神经递质释放过程中的可溶性NSF附着蛋白受体(SNARE)和相关蛋白

近年来，对突触小泡释放神经递质分子机制的研究迅速发展，发现了大量位于神经末梢的蛋白质.它们之间的相互作用与突触小泡释放神经递质相关，特别是位于突触小泡膜上的突触小泡蛋白/突触小泡相关膜蛋白(synaptobrevin/VAMP),位于突触前膜上的syntaxin和突触小体相关蛋白(synaptosome-associated protein of 25 ku)，三者聚合形成的可溶性NSF附着蛋白受体(SNARE)核心复合体在突触小泡的胞裂外排、释放递质过程中有重要作用.而一些已知及未知的与SNARE蛋白有相互作用的蛋白质,可通过调节SNARE核心复合体的形成与解离来影响突触小泡的胞裂外排，从而可以调节突触信号传递的效率及强度，在突触可塑性的形成中起重要作用.

SNARE and Interacting Proteins Involved in Neurotransmitter Release

Synaptic vesicle docking and fusion at release sites require the association of proteins on both vesicle and plasma membranes. Syntaxin interacts with synaptobrevin/VAMP and SNAP-25, constituting the SNARE core complex. This complex's formation comprises the minimal molecular requirement for membrane fusion in vitro. However, the Ca²⁺-triggered synaptic vesicle fusion with presynaptic plasma membrane can be regulated rapidly and tightly when the main SNARE intermediate is so stable. Some synaptic proteins, which regulate the accessibility of SNARE components by interacting with the individual SNARE proteins, might tightly control assembly of functional fusion machinery. Thus, the identification of regulators or molecular switches involved in the assembly of the fusion core complexes is critical for elucidating the molecular mechanisms underlying neurotransmitter release and synaptic plasticity.