WAVE binds Ena/VASP for enhanced Arp2/3 complex-based actin assembly
WAVE binds Ena/VASP for enhanced Arp2/3 complex-based actin assembly
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DOI：
10.1091/mbc.e14-07-1200
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发表时间：
2015-01-01
影响因子：
3.3
通讯作者：
Plastino, Julie
中科院分区：
文献类型：
--
作者：
Havrylenko, Svitlana;Noguera, Philippe;Plastino, Julie
WAVE复合物是Arp 2/3复合物的主要激活剂，用于肌动蛋白丝成核和在运动细胞的板状伪足中组装。在板状伪足突出中的其他重要参与者是Ena/VASP蛋白，其增强肌动蛋白丝伸长。在这里，我们研究的Arp 2/3复合物的成核活性和延伸活性的Ena/VASP蛋白的肌动蛋白网络的形成之间的分子协调。使用在体外珠运动性测定，我们表明，波直接结合VASP，导致在Arp2/3复合物为基础的肌动蛋白组件的增加。我们表明，这种相互作用是重要的，在体内以及，在秀丽隐杆线虫胚胎发生的腹外壳事件的形成板状伪足。Ena/VASP结合F-肌动蛋白和profilin复合的G-肌动蛋白的能力对于其作用是重要的，而Ena/VASP四聚化不是必需的。我们的数据是一致的想法，即结合Ena/VASP的WAVE增强Arp 2/3复合物的活性和片状lipodial肌动蛋白组装。
The WAVE complex is the main activator of the Arp2/3 complex for actin filament nucleation and assembly in the lamellipodia of moving cells. Other important players in lamellipodial protrusion are Ena/VASP proteins, which enhance actin filament elongation. Here we examine the molecular coordination between the nucleating activity of the Arp2/3 complex and the elongating activity of Ena/VASP proteins for the formation of actin networks. Using an in vitro bead motility assay, we show that WAVE directly binds VASP, resulting in an increase in Arp2/3 complex-based actin assembly. We show that this interaction is important in vivo as well, for the formation of lamellipodia during the ventral enclosure event of Caenorhabditis elegans embryogenesis. Ena/VASP's ability to bind F-actin and profilin-complexed G-actin are important for its effect, whereas Ena/VASP tetramerization is not necessary. Our data are consistent with the idea that binding of Ena/VASP to WAVE potentiates Arp2/3 complex activity and lamellipodial actin assembly.