磷酸化开关对粘附体连接动力学的调节。

Journal of signal transduction Pub Date : 2012-01-01 Epub Date: 2012-07-12 DOI:10.1155/2012/125295
Cristina Bertocchi, Megha Vaman Rao, Ronen Zaidel-Bar
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引用次数: 56

摘要

粘附连接通过跨膜钙粘蛋白受体和连接蛋白网络连接相邻细胞的肌动蛋白细胞骨架。这些接头与钙粘蛋白之间的相互作用以及位于粘附连接处的肌动蛋白调节因子的活性受到严格控制,以促进细胞连接处的组装或拆卸,以响应外部或内部力和/或信号的变化。酪氨酸、丝氨酸或苏氨酸残基的磷酸化在大多数粘附连接蛋白上起着开关的作用,打开或关闭它们与其他蛋白质的相互作用和/或它们的酶活性。在这里,我们概述了调节粘附体连接蛋白磷酸化的激酶和磷酸酶,并列举了导致粘附体连接组装或拆卸的磷酸化事件的例子,强调了磷酸化开关在调节其动力学中的重要作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Regulation of adherens junction dynamics by phosphorylation switches.

Regulation of adherens junction dynamics by phosphorylation switches.

Adherens junctions connect the actin cytoskeleton of neighboring cells through transmembrane cadherin receptors and a network of adaptor proteins. The interactions between these adaptors and cadherin as well as the activity of actin regulators localized to adherens junctions are tightly controlled to facilitate cell junction assembly or disassembly in response to changes in external or internal forces and/or signaling. Phosphorylation of tyrosine, serine, or threonine residues acts as a switch on the majority of adherens junction proteins, turning "on" or "off" their interactions with other proteins and/or their enzymatic activity. Here, we provide an overview of the kinases and phosphatases regulating phosphorylation of adherens junction proteins and bring examples of phosphorylation events leading to the assembly or disassembly of adherens junctions, highlighting the important role of phosphorylation switches in regulating their dynamics.

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