Cooper J A, Schafer D A
Department of Cell Biology, Washington University, Box 8228, St Louis, MO 631110, USA.
Curr Opin Cell Biol. 2000 Feb;12(1):97-103. doi: 10.1016/s0955-0674(99)00062-9.
The most important discovery in the field is that the Arp2/3 complex nucleates assembly of actin filaments with free barbed ends. Arp2/3 also binds the sides of actin filaments to create a branched network. Arp2/3's nucleation activity is stimulated by WASP family proteins, some of which mediate signaling from small G-proteins. Listeria movement caused by actin polymerization can be reconstituted in vitro using purified proteins: Arp2/3 complex, capping protein, actin depolymerizing factor/cofilin, and actin. actin depolymerizing factor/cofilin increases the rate at which actin subunits leave pointed ends, and capping protein caps barbed ends.
该领域最重要的发现是,Arp2/3复合物能使带有游离刺端的肌动蛋白丝成核组装。Arp2/3还与肌动蛋白丝的侧面结合,形成一个分支网络。WASP家族蛋白可刺激Arp2/3的成核活性,其中一些蛋白介导来自小G蛋白的信号传导。利用纯化的蛋白质,可在体外重建由肌动蛋白聚合引起的李斯特菌运动:Arp2/3复合物、封端蛋白、肌动蛋白解聚因子/丝切蛋白和肌动蛋白。肌动蛋白解聚因子/丝切蛋白可提高肌动蛋白亚基从尖端离开的速率,封端蛋白则封闭刺端。