凝胶球蛋白切断和覆盖肌动蛋白丝的机制

IF 12.5 1区生物学 Q1 BIOCHEMISTRY & MOLECULAR BIOLOGY

Nature Structural & Molecular Biology Pub Date : 2024-10-24 DOI:10.1038/s41594-024-01412-5

Kyle R. Barrie, Grzegorz Rebowski, Roberto Dominguez

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引用次数: 0

摘要

Gelsolin 是 Ca2+ 激活的 F-肌动蛋白切断和封顶蛋白家族的典型成员。我们在此报告了F-肌动蛋白倒钩末端与Ca2+结合的人类凝胶溶蛋白的结构。其中一个结构显示凝胶溶蛋白的六个结构域（G1G6）和结构域间连接器缠绕在 F-肌动蛋白上，而另一个结构显示了结构域 G1G3--一个在细胞凋亡过程中观察到的片段--结合在 F-肌动蛋白的两侧。G1G6 在 F-肌动蛋白的一侧，而 G1G3 则在两侧，它们的构象发生了变化，从而引发了断裂。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。

Mechanism of actin filament severing and capping by gelsolin

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Mechanism of actin filament severing and capping by gelsolin

Gelsolin is the prototypical member of a family of Ca2+-activated F-actin severing and capping proteins. Here we report structures of Ca2+-bound human gelsolin at the barbed end of F-actin. One structure reveals gelsolin’s six domains (G1G6) and interdomain linkers wrapping around F-actin, while another shows domains G1G3—a fragment observed during apoptosis—binding 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. The authors use cryo-electron microscopy to reveal two structural states of Ca2+-activated gelsolin bound to the actin filament, illuminating the mechanisms of filament severing and barbed end capping.

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来源期刊

Nature Structural & Molecular Biology BIOCHEMISTRY & MOLECULAR BIOLOGY-BIOPHYSICS

CiteScore

22.00

自引率

1.80%

发文量

160

审稿时长

3-8 weeks

期刊介绍： Nature Structural & Molecular Biology is a comprehensive platform that combines structural and molecular research. Our journal focuses on exploring the functional and mechanistic aspects of biological processes, emphasizing how molecular components collaborate to achieve a particular function. While structural data can shed light on these insights, our publication does not require them as a prerequisite.