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首页> 外文期刊>American Journal of Physiology >Rac is a dominant regulator of cadherin-directed actin assembly that is activated by adhesive ligation independently of Tiam1.
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Rac is a dominant regulator of cadherin-directed actin assembly that is activated by adhesive ligation independently of Tiam1.

机译：Rac是钙粘蛋白定向肌动蛋白装配的主要调节剂，其通过粘合剂连接独立于Tiam1激活。

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摘要

Classic cadherins function as adhesion-activated cell signaling receptors. On adhesive ligation, cadherins induce signaling cascades leading to actin cytoskeletal reorganization that is imperative for cadherin function. In particular, cadherin ligation activates actin assembly by the actin-related protein (Arp)2/3 complex, a process that critically affects the ability of cells to form and extend cadherin-based contacts. However, the signaling pathway(s) that activate Arp2/3 downstream of cadherin adhesion remain poorly understood. In this report we focused on the Rho family GTPases Rac and Cdc42, which can signal to Arp2/3. We found that homophilic engagement of E-cadherin simultaneously activates both Rac1 and Cdc42. However, by comparing the impact of dominant-negative Rac1 and Cdc42 mutants, we show that Rac1 is the dominant regulator of cadherin-directed actin assembly and homophilic contact formation. To pursue upstream elements of the Rac1 signaling pathway, we focused on the potential contribution of Tiam1 to cadherin-activated Rac signaling. We found that Tiam1 or the closely-related Tiam2/STEF1 was recruited to cell-cell contacts in an E-cadherin-dependent fashion. Moreover, a dominant-negative Tiam1 mutant perturbed cell spreading on cadherin-coated substrata. However, disruption of Tiam1 activity with dominant-negative mutants or RNA interference did not affect the ability of E-cadherin ligation to activate Rac1. We conclude that Rac1 critically influences cadherin-directed actin assembly as part of a signaling pathway independent of Tiam1.
机译：经典的钙粘蛋白可作为粘附激活的细胞信号转导受体。在粘附性连接上，钙粘着蛋白诱导信号传导级联，导致肌动蛋白细胞骨架重组，这对于钙粘着蛋白功能必不可少。特别是，钙粘着蛋白的连接通过肌动蛋白相关蛋白（Arp）2/3复合物激活肌动蛋白组装，这一过程严重影响细胞形成和扩展基于钙粘着蛋白的接触的能力。然而，激活钙粘蛋白粘附下游的Arp2 / 3的信号传导途径仍然知之甚少。在本报告中，我们重点介绍Rho系列GTPases Rac和Cdc42，它们可以向Arp2 / 3发出信号。我们发现E-钙粘着蛋白的同质参与同时激活Rac1和Cdc42。但是，通过比较显性负性Rac1和Cdc42突变体的影响，我们显示Rac1是钙粘蛋白定向肌动蛋白装配和同型接触形成的显性调节剂。为了追求Rac1信号通路的上游元素，我们专注于Tiam1对钙粘蛋白激活的Rac信号的潜在贡献。我们发现，Tiam1或紧密相关的Tiam2 / STEF1以E-钙粘着蛋白依赖性的方式募集到细胞间接触。此外，显性阴性Tiam1突变体扰动了细胞在钙粘蛋白涂层基质上的扩散。但是，用显性阴性突变体破坏Tiam1活性或RNA干扰并不影响E-钙粘蛋白连接激活Rac1的能力。我们得出结论，Rac1作为独立于Tiam1的信号传导途径的一部分，严重影响钙粘蛋白定向的肌动蛋白组装。

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