Myosin II activity is required for structural plasticity at the axon initial segment.

Myosin II activity is required for structural plasticity at the axon initial segment.
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肌动蛋白II活性是轴突初始段处的结构可塑性所必需的。

DOI:
10.1111/ejn.13597
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发表时间:
2017-07
期刊:
The European journal of neuroscience
影响因子:
--
通讯作者:
Grubb MS
Grubb MS
中科院分区:
其他
文献类型:
--
作者:
Evans MD;Tufo C;Dumitrescu AS;Grubb MS

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在神经元中,轴突具有一个分子定义和高度组织的近端区域——轴突初始段(AIS),这是电兴奋性和细胞极性的关键调节器。尽管AIS是一个具有特殊细胞骨架结构的大而致密的结构,但它具有惊人的可塑性,神经元活动的持续改变会导致其位置、长度或分子组成的显著改变。然而,尽管导致这种可塑性的上游依赖于活性的信号通路已经开始被阐明,但在AIS产生结构变化的下游机制是完全未知的。在这里,我们使用大鼠海马的解离培养来证明齿状颗粒细胞的两种AIS可塑性——长期的重新定位和更快速的缩短——被blebbistatin(一种有效的选择性肌球蛋白II atp酶抑制剂)完全阻断。这些数据建立了肌球蛋白II和AIS功能之间的联系,并表明肌球蛋白II在结构上的主要作用可能是影响活性依赖性形态改变。
In neurons, axons possess a molecularly defined and highly organised proximal region – the axon initial segment (AIS) – that is a key regulator of both electrical excitability and cellular polarity. Despite existing as a large, dense structure with specialised cytoskeletal architecture, the AIS is surprisingly plastic, with sustained alterations in neuronal activity bringing about significant alterations to its position, length or molecular composition. However, although the upstream activity‐dependent signalling pathways that lead to such plasticity have begun to be elucidated, the downstream mechanisms that produce structural changes at the AIS are completely unknown. Here, we use dissociated cultures of rat hippocampus to show that two forms of AIS plasticity in dentate granule cells – long‐term relocation, and more rapid shortening – are completely blocked by treatment with blebbistatin, a potent and selective myosin II ATPase inhibitor. These data establish a link between myosin II and AIS function, and suggest that myosin II's primary role at the structure may be to effect activity‐dependent morphological alterations.
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