Visualizing dynamic actin cross-linking processes driven by the actin-binding protein anillin
Visualizing dynamic actin cross-linking processes driven by the actin-binding protein anillin
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DOI：
10.1002/1873-3468.13720
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发表时间：
2019-12-31
期刊：
影响因子：
3.5
通讯作者：
Yajima, Junichiro
中科院分区：
文献类型：
--
作者：
Matsuda, Kyohei;Sugawa, Mitsuhiro;Yajima, Junichiro
苯胺林是一种肌动蛋白丝交联蛋白，在胞质分裂期间稳定基于肌动蛋白的收缩环。为了阐明潜在的肌动蛋白丝和苯胺之间的分子间相互作用，我们利用全内反射荧光显微镜（TIRFM）和高速原子力显微镜（Hs-AFM）。使用TIRFM的单分子成像显示，苯胺作为单体存在，对肌动蛋白丝具有相对较低的结合亲和力。使用Hs-AFM对由苯胺引起的肌动蛋白丝交联动力学的实时成像显示，苯胺单体与肌动蛋白丝在8 nm的距离处交联，并且这些丝的极性是平行和反平行的。这些结果与苯胺在体内肌动蛋白环转换中发挥作用一致，其中它可能是负责使环状非极性肌动蛋白束变薄。
Anillin is a type of actin filament cross-linking protein that stabilizes the actin-based contractile ring during cytokinesis. To elucidate the underlying intermolecular interactions between actin filaments and anillin, we utilized total internal reflection fluorescence microscopy (TIRFM) and high-speed atomic force microscopy (Hs-AFM). Single-molecule imaging of anillin using TIRFM showed that anillin exists as monomers with relatively low binding affinity for actin filaments. Real-time imaging of actin filament cross-linking dynamics induced by anillin using Hs-AFM revealed that anillin monomers cross-link with actin filaments at a distance of 8 nm and that the polarity of those filaments is both parallel and antiparallel. These results are consistent with anillin playing a role in actin ring transition in vivo, where it might be responsible for thinning the ring-shaped apolar actin bundles.