Inside view of cell locomotion through single-molecule: fast F-/G-actin cycle and G-actin regulation of polymer restoration.
Inside view of cell locomotion through single-molecule: fast F-/G-actin cycle and G-actin regulation of polymer restoration.
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DOI：
10.2183/pjab.86.62
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发表时间：
2010
期刊：
影响因子：
--
通讯作者：
Watanabe N
中科院分区：
文献类型：
--
作者：
Watanabe N
肌动蛋白细胞骨架驱动细胞运动和组织重塑。活细胞荧光单分子成像的发明为直接观察细胞中肌动蛋白重塑过程打开了一扇窗。从那时起，一些意想不到的分子功能被揭示出来。一个是F-actin网络断裂的机制。在片状伪足中，三分之一的新聚合的F-肌动蛋白在10秒内分解。这种快速的F-肌动蛋白周转是由涉及cofilin和AIP 1的丝切断/破坏活性促进的。令人惊讶的快速解离动力学的倒钩端相互作用，包括加帽蛋白表明，F-肌动蛋白营业额可能会通过重复中断/重新组装附近的倒钩端的细丝。肌动蛋白聚合的图像也被揭示出来。在细胞的前缘，Arp 2/3复合物在窄边缘区域高度活化。相比之下，mDia 1及其相关的形成蛋白同源蛋白显示长距离的定向分子运动，利用其进行性肌动蛋白帽的能力。最近，这两个独立开发的项目汇聚成mDia 1介导的丝成核和肌动蛋白解体之间的时空耦合的发现。据推测，G-肌动蛋白的局部浓度波动调节特定肌动蛋白成核剂（包括mDia 1）的肌动蛋白成核效率。药理学扰动和定量分子行为分析协同作用，揭示隐藏在肌动蛋白周转周期和细胞信号传导的分子联系。
The actin cytoskeleton drives cell locomotion and tissue remodeling. The invention of live-cell fluorescence single-molecule imaging opened a window for direct viewing of the actin remodeling processes in the cell. Since then, a number of unanticipated molecular functions have been revealed. One is the mechanism of F-actin network breakdown. In lamellipodia, one third of newly polymerized F-actin disassembles within 10 seconds. This fast F-actin turnover is facilitated by the filament severing/disrupting activity involving cofilin and AIP1. Astoundingly fast dissociation kinetics of the barbed end interactors including capping protein suggests that F-actin turnover might proceed through repetitive disruption/reassembly of the filament near the barbed end. The picture of actin polymerization is also being revealed. At the leading edge of the cell, Arp2/3 complex is highly activated in a narrow edge region. In contrast, mDia1 and its related Formin homology proteins display a long-distance directional molecular movement using their processive actin capping ability. Recently, these two independently-developed projects converged into a discovery of the spatiotemporal coupling between mDia1-mediated filament nucleation and actin disassembly. Presumably, the local concentration fluctuation of G-actin regulates the actin nucleation efficiency of specific actin nucleators including mDia1. Pharmacological perturbation and quantitative molecular behavior analysis synergize to reveal hidden molecular linkages in the actin turnover cycle and cell signaling.
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影响因子：
16
作者：
Andrianantoandro, Ernesto;Pollard, Thomas D.
通讯作者：
Pollard, Thomas D.
影响因子：
64.5
作者：
Ahuja, Rashmi;Pinyol, Roser;Qualmann, Britta
通讯作者：
Qualmann, Britta
影响因子：
64.5
作者：
Boquet, I;Boujemaa, R;Préat, T
通讯作者：
Préat, T
影响因子：
5.7
作者：
Boczkowska, Malgorzata;Rebowski, Grzegorz;Dominguez, Roberto
通讯作者：
Dominguez, Roberto
肌动蛋白去聚合因子（ADF/Cofilin）提高了细丝流动率：基于肌动蛋白的运动的影响。
DOI：
10.1083/jcb.136.6.1307
发表时间：
1997-03-24
期刊：
The Journal of cell biology
影响因子：
--
作者：
Carlier MF;Laurent V;Santolini J;Melki R;Didry D;Xia GX;Hong Y;Chua NH;Pantaloni D
通讯作者：
Pantaloni D