Mechanism of Actin Filament Severing and Capping by Gelsolin

Kyle R Barrie, Grzegorz Rebowski, Roberto Dominguez
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Abstract

Gelsolin is the prototypical member of a family of Ca2+-dependent F-actin severing and capping proteins. A structure of Ca2+-bound full-length gelsolin at the barbed end shows domains G1G6 and the inter-domain linkers wrapping around F-actin. Another structure shows domains G1G3, a fragment produced during apoptosis, on both sides of F-actin. Conformational changes that trigger severing occur on one side of F-actin with G1G6 and on both sides with G1G3. Gelsolin remains bound after severing, blocking subunit exchange.
凝胶球蛋白切断和覆盖肌动蛋白丝的机制
Gelsolin 是依赖 Ca2+ 的 F-肌动蛋白切断和封顶蛋白家族的典型成员。与 Ca2+ 结合的全长 Gelsolin 的倒钩末端结构显示,结构域 G1G6 和结构域间连接器缠绕着 F-肌动蛋白。另一个结构图显示了位于 F-肌动蛋白两侧的结构域 G1G3(一种在细胞凋亡过程中产生的片段)。G1G6在F-肌动蛋白的一侧,G1G3在F-肌动蛋白的两侧,这些构象变化引发了切断。Gelsolin 在断裂后保持结合,阻止亚基交换。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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