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首页> 外文期刊>The European Journal of Neuroscience >Regulated recycling and plasma membrane recruitment of the high-affinity choline transporter.
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Regulated recycling and plasma membrane recruitment of the high-affinity choline transporter.

机译：调节高亲和力胆碱转运蛋白的回收利用和质膜募集。

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摘要

The high-affinity choline transporter (CHT1) is responsible for uptake of choline from the synaptic cleft and supplying choline for acetylcholine synthesis. CHT1 internalization by clathrin-coated vesicles is proposed to represent a mechanism by which high-affinity choline uptake can be modulated. We show here that internalized CHT1 is rapidly recycled back to the cell surface in both human embryonic kidney cells (HEK 293 cells) and SH-SY5Y neuroblastoma cells. This rapidly recycling pool of CHT1 comprises about 10% of total CHT1 protein. In the SH-SY5Y neuroblastoma cell line K(+)-depolarization promotes Ca(2+)-dependent increase in the rate of CHT1 recycling to the plasma membrane without affecting the rate of CHT1 internalization. K(+)-depolarization also increases the size of the pool of CHT1 protein that can be mobilized to the plasma membrane. Thus, the activity-dependent increase in plasma membrane CHT1 localization appears to be regulated by two mechanisms: (i) an increase in the rate of externalization of the intracellular CHT1 pool; and (ii) the recruitment of additional intracellular transporters to the recycling pool.
机译：高亲和力胆碱转运蛋白（CHT1）负责从突触裂隙摄取胆碱，并提供胆碱用于乙酰胆碱合成。提出网格蛋白包被的囊泡CHT1内化代表一种机制，通过该机制可以调节高亲和力的胆碱摄取。我们在这里显示内部化的CHT1迅速循环回到人类胚胎肾细胞（HEK 293细胞）和SH-SY5Y神经母细胞瘤细胞的细胞表面。 CHT1的这种快速回收池约占CHT1总蛋白的10％。在SH-SY5Y神经母细胞瘤细胞系K（+）-去极化促进CHT1循环到质膜的速率依赖Ca（2+）的增加，而不影响CHT1内在化的速率。 K（+）去极化还增加了可动员至质膜的CHT1蛋白池的大小。因此，依赖于活性的质膜CHT1定位增加似乎受到两种机制的调节：（i）细胞内CHT1库外部化速率的增加; （ii）向回收池募集额外的细胞内转运蛋白。

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