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

被引:29
作者
COFFEY, ET [1 ]
SIHRA, TS [1 ]
NICHOLLS, DG [1 ]
POCOCK, JM [1 ]
机构
[1] UNIV DUNDEE,INST MED SCI,DEPT BIOCHEM,DUNDEE DD1 4HN,SCOTLAND
基金
英国惠康基金;
关键词
GLUTAMATE EXOCYTOSIS; NERVE TERMINAL; PHOSPHORYLATION; CALCIUM CHANNEL;
D O I
10.1016/0014-5793(94)01061-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:264 / 268
页数:5
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