Synergy between Cyclase-associated protein and Cofilin accelerates actin filament depolymerization by two orders of magnitude.,Nature Communications

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Synergy between Cyclase-associated protein and Cofilin accelerates actin filament depolymerization by two orders of magnitude.
Nature Communications ( IF 14.7 ) Pub Date : 2019-11-22 , DOI: 10.1038/s41467-019-13268-1
Shashank Shekhar _{1,

2,

3} , Johnson Chung ₃ , Jane Kondev ₂ , Jeff Gelles ₃ , Bruce L Goode ₁

Affiliation

Cellular actin networks can be rapidly disassembled and remodeled in a few seconds, yet in vitro actin filaments depolymerize slowly over minutes. The cellular mechanisms enabling actin to depolymerize this fast have so far remained obscure. Using microfluidics-assisted TIRF, we show that Cyclase-associated protein (CAP) and Cofilin synergize to processively depolymerize actin filament pointed ends at a rate 330-fold faster than spontaneous depolymerization. Single molecule imaging further reveals that hexameric CAP molecules interact with the pointed ends of Cofilin-decorated filaments for several seconds at a time, removing approximately 100 actin subunits per binding event. These findings establish a paradigm, in which a filament end-binding protein and a side-binding protein work in concert to control actin dynamics, and help explain how rapid actin network depolymerization is achieved in cells.

中文翻译：

环化酶相关蛋白和 Cofilin 之间的协同作用可将肌动蛋白丝解聚加速两个数量级。

细胞肌动蛋白网络可以在几秒钟内快速分解和重塑，但体外肌动蛋白丝在几分钟内缓慢解聚。迄今为止，使肌动蛋白如此快速解聚的细胞机制仍不清楚。使用微流体辅助 TIRF，我们发现环化酶相关蛋白 (CAP) 和 Cofilin 协同作用，以比自发解聚快 330 倍的速度持续解聚肌动蛋白丝尖端。单分子成像进一步揭示，六聚体 CAP 分子与 Cofilin 修饰的细丝的尖端每次相互作用几秒钟，每次结合事件去除大约 100 个肌动蛋白亚基。这些发现建立了一个范例，其中丝末端结合蛋白和侧结合蛋白协同工作来控制肌动蛋白动力学，并有助于解释细胞中肌动蛋白网络如何快速解聚。

更新日期：2019-11-22

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