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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >SEC14-like protein 1 interacts with cholinergic transporters.
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SEC14-like protein 1 interacts with cholinergic transporters.

机译：SEC14样蛋白1与胆碱能转运蛋白相互作用。

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摘要

Trafficking of the vesicular acetylcholine transporter (VAChT) to synaptic vesicles has the potential to regulate storage and release of acetylcholine. We used the C-terminal tail of the vesicular acetylcholine transporter as bait for the screening of a brain cDNA library by yeast-two hybrids. Here we report an interaction uncovered in this screening with SEC14L1, a mammalian SEC14-like protein that may function as a phospholipid transfer protein. The interaction of VAChT and SEC14L1 occurred through the GOLD domain found in the latter and was confirmed in mammalian cells. In addition, we also found that SEC14L1 co-immunoprecipitates with the high affinity choline transporter (CHT1), but not with synaptophysin or synaptotagmin. In cultured cells SEC14L1 was predominantly found in the cytosol with little or no localization in defined organelles. In contrast, overexpression of VAChT or CHT1 with SEC14L1 recruited the latter to large intracellular organelles similar to vesicles or vesicle aggregates. Finally, we find that overexpression of SEC14L1 modestly decreases high affinity choline transport activity. We suggest that interaction of cholinergic transporters with proteins containing the GOLD domain may be relevant for transporter function.
机译：将水泡乙酰胆碱转运蛋白（VAChT）转运到突触小泡具有调节乙酰胆碱的储存和释放的潜力。我们使用水泡乙酰胆碱转运蛋白的C末端尾巴作为诱饵，通过酵母-两个杂种筛选脑cDNA文库。在这里，我们报道了在与SEC14L1的筛选中发现的相互作用，SEC14L1是一种哺乳动物的SEC14样蛋白，可能起磷脂转移蛋白的作用。 VAChT和SEC14L1的相互作用是通过在后者中发现的GOLD域发生的，并已在哺乳动物细胞中得到证实。此外，我们还发现SEC14L1与高亲和力胆碱转运蛋白（CHT1）共同免疫沉淀，但不与突触素或突触结合素共同免疫沉淀。在培养的细胞中，主要在细胞质中发现SEC14L1，在限定的细胞器中几乎没有或没有定位。相比之下，VAChT或CHT1与SEC14L1的过表达将后者召集到类似于囊泡或囊泡聚集体的大细胞内细胞器中。最后，我们发现SEC14L1的过表达适度降低了高亲和力胆碱转运活性。我们建议胆碱能转运蛋白与包含GOLD域的蛋白质的相互作用可能与转运蛋白功能有关。

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