核和丝附着过程中发挥重要作用,它们通过Arp2/3复合物刺激肌动蛋白分支形成和成核。最近的一份报告表明,NPF之一的N-WASP在运动过程中利用不同结构域介导成核和附着。这种生化机制的惊人细节使得有必要重新考虑为基于肌动蛋白的运动所提出的生物物理模型。