SNARE complex oligomerization by synaphin/complexin is essential for synaptic vesicle exocytosis
SNARE complex oligomerization by synaphin/complexin is essential for synaptic vesicle exocytosis
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DOI：
10.1016/s0092-8674(01)00229-x
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发表时间：
2001-02-09
期刊：
影响因子：
64.5
通讯作者：
Abe, T
中科院分区：
文献类型：
--
作者：
Tokumaru, H;Umayahara, K;Abe, T
突触蛋白/复合蛋白是优先结合SNARE复合物内的突触融合蛋白的细胞溶质蛋白。我们发现突触蛋白促进SNARE形成预复合物，然后寡聚成更高级的结构。来自突触蛋白的突触融合蛋白结合域的中心肽竞争性抑制这两种蛋白质相互作用并防止SNARE复合物寡聚化。注射这种肽到鱿鱼巨大的突触前末梢抑制神经递质的释放在突触囊泡胞吐的后期预融合步骤。我们认为SNARE复合物的寡聚化形成了一个更高级的结构，为突触囊泡的有效、受调控的融合创造了一个SNARE支架。
Synaphin/complexin is a cytosolic protein that preferentially binds to syntaxin within the SNARE complex. We find that synaphin promotes SNAREs to form pre-complexes that oligomerize into higher order structures. A peptide from the central, syntaxin binding domain of synaphin competitively inhibits these two proteins from interacting and prevents SNARE complexes from oligomerizing. Injection of this peptide into squid giant presynaptic terminals inhibited neurotransmitter release at a late prefusion step of synaptic vesicle exocytosis. We propose that oligomerization of SNARE complexes into a higher order structure creates a SNARE scaffold for efficient, regulated fusion of synaptic vesicles.