Bhardwaj Piyush, Kulasiri Don, Samarasinghe Sandhya
Centre of Advanced Computational Solutions (C-fACS); Department of Molecular Biosciences, Lincoln University, Christchurch, New Zealand.
Centre of Advanced Computational Solutions (C-fACS), Lincoln University, Christchurch, New Zealand.
Neural Regen Res. 2021 Apr;16(4):700-706. doi: 10.4103/1673-5374.295332.
The axon initial segment (AIS) region is crucial for action potential initiation due to the presence of high-density AIS protein voltage-gated sodium channels (Na). Na channels comprise several serine residues responsible for the recruitment of Na channels into the structure of AIS through interactions with ankyrin-G (AnkG). In this study, a series of computational experiments are performed to understand the role of AIS proteins casein kinase 2 and AnkG on Na channel recruitment into the AIS. The computational simulation results using Virtual cell software indicate that Na channels with all serine sites available for phosphorylation bind to AnkG with strong affinity. At the low initial concentration of AnkG and casein kinase 2, the concentration of Na channels reduces significantly, suggesting the importance of casein kinase 2 and AnkG in the recruitment of Na channels.
轴突起始段（AIS）区域对于动作电位的起始至关重要，这是因为存在高密度的AIS蛋白电压门控钠通道（Na）。钠通道包含几个丝氨酸残基，这些残基通过与锚蛋白G（AnkG）相互作用负责将钠通道招募到AIS结构中。在本研究中，进行了一系列计算实验以了解AIS蛋白酪蛋白激酶2和AnkG在钠通道招募到AIS中的作用。使用虚拟细胞软件的计算模拟结果表明，所有丝氨酸位点都可用于磷酸化的钠通道与AnkG具有很强的亲和力。在AnkG和酪蛋白激酶2的初始浓度较低时，钠通道的浓度显著降低，这表明酪蛋白激酶2和AnkG在钠通道招募中的重要性。
