Aurora A kinase negatively regulates Rho-kinase by phosphorylation in vivo
Aurora A kinase negatively regulates Rho-kinase by phosphorylation in vivo
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DOI：
10.1016/j.bbrc.2013.05.028
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发表时间：
2013-06-14
影响因子：
3.1
通讯作者：
Matsuzaki, Fumio
中科院分区：
文献类型：
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作者：
Moon, Woongjoon;Matsuzaki, Fumio
Aurora-A激酶（AurA）是涉及微管的细胞过程的关键调节剂。它也被牵连在肌动蛋白依赖性事件，但该过程的机制尚未完全理解。在这里，我们提供的遗传和生化证据表明，AurA负调控果蝇，唯一已知的Rho激酶的直系同源果蝇。AurA在体外直接磷酸化Drok，并且Drok的非磷酸化形式在体内的过表达引起类似的但比野生型Drok强得多的作用。由Drok的非磷酸化形式诱导的缺陷通过降低下游肌球蛋白的功能来补偿。因此，Drok被AurA磷酸化通常抑制Drok活性。我们认为AurA通过磷酸化Rho激酶直接调节肌动蛋白依赖的过程。(C)2013作者爱思唯尔公司出版All rights reserved.
Aurora-A kinase (AurA) is a key regulator of cellular processes involving microtubules. It has also been implicated in actin-dependent events, but the mechanisms that underlie the processes are not fully understood. Here we provide genetic and biochemical evidence suggesting that AurA negatively regulates Drok, the only known Rho-kinase orthologue in Drosophila. AurA directly phosphorylates Drok in vitro, and the overexpression of the nonphosphorylatable forms of Drok in vivo causes similar, but much stronger effects than that of wild-type Drok. The defects induced by the nonphosphorylatable forms of Drok are compensated by reducing the function of myosin downstream. Thus, phosphorylation of Drok by AurA normally suppresses Drok activity. We propose that AurA directly regulates actin-dependent processes by phosphorylating Rho-kinase. (C) 2013 The Authors. Published by Elsevier Inc. All rights reserved.