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Vinculin activation by talin through helical bundle conversion

机译：talin通过螺旋束转换激活Vinculin

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摘要

Vinculin is a conserved component and an essential regulator of both cell―cell (cadnerin-mediated) and cell―matrix (integrity―talin-mediated focal adhesions) junctions, and it anchors these adhesion complexes to the actin cytoskeleton by binding to talin in integrin complexes or to α-actinin in cadherin junctions. In its resting state, vinculin is held in a closed conformation through interactions between its head (Vh) and tail (Vt) domains. The binding of vinculin to focal adhesions requires its association with talin. Here we report the crystal structures of human vinculin in its inactive and talin-activated states. Talin binding induces marked conformational changes in Vh, creating a novel helical bundle structure, and this alteration actively displaces Vt from Vh. These results, as well as the ability of α-actinin to also bind to Vh and displace Vt from pre-existing Vh-Vt complexes, support a model whereby Vh functions as a domain that undergoes marked structural changes that allow vinculin to direct cytoskeletal assembly in focal adhesions and adherens junctions. Notably, talin's effects on Vh structure establish helical bundle conversion as a signalling mechanism by which proteins direct cellular responses.
机译：Vinculin是细胞-细胞（钙粘蛋白介导的）和细胞-基质（完整性-塔林介导的粘着斑）连接的保守成分和重要调节剂，它通过与整联蛋白中的塔林结合而将这些粘附复合物锚定在肌动蛋白细胞骨架上。钙粘蛋白连接处的复合物或α-肌动蛋白。在其静止状态下，纽蛋白通过其头部（Vh）和尾部（Vt）域之间的相互作用而保持封闭状态。新霉素与粘着斑的结合需要与talin结合。在这里，我们报告了处于非活动状态和塔林激活状态的人长春花素的晶体结构。塔林结合在Vh中引起明显的构象变化，从而产生新的螺旋束结构，并且这种改变将Vt从Vh中置换出来。这些结果以及α-肌动蛋白也能结合Vh并从先前存在的Vh-Vt复合物中置换Vt的能力，支持了这样一种模型，其中Vh充当结构域，该结构域经历了明显的结构变化，从而使长春亭蛋白能够指导细胞骨架组装在粘连和粘连连接处。值得注意的是，塔林对Vh结构的影响将螺旋束转换确立为蛋白质指导细胞应答的信号传导机制。

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