Calcium-dependent interaction of N-type calcium channels with the synaptic core complex

被引:304
作者
Sheng, ZH [1 ]
Rettig, J [1 ]
Cook, T [1 ]
Catterall, WA [1 ]
机构
[1] UNIV WASHINGTON, DEPT PHARMACOL, SEATTLE, WA 98195 USA
关键词
D O I
10.1038/379451a0
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
NEUROTRANSMITTER release is initiated by influx of Ca2+ through voltage-gated Ca2+ channels(1,2), within 200 mu s of the action potential arriving at the synaptic terminal(3), as the Ca2+ concentration increases from 100 nM to >200 mu M(4). Exocytosis requires high Ca2+ concentration, with a threshold of 20-50 mu M and half-maximal activation at 190 mu M(5,6). The synaptic membrane syntaxin(7,8), 25K synaptosome-associated protein (SNAP25)9, and vesicle-associated membrane protein (VAMP)/synaptobrevin(10-12), are thought to form a synaptic core complex which mediates vesicle docking and membrane fusion(13-19) Synaptotagmin may be the low-affinity Ca2+-sensor(20-24), but other Ca2+-sensors are involved(25-27) as residual neurotransmission persists in synaptotagmin-null mutants. Syntaxin binds to N-type Ca2+ channels(7,8,28,29) at a site in the intracellular loop connecting domains II and III30. Here we describe Ca2+ dependent interaction of this site with syntaxin and SNAP25 which has a biphasic dependence on Ca2+, with maximal binding at 20 mu M free Ca2+, near the threshold for transmitter release. Ca2+-dependent interaction of Ca2+ channels with the synaptic core complex may be important for Ca2+-dependent docking and fusion of synaptic vesicles.
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页码:451 / 454
页数:4
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