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首页> 外文期刊>Cell communication & adhesion >F-actin Binding Region of SPIN90 C-terminus Is Essential for Actin Polymerization and Lamellipodia Formation
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F-actin Binding Region of SPIN90 C-terminus Is Essential for Actin Polymerization and Lamellipodia Formation

机译：SPIN90 C端的F-肌动蛋白结合区是肌动蛋白聚合和Lamellipodia形成所必需的。

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We recently reported that SPIN90 is able to bind with several proteins involved in regulating actin cytoskeleton networks, including dynamin, WASP, PIX, and Nck. Based on these findings, we investigated how SPIN90 regulates the actin cytoskeleton and promotes actin assembly. This study demonstrated that aluminium fluoride-induced localization of SPIN90 to lamellipodia requires amino acids 582-722 at the SPIN90 C-terminus, which is also essential for F-actin binding and Arp2/3 complex mediated polymerization of actin into branched actin filaments. Furthermore, after deletion of the F-actin binding region (582-722 SPIN90) failed to localize at the membrane edge and was unable to promote lamellipodia formation, suggesting that the F-actin binding region in the SPIN90 C-terminus is essential for the formation of branched actin networks and regulation of the actin cytoskeleton at the leading edge of cells.
机译：我们最近报道，SPIN90能够与几种参与调节肌动蛋白细胞骨架网络的蛋白质结合，包括动力蛋白，WASP，PIX和Nck。基于这些发现，我们研究了SPIN90如何调节肌动蛋白的细胞骨架并促进肌动蛋白组装。这项研究表明，氟化铝诱导的SPIN90定位于片状脂蛋白，需要在SPIN90 C末端具有582-722位氨基酸，这对于F-肌动蛋白结合以及Arp2 / 3络合物介导的肌动蛋白聚合成支链肌动蛋白丝也是必不可少的。此外，删除F-肌动蛋白结合区（582-722 SPIN90）后，无法定位在膜边缘，并且无法促进片状脂蛋白的形成，这表明SPIN90 C端的F-肌动蛋白结合区是必需的。分支肌动蛋白网络的形成和细胞前缘肌动蛋白细胞骨架的调节。

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