首页> 外文期刊>The Journal of Physiology >Activity-dependent control of bulk endocytosis by protein dephosphorylation in central nerve terminals.
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Activity-dependent control of bulk endocytosis by protein dephosphorylation in central nerve terminals.

机译:通过中枢神经末梢蛋白质去磷酸化的大量内吞作用的活动依赖控制。

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摘要

Bulk endocytosis is the process by which nerve terminals retrieve large amounts of synaptic vesicle membrane during periods of strong stimulation intensity. The process is rapidly activated and is most probably calcium dependent in a similar manner to synaptic vesicle exocytosis. This article briefly summarizes the current knowledge of bulk endocytosis with respect to its activation, kinetics and molecular mechanism. It also presents recent data from our laboratory showing that the dephosphorylation of a group of endocytosis proteins called the dephosphins by the Ca(2+)-dependent protein phosphatase calcineurin is key to the activity-dependent stimulation of the process. Possible downstream effectors of calcineurin are discussed such as the large GTPase dynamin I and its phosphorylation-dependent interaction partner syndapin I.
机译:大量的内吞作用是神经末梢在强烈刺激强度期间恢复大量突触小泡膜的过程。该过程被迅速激活,并且很可能以与突触囊泡胞吐相似的方式依赖钙。本文简要总结了有关批量内吞作用的激活,动力学和分子机制的最新知识。它还提供了来自我们实验室的最新数据,表明由Ca(2+)依赖性蛋白磷酸酶钙调磷酸酶对一组称为脱磷蛋白的内吞蛋白的去磷酸化是该过程的活性依赖性刺激的关键。讨论了钙调神经磷酸酶的可能的下游效应子,例如大的GTPase dynamin I及其依赖磷酸化的相互作用伴侣syndapinI。

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