Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches
Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches
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DOI：
10.1073/pnas.1911183117
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发表时间：
2020-06-16
影响因子：
11.1
通讯作者：
De La Cruz, Enrique M.
中科院分区：
文献类型：
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作者：
Pandit, Nandan G.;Cao, Wenxiang;De La Cruz, Enrique M.
由Arp2/3复合体形成的分支肌动蛋白丝网络在细胞基本功能中产生和经历机械力，包括细胞运动和内吞作用。在体外和细胞中，外部力量调节分支肌动蛋白网络的组装和结构。关于机械力如何影响肌动蛋白丝网络的分解，特别是分支的解离，人们知之甚少。我们使用微流体对纯化肌动蛋白和裂变酵母Arp2/3复合体形成的分支施加力，并使用全内反射荧光显微镜实时观察脱支事件。在0 pN到2 pN范围内，枝条上的低力加速了它们与母丝的分离，从小时到小时超过两个数量级
Networks of branched actin filaments formed by Arp2/3 complex generate and experience mechanical forces during essential cellular functions, including cell motility and endocytosis. External forces regulate the assembly and architecture of branched actin networks both in vitro and in cells. Considerably less is known about how mechanical forces influence the disassembly of actin filament networks, specifically, the dissociation of branches. We used microfluidics to apply force to branches formed from purified muscle actin and fission yeast Arp2/3 complex and observed debranching events in real time with total internal reflection fluorescence microscopy. Low forces in the range of 0 pN to 2 pN on branches accelerated their dissociation from mother filaments more than two orders of magnitude, from hours to