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首页> 外文期刊>Cellular Signalling >Adaptor protein Nck1 interacts with p120 Ras GTPase-activating protein and regulates its activity
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Adaptor protein Nck1 interacts with p120 Ras GTPase-activating protein and regulates its activity

机译:衔接子蛋白Nck1与p120 Ras GTPase激活蛋白相互作用并调节其活性

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摘要

Adaptor protein Nck1 binds a number of intracellular proteins and influences various signaling pathways. Here we show that Nck1 directly binds and activates the GTPase-activating protein of Ras (RasGAP), which is responsible for the down-regulation of Ras. The first and the third SH3 domains of Nck1 and the NH_2-terminal proline-rich sequence of RasGAP contribute most to the complex formation causing direct molecular interaction between the two proteins. Cell adhesion to the substrate is obligatory for the Nck1 and RasGAP association, as cell detachment makes RasGAP incapable of associating with Nck1. This leads to the complex dissipation, decrease of RasGAP activity and the increase of H-Ras-GTP level in the detached cells. Our findings reveal unexpected feature of adaptor protein Nck1 as the regulator of RasGAP activity.
机译:衔接蛋白Nck1结合许多细胞内蛋白并影响各种信号通路。在这里,我们显示Nck1直接结合并激活Ras的GTPase激活蛋白(RasGAP),后者负责Ras的下调。 Nck1的第一个和第三个SH3结构域以及RasGAP的富含NH_2末端的脯氨酸序列对复合物的形成贡献最大,从而导致两种蛋白质之间的直接分子相互作用。 Nck1和RasGAP的结合必须与细胞粘附,因为细胞分离使RasGAP无法与Nck1结合。这导致分离细胞中的复杂耗散,RasGAP活性降低和H-Ras-GTP水平升高。我们的发现揭示了衔接蛋白Nck1作为RasGAP活性调节剂的出乎意料的特征。

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