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首页> 外文期刊>Journal of Molecular Biology >Real-Time Single-Molecule Kinetic Analyses of AIP1-Enhanced Actin Filament Severing in the Presence of Cofilin
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Real-Time Single-Molecule Kinetic Analyses of AIP1-Enhanced Actin Filament Severing in the Presence of Cofilin

机译：AIP1 - 增强肌肽细丝切割在辛苷存在下的实时单分子动力学分析

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摘要

Rearrangement of actin filaments by polymerization, depolymerization, and severing is important for cell locomotion, membrane trafficking, and many other cellular functions. Cofilin and actin-interacting protein 1 (AIP1; also known as WDR1) are evolutionally conserved proteins that cooperatively sever actin filaments. However, little is known about the biophysical basis of the actin filament severing by these proteins. Here, we performed single-molecule kinetic analyses of fluorescently labeled AIP1 during the severing process of cofilin-decorated actin filaments. Results demonstrated that binding of a single AIP molecule was sufficient to enhance filament severing. After AIP1 binding to a filament, severing occurred with a delay of 0.7 s. Kinetics of binding and dissociation of a single AIP1 molecule to/from actin filaments followed a second-order and a first-order kinetics scheme, respectively. AIP1 binding and severing were detected preferentially at the boundary between the cofilin-decorated and bare regions on actin filaments. Based on the kinetic parameters explored in this study, we propose a possible mechanism behind the enhanced severing by AIP1. (C) 2018 Elsevier Ltd. All rights reserved.
机译：通过聚合，解聚和切割重新排列肌动蛋白长丝对细胞运动，膜运输和许多其他细胞功能非常重要。 Cofilin和肌动蛋白相互作用蛋白1（AIP1;也称为WDR1）是进化保守的蛋白质，其合作切除肌动蛋白细丝。然而，对于这些蛋白质的肌动蛋白细丝切割的生物物理基础知之甚少。这里，在辛苷装饰肌动蛋白长丝的切断过程中，我们在切断过程中进行了单分子动力学分析。结果表明，单个AIP分子的结合足以增强长丝切割。在AIP1结合到长丝之后，切断发生延迟0.7秒。单个AIP1分子与肌动蛋白长丝的结合和解离的动力学分别为二阶和一阶动力学方案。优先检测AIP1结合和切断，在肌蛋白长丝上的Cofilin装饰和裸区域之间的边界处检测到。根据本研究探索的动力学参数，我们提出了AIP1增强切断后的可能机制。 （c）2018年elestvier有限公司保留所有权利。

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