PHOSPHORYLATION OF SYNAPSIN-I AND MARCKS IN NERVE-TERMINALS IS MEDIATED BY CA2+ ENTRY VIA AN AGA-GI SENSITIVE CA2+ CHANNEL WHICH IS COUPLED TO GLUTAMATE EXOCYTOSIS
PHOSPHORYLATION OF SYNAPSIN-I AND MARCKS IN NERVE-TERMINALS IS MEDIATED BY CA2+ ENTRY VIA AN AGA-GI SENSITIVE CA2+ CHANNEL WHICH IS COUPLED TO GLUTAMATE EXOCYTOSIS
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DOI：
10.1016/0014-5793(94)01061-7
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发表时间：
1994-10-24
期刊：
影响因子：
3.5
通讯作者：
POCOCK, JM
中科院分区：
文献类型：
--
作者：
COFFEY, ET;SIHRA, TS;POCOCK, JM
在哺乳动物皮层突触体中，Ca 2+进入是突触蛋白I和MARCKS蛋白的胞吐和磷酸化的先决条件。新型蜘蛛毒素Aga-GI完全阻断KCl诱发的谷氨酸胞吐，但仅部分抑制KCl诱发的细胞质Ca 2+升高，从而揭示了KCl诱导的Ca 2+进入的至少两种途径。Aga-GI完全减弱KCl诱导的突触蛋白I和MARCKS蛋白磷酸化。因此，我们得出结论，突触蛋白I和MARCKS蛋白的胞吐作用和磷酸化都通过对Aga-GI敏感的神经末梢处的电压依赖性Ca 2+通道的子集特异性地耦合到Ca 2+进入。
Ca2+ entry is a prerequisite for both exocytosis and the phosphorylation of synapsin I and MARCKS proteins in mammalian cerebrocortical synaptosomes. The novel spider toxin Aga-GI completely blocks KCl-evoked glutamate exocytosis but only partially inhibits KCl-evoked cytoplasmic Ca2+ elevations, thus revealing at least two pathways for KCl-induced Ca2+ entry. Aga-GI completely attenuates KCl-induced phosphorylation of synapsin I and MARCKS proteins. We therefore conclude that both exocytosis and the phosphorylation of synapsin I and MARCKS proteins are specifically coupled to Ca2+ entry via a subset of voltage dependent Ca2+ channels at the nerve terminal which are sensitive to Aga-GI.