FUSION COMPLEX-FORMATION PROTECTS SYNAPTOBREVIN AGAINST PROTEOLYSIS BY TETANUS TOXIN LIGHT-CHAIN
FUSION COMPLEX-FORMATION PROTECTS SYNAPTOBREVIN AGAINST PROTEOLYSIS BY TETANUS TOXIN LIGHT-CHAIN
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DOI：
10.1016/0014-5793(94)01070-6
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发表时间：
1994-10-24
期刊：
影响因子：
3.5
通讯作者：
BETZ, H
中科院分区：
文献类型：
--
作者：
PELLEGRINI, LL;OCONNOR, V;BETZ, H
梭菌神经毒素破伤风毒素是一种锌依赖性蛋白酶，通过选择性切割突触囊泡蛋白小突触泡蛋白来抑制神经递质胞吐作用。突触泡蛋白被认为是两种神经元质膜蛋白，突触融合蛋白和SNAP-25的受体，其在不可水解的ATP类似物的存在下与可溶性融合蛋白NSF和α-SNAP形成20 S融合复合物。在这里，我们表明，小突触泡蛋白，当在这个20 S复合物，或其7 S前体，是保护免受蛋白水解的酶活性破伤风毒素轻链。我们的数据定义了不同的突触泡蛋白池，这些池提供了囊泡/质膜相互作用不同步骤的标记物。
The clostridial neurotoxin, tetanus toxin, is a Zn2+-dependent protease which inhibits neurotransmitter exocytosis by selective cleavage of the synaptic vesicle protein, synaptobrevin. Synaptobrevin is thought to serve as a receptor for two neuronal plasma membrane proteins, syntaxin and SNAP-25, which in the presence of non-hydrolyzable ATP analogs form a 20 S fusion complex with the soluble fusion proteins NSF and alpha-SNAP. Here we show that synaptobrevin, when in this 20 S complex, or its 7 S precursor, is protected against proteolysis by the enzymatically active tetanus toxin light chain. Our data define distinct pools of synaptobrevin, which provide markers of different steps of vesicle/plasma membrane interaction.