Department of Molecular and Cellular Physiology, Department of Neurology and Neurological Sciences, Department of Structural Biology, Department of Photon Science, Howard Hughes Medical Institute, Stanford University, Stanford, California 94305, USA; email:
Annu Rev Biophys. 2018 May 20;47:469-497. doi: 10.1146/annurev-biophys-070816-034117.
This review summarizes current knowledge of synaptic proteins that are central to synaptic vesicle fusion in presynaptic active zones, including SNAREs (soluble N-ethylmaleimide sensitive factor attachment protein receptors), synaptotagmin, complexin, Munc18 (mammalian uncoordinated-18), and Munc13 (mammalian uncoordinated-13), and highlights recent insights in the cooperation of these proteins for neurotransmitter release. Structural and functional studies of the synaptic fusion machinery suggest new molecular models of synaptic vesicle priming and Ca-triggered fusion. These studies will be a stepping-stone toward answering the question of how the synaptic vesicle fusion machinery achieves such high speed and sensitivity.
本文综述了目前关于突触蛋白的认识，这些蛋白在突触前活性区的突触小泡融合中起核心作用，包括 SNAREs（可溶性 NSF 附着蛋白受体）、突触融合蛋白、突触结合蛋白、Munc18（哺乳动物无协调蛋白-18）和 Munc13（哺乳动物无协调蛋白-13），并强调了这些蛋白在神经递质释放中合作的最新见解。对突触融合机制的结构和功能研究提出了突触小泡引发和 Ca2+触发融合的新的分子模型。这些研究将是回答突触小泡融合机制如何实现如此高速和高灵敏度这一问题的踏脚石。
