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首页> 外文期刊>Biochemistry >Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments.
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Regulation of actin filament dynamics by actin depolymerizing factor/cofilin and actin-interacting protein 1: new blades for twisted filaments.

机译：通过肌动蛋白解聚因子/ cofilin和与肌动蛋白相互作用的蛋白1调节肌动蛋白丝的动力学：扭曲丝的新刀片。

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摘要

Actin depolymerizing factor (ADF)/cofilin enhances turnover of actin filaments by severing and depolymerizing filaments. A number of proteins functionally interact with ADF/cofilin to modulate the dynamics of actin filaments. Actin-interacting protein 1 (AIP1) has emerged as a conserved WD-repeat protein that specifically enhances ADF/cofilin-induced actin dynamics. Interaction of AIP1 with actin was originally characterized by a yeast two-hybrid system. However, biochemical studies revealed its unique activity on ADF/cofilin-bound actin filaments. AIP1 alone has negligible effects on actin filament dynamics, whereas in the presence of ADF/cofilin, AIP1 enhances filament fragmentation by capping ends of severed filaments. Studies in model organisms demonstrated that AIP1 genetically interacts with ADF/cofilin and participates in several actin-dependent cellular events. The crystal structure of AIP1 revealed its unique structure with two seven-bladed beta-propeller domains. Thus, AIP1 is a new class of actin regulatory proteins that selectively enhances ADF/cofilin-dependent actin filament dynamics.
机译：肌动蛋白解聚因子（ADF）/ cofilin通过切断和解聚长丝来提高肌动蛋白丝的周转率。许多蛋白质在功能上与ADF / cofilin相互作用，以调节肌动蛋白丝的动力学。肌动蛋白相互作用蛋白1（AIP1）已作为一种保守的WD重复蛋白出现，该蛋白专门增强ADF / cofilin诱导的肌动蛋白动力学。 AIP1与肌动蛋白的相互作用最初的特征是酵母双杂交系统。然而，生化研究表明其对ADF / cofilin结合的肌动蛋白丝具有独特的活性。单独的AIP1对肌动蛋白丝的动力学影响微不足道，而在ADF / cofilin的存在下，AIP1通过覆盖切断的丝的末端来增强丝断裂。对模型生物的研究表明，AIP1与ADF / cofilin发生了遗传相互作用，并参与了多种肌动蛋白依赖性细胞事件。 AIP1的晶体结构显示了其独特的结构，带有两个七叶β-螺旋桨结构域。因此，AIP1是一类新型的肌动蛋白调节蛋白，可选择性增强ADF / cofilin依赖性肌动蛋白丝的动力学。

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