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Control of nuclear organization by F-actin binding proteins

机译：F-肌动蛋白结合蛋白控制核组织

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The regulation of nuclear shape and deformability is a key factor in controlling diverse events from embryonic development to cancer cell metastasis, but the mechanisms governing this process are still unclear. Our recent study demonstrated an unexpected role for the F-actin bundling protein fascin in controlling nuclear plasticity through a direct interaction with Nesprin-2. Nesprin-2 is a component of the LINC complex that is known to couple the F-actin cytoskeleton to the nuclear envelope. We demonstrated that fascin, which is predominantly associated with peripheral F-actin rich filopodia, binds directly to Nesprin-2 at the nuclear envelope in a range of cell types. Depleting fascin or specifically blocking the fascin-Nesprin-2 complex leads to defects in nuclear polarization, movement and cell invasion. These studies reveal a novel role for an F-actin bundling protein in control of nuclear plasticity and underline the importance of defining nuclear-associated roles for F-actin binding proteins in future.
机译：核形状和可变形性的调节是控制从胚胎发育到癌细胞转移的各种事件的关键因素，但是控制该过程的机制仍不清楚。我们最近的研究表明F-肌动蛋白捆绑蛋白fascin通过与Nesprin-2的直接相互作用在控制核可塑性中具有出乎意料的作用。 Nesprin-2是LINC复合物的一个成分，已知该复合物会将F-肌动蛋白的细胞骨架与核膜结合。我们证明，主要与外围F-肌动蛋白丰富的丝状伪足相关的fascin，在多种细胞类型的核膜上直接与Nesprin-2结合。耗尽fascin或特异性阻断fascin-Nesprin-2复合物会导致核极化，运动和细胞侵袭的缺陷。这些研究揭示了F-肌动蛋白束缚蛋白在控制核可塑性中的新作用，并强调了在未来定义F-肌动蛋白结合蛋白的核相关作​​用的重要性。

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