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Cooperation between tropomyosin and α-actinin inhibits fimbrin association with actin filament networks in fission yeast

机译:原肌球蛋白和α-肌动蛋白之间的合作抑制裂殖酵母中纤维蛋白与肌动蛋白丝网络的缔合。

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摘要

We previously discovered that competition between fission yeast actin binding proteins (ABPs) for binding F-actin facilitates their sorting to different cellular networks. Specifically, competition between endocytic actin patch ABPs fimbrin Fim1 and cofilin Adf1 enhances their activities, and prevents tropomyosin Cdc8’s association with actin patches. However, these interactions do not explain how Fim1 is prevented from associating strongly with other F-actin networks such as the contractile ring. Here, we identified α-actinin Ain1, a contractile ring ABP, as another Fim1 competitor. Fim1 competes with Ain1 for association with F-actin, which is dependent upon their F-actin residence time. While Fim1 outcompetes both Ain1 and Cdc8 individually, Cdc8 enhances the F-actin bundling activity of Ain1, allowing Ain1 to generate F-actin bundles that Cdc8 can bind in the presence of Fim1. Therefore, the combination of contractile ring ABPs Ain1 and Cdc8 is capable of inhibiting Fim1’s association with F-actin networks.
机译:我们先前发现裂变酵母肌动蛋白结合蛋白(ABP)之间的结合F-肌动蛋白的竞争促进了它们对不同细胞网络的分类。具体而言,内吞肌动蛋白补丁ABP的纤维蛋白Fim1和cofilin Adf1之间的竞争增强了它们的活性,并阻止了原肌球蛋白Cdc8与肌动蛋白补丁的关联。但是,这些相互作用不能解释如何防止Fim1与其他F-肌动蛋白网络(如收缩环)牢固地关联。在这里,我们确定了收缩环ABPα-肌动蛋白Ain1是另一个Fim1竞争者。 Fim1与Ain1竞争与F-肌动蛋白的关联,这取决于它们的F-肌动蛋白停留时间。尽管Fim1分别胜过Ain1和Cdc8,但Cdc8增强了Ain1的F-肌动蛋白束缚活性,使Ain1可以生成Fdc1可以结合的F-肌动蛋白束。因此,收缩环ABP Ain1和Cdc8的结合能够抑制Fim1与F-肌动蛋白网络的联系。

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