凝胶球蛋白切断和覆盖肌动蛋白丝的机制

bioRxiv - Biochemistry Pub Date : 2024-09-10 DOI:10.1101/2024.09.10.612341

Kyle R Barrie, Grzegorz Rebowski, Roberto Dominguez

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引用次数: 0

摘要

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。

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Mechanism of Actin Filament Severing and Capping by Gelsolin

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.

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bioRxiv - Biochemistry

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