SYNTAXIN AND SYNAPTOBREVIN FUNCTION DOWNSTREAM OF VESICLE DOCKING IN DROSOPHILA
SYNTAXIN AND SYNAPTOBREVIN FUNCTION DOWNSTREAM OF VESICLE DOCKING IN DROSOPHILA
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DOI：
10.1016/0896-6273(95)90154-x
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发表时间：
1995-09-01
期刊：
影响因子：
16.2
通讯作者：
SWEENEY, ST
中科院分区：
文献类型：
--
作者：
BROADIE, K;PROKOP, A;SWEENEY, ST
在突触传递中，小泡通过突触短蛋白 (V-SNARE) 与突触蛋白 (t-SNARE) 的结合而停靠在突触前活动区。我们在缺乏神经突触短蛋白（n-synaptobrevin）或突触蛋白的果蝇品系中测试了这一假设。我们之前表明，任何一种蛋白质的丢失都会完全阻断突触传递。在这里，我们尝试确定这种阻断的水平。从超微结构上看，囊泡仍然以突触前膜为目标，并正常停靠在专门的释放位点。这些囊泡是成熟且有功能的，因为自发囊泡融合在不存在 n-突触短蛋白的情况下持续存在，并且囊泡融合是在不存在突触蛋白的情况下由高渗盐水触发的。我们得出的结论是，SNARE 假说不能完全解释这些囊泡的作用 相反，这两种蛋白质在对接下游发挥着不同的作用。
In synaptic transmission, vesicles are proposed to dock at presynaptic active zones by the association of synaptobrevin (V-SNARE) with syntaxin (t-SNARE). We test this hypothesis in Drosophila strains lacking neural synaptobrevin (n-synaptobrevin) or syntaxin, We showed previously that loss of either protein completely blocks synaptic transmission, Here, we attempt to establish the level of this blockade. Ultrastructurally, vesicles are still targeted to the presynaptic membrane and dock normally at specialized release sites, These vesicles are mature and functional since spontaneous vesicle fusion persists in the absence of n-synaptobrevin and since vesicle fusion is triggered by hyperosmotic saline in the absence of syntaxin, We conclude that the SNARE hypothesis cannot fully explain the role of these proteins in synaptic transmission, Instead, both proteins play distinct roles downstream of docking.