Regulation of synaptic vesicle exocytosis by soluble proteins

为了理解可溶性蛋白质如Munc 18 -1、tomosyn 1和突触蛋白/复合蛋白调节突触囊泡胞吐的机制，我们产生了Munc 18 -1和tomosyn 1的海马CA 3特异性敲除（KO）小鼠。在CA 3区缺乏Munc 18 -1基因的小鼠出生后1周，神经元变性已经很明显，这使得突触传递的分析变得困难。Tomosyn 1 KO小鼠表现出较大的EPSP和较小的成对脉冲易化。突触蛋白C-末端区域与突触结合蛋白1的结合参与了来自PC 12 β 1的致密核心囊泡胞吐。

To understand the mechanisms by which soluble proteins such as Munc18-1, tomosyn 1 and synaphin/complexin regulate synaptic vesicle exocytosis, we generated hippocampal CA3-specific knockout(KO) mice of Munc18-1 and tomosyn 1. Neuronal degeneration was already apparent 1week after birth in mice lacking the Munc18-1 gene in the CA3 region, rendering the analysis of synaptic transmission difficult. Tomosyn 1 KO mice exhibited larger EPSPs and smaller paired pulse facilitations. The involvement of the binding of the synaphin C-terminal region with synaptotagmin 1 in dense-core vesicle exocytosis from PC12 cessl was suggested.