Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
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DOI：
10.1126/science.281.5373.105
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发表时间：
1998-07-03
期刊：
影响因子：
56.9
通讯作者：
Mitchison, TJ
中科院分区：
文献类型：
--
作者：
Welch, MD;Rosenblatt, J;Mitchison, TJ
单核细胞增生性李斯特菌细胞表面的肌动蛋白微丝组装需要细菌表面蛋白和宿主细胞Arp2/3复合体。纯化的Arp2/3复合体在体外加速了肌动蛋白聚合的成核，而纯化的ActA则无此作用。然而，当Arp2/3复合体和Acta结合时，协同刺激肌动蛋白细丝的成核。这种激活宿主Arp2/3复合体的机制可能类似于细胞控制Arp2/3复合体活性的策略，从而控制肌动蛋白聚合的空间和时间分布。
Actin filament assembly at the cell surface of the pathogenic bacterium Listeria monocytogenes requires the bacterial ActA surface protein and the host cell Arp2/3 complex. Purified Arp2/3 complex accelerated the nucleation of actin polymerization in vitro, but pure ActA had no effect. However, when combined, the Arp2/3 complex and ActA synergistically stimulated the nucleation of actin filaments. This mechanism of activating the host Arp2/3 complex at the L. monocytogenes surface may be similar to the strategy used by cells to control Arp2/3 complex activity and hence the spatial and temporal distribution of actin polymerization.