Pantaloni D, Boujemaa R, Didry D, Gounon P, Carlier M F
Laboratoire d'Enzymologie et Biochimie Structurale, CNRS, Gif-sur-Yvette, France.
Nat Cell Biol. 2000 Jul;2(7):385-91. doi: 10.1038/35017011.
The Arp2/3 complex is an essential regulator of actin polymerization in response to signalling and generates a dendritic array of filaments in lamellipodia. Here we show that the activated Arp2/3 complex interacts with the barbed ends of filaments to initiate barbed-end branching. Barbed-end branching by Arp2/3 quantitatively accounts for polymerization kinetics and for the length correlation of the branches of filaments observed by electron microscopy. Filament branching is visualized at the surface of Listeria in a reconstituted motility assay. The functional antagonism between the Arp2/3 complex and capping proteins is essential in the maintenance of the steady state of actin assembly and actin-based motility.
Arp2/3复合物是响应信号传导时肌动蛋白聚合的关键调节因子,并在片足中产生丝状伪足的树枝状阵列。我们在此表明,活化的Arp2/3复合物与丝状伪足的尖端相互作用以启动尖端分支。Arp2/3介导的尖端分支在数量上解释了聚合动力学以及电子显微镜观察到的丝状伪足分支的长度相关性。在重组运动分析中,丝状伪足分支在李斯特菌表面可见。Arp2/3复合物与封端蛋白之间的功能拮抗作用对于维持肌动蛋白组装和基于肌动蛋白的运动的稳态至关重要。