Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility
Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility
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DOI：
10.1016/s0092-8674(02)00731-6
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发表时间：
2002-05-17
期刊：
影响因子：
64.5
通讯作者：
Gertler, FB
中科院分区：
文献类型：
--
作者：
Bear, JE;Svitkina, TM;Gertler, FB
细胞运动需要板足突，这是一个由肌动蛋白聚合驱动的过程。Ena/VASP蛋白在突出的板足中积累，促进病原体李斯特菌的快速动蛋白驱动运动。相反，Ena/VASP负向调节细胞易位。为了解决这一矛盾，我们分析了Ena/VASP在板足突中的作用。缺乏Ena/ vasp的板足突出速度较慢，但更持久，这与细胞易位率增加一致。与对照组相比，缺乏Ena/ vasp的板足肌动蛋白网络含有更短、更高度分支的细丝。具有过量Ena/VASP的板足类具有较长的、较少分枝的细丝。在体外，Ena/VASP通过与倒钩端相互作用促进肌动蛋白丝的伸长，从而屏蔽其封盖蛋白。我们得出结论，Ena/VASP通过控制板足内肌动蛋白丝网络的几何形状来调节细胞运动。
Cell motility requires lamellipodial protrusion, a process driven by actin polymerization. Ena/VASP proteins accumulate in protruding lamellipodia and promote the rapid actin-driven motility of the pathogen Listeria. In contrast, Ena/VASP negatively regulate cell translocation. To resolve this paradox, we analyzed the function of Ena/VASP during lamellipodial protrusion. Ena/VASP-deficient lamellipodia protruded slower but more persistently, consistent with their increased cell translocation rates. Actin networks in Ena/VASP-deficient lamellipodia contained shorter, more highly branched filaments compared to controls. Lamellipodia with excess Ena/VASP contained longer, less branched filaments. In vitro, Ena/VASP promoted actin filament elongation by interacting with barbed ends, shielding them from capping protein. We conclude that Ena/VASP regulates cell motility by controlling the geometry of actin filament networks within lamellipodia.