肌动蛋白
胶溶蛋白
拟南芥
细胞生物学
肌动蛋白结合蛋白
肌动蛋白重塑
MDia1公司
踏步
生物
突变体
化学
生物物理学
肌动蛋白细胞骨架
微丝
生物化学
细胞骨架
基因
细胞
作者
Yuhui Zhuang,Yingjie Wang,Cuixia Jiao,Zhonglin Shang,Shanjin Huang
出处
期刊:Plant Journal
[Wiley]
日期:2024-08-02
卷期号:119 (6): 2854-2866
被引量:1
摘要
Being a bona fide actin bundler, Arabidopsis villin5 (VLN5) plays a crucial role in regulating actin stability and organization within pollen tubes. Despite its significance, the precise mechanism through which VLN5 bundles actin filaments has remained elusive. Through meticulous deletion analysis, we have unveiled that the link between gelsolin repeat 6 (G6) and the headpiece domain (VHP), rather than VHP itself, is indispensable for VLN5-mediated actin bundling. Further refinement of this region has pinpointed a critical sequence spanning from Val763 to Ser823, essential for VLN5's actin-bundling activity. Notably, the absence of Val763-Ser823 in VLN5 results in decreased filamentous decoration within pollen tubes and a diminished ability to rescue actin bundling defects in vln2vln5 mutant pollen tubes compared to intact VLN5. Moreover, our findings highlight that the Val763-Ser823 sequence harbors a binding site for F-actin, suggesting that this linker-based F-actin binding site, in conjunction with the F-actin binding site localized in G1-G6, enables a single VLN5 to concurrently bind to two adjacent actin filaments. Therefore, our study unveils a novel mechanism by which VLN5 bundles actin filaments.
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