The Membrane Interaction of Alpha-Synuclein.
The Membrane Interaction of Alpha-Synuclein.
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α-突触核蛋白的膜相互作用
DOI：
10.3389/fncel.2021.633727
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发表时间：
2021
影响因子：
5.3
通讯作者：
Dong W
中科院分区：
文献类型：
--
作者：
Liu C;Zhao Y;Xi H;Jiang J;Yu Y;Dong W
α-突触核蛋白（α-Synuclein，α-Syn）是一种与帕金森病（Parkinson's disease，PD）密切相关的突触前蛋白，其致病机制已被广泛研究。然而，α-Syn作为突触前的一种生理蛋白，其生理功能尚不清楚。其在神经末梢中的位置和对膜融合的影响也暗示其在突触传递中的功能作用，包括其通过其N-末端和无定形C-末端与高曲率膜的可能相互作用。破坏膜相互作用的PD相关突变体（例如，A30 P和G51 D）的研究还表明α-Syn的致病机制与生理作用之间通过膜结合的关系。在这里，我们总结了最近关于α-Syn及其变体如何与膜相互作用并影响突触传递的研究。我们列出了蛋白质的生理功能和病理机制之间的几种膜相关联系，这些联系有助于扩大目前对α-Syn的理解。
A presynaptic protein closely related to Parkinson's disease (PD), α-synuclein (α-Syn), has been studied extensively regarding its pathogenic mechanisms. As a physiological protein in presynapses, however, α-Syn's physiological function remains unclear. Its location in nerve terminals and effects on membrane fusion also imply its functional role in synaptic transmission, including its possible interaction with high-curvature membranes via its N-terminus and amorphous C-terminus. PD-related mutants that disrupt the membrane interaction (e.g., A30P and G51D) additionally suggest a relationship between α-Syn's pathogenic mechanisms and physiological roles through the membrane binding. Here, we summarize recent research on how α-Syn and its variants interact with membranes and influence synaptic transmission. We list several membrane-related connections between the protein's physiological function and the pathological mechanisms that stand to expand current understandings of α-Syn.
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