Mios在调节LIM Kinase对cofilin磷酸化中的 作用

肌动蛋白作为一种球状蛋白质，基本存在于所有真核细胞中，并且可以通过
聚合形成丝状肌动蛋白（Actin Fliament， F-actin），是细胞骨架及肌肉收缩装置的
基本组成成分。在动物细胞中许多必须的生理过程都需要肌动蛋白的动态变化，
如细胞迁移，细胞分裂以及细胞的内吞作用等等。 过去的数十年中， F-actin 的动
力学一直是研究的热点，该领域至今仍然充满了争议以及未知。在这篇论文中，
我们发现了一个新的肌动蛋白调节因子 Mios，遗传研究表明， Mios 的敲除会导致
F-actin 的升高，说明 Mios 可能会影响肌动蛋白动力学。 本文的中心是利用生物化
学手段，研究 Mios 通过影响 LIM 激酶（LIM Kinase， LIMK） 对 cofilin 磷酸化这
一过程进而调控肌动蛋白动力学变化。
肌动蛋白解聚因子（cofilin） 通过对加速肌动蛋白的解聚进而影响肌动蛋白的
动态调节， LIMK 可通过磷酸化 cofilin 进而抑制 cofilin 的活性，但影响磷酸化调
节水平的机制尚未明确。 基于肖老师在四川大学的课题组的发现， 在外周神经系
统中特异性敲除 Mios 会导致 F-actin 增加，磷酸化 cofilin 水平升高的现象，这表
明 Mios 的敲除影响了 cofilin 的磷酸化水平，进而影响了肌动蛋白动力学，但具体
机制尚未清楚。
Mios 蛋白作为 GATOR2 复合体的一个亚基，在 N 端含有一个 WD40 Repeat
Domain（WDR Domain）和一个在 C 端的锌带状结构域（Zinc Ribbon Domain）。
以往对于 Mios 的研究主要聚焦于 Mios 依赖 GATOR2 复合体对 mTORC1 信号通路
的调控以及 Mios 在细胞核内调控核基因的功能。本研究中，通过 GST pull-down、
激酶-底物反应以及肌动蛋白解聚试验， 发现了 Mios 在调控肌动蛋白的动态变化中
具有双重作用， 一方面可以抑制 LIMK 对 cofilin 的磷酸化，另一方面与 cofilin 结
合降低了 cofilin 解聚肌动蛋白的活性，并且 Mios 发挥这一功能既不依赖于 WDR
结构域，也不依赖于锌带状结构域，而是依赖于 Mios 中间的一段未知结构域。
Mios 蛋白这种新功能的发现为肌动蛋白动力学调节提供了新的分子模型，对了解
肌动蛋白动力学具有重要意义。
 

Actin, as a globular protein, exists in almost all eukaryotic cells. Actin Fliation
(F-actin) is a basic component of the cytoskeleton and muscle contraction apparatus.
Many essential physiological processes in animal cells require actin dynamics, such as
cell migration, cell division and endocytosis. In the past decades, the dynamics of
F-actin has been the focus of research, which is still full of controversy and unknown. In
this paper, we found a new actin regulatory factor, Mios. Genetic studies show that the
knockout of Mios leads to an increase in F-actin, suggesting that Mios may affect actin
dynamics. This paper is focus on study the effect of Mios on the phosphorylation of
cofilin by LIM Kinase (LIMK) and actin dynamics by biochemical methods.
Actin dynamics plays an important role in myelination. Actin depolymerization
factor (cofilin) affects actin dynamic by accerlating the speed of actin depolymerization.
LIMK can inhibit the activity of cofilin by phosphorylating cofilin, but the mechanism
under LIMK affects the phosphorylation level of cofilin is still unknown. Based on
previous findings from Prof. Xiao’s Lab in Sichuan University, conditional knockout of
Mios in peripheral nervous system leads to an increase in F-actin and phosphorylated
cofilin levels, which indicates that the knockout of Mios affects the phosphorylation
level of cofilin and actin dynamics, but the specific mechanism is not yet clear.
As a component of GATOR2 complex, Mios protein contains a WD40 Repeat
Domain (WDR Domain) at N-terminal and a Zinc Ribbon Domainat at C-terminal.
Previous studies on Mios have focused on the regulation of mTORC1 signaling pathway
by GATOR2 complex and the function of regulating nuclear genes. In this study, GST
pull-down, kinase-substrate reaction and actin depolymerization experiments were used
to provide Mios with a new key function: regulating actin dynamic and myelination.
Results showed that Mios has dual roles in regulating actin dynamics: on the one hand,
it can inhibit the phosphorylation of cofilin by LIMK, on the other hand, it’s binding
with cofilin decreases the activity of cofilin depolymerization actin. The more important
is, this function depend neither on the WDR domain nor the Zinc Ribbon Domain, but
depend on an unknown domain in the middle of Mios. The discovery of the new
function of Mios provides a new molecular model for the regulation of actin dynamics,
which is of great significance for understanding acin dynamics.
 

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