在神经递质的分泌过程中，突触囊泡和质膜在一系列蛋白，磷脂分子及其复合物调控下完成膜融合过程。 Munc13/unc13家族蛋白作为含有多结构域和多功能性蛋白质，在膜融合过程中发挥重要作用。然而， Munc13/unc13调控膜融合过程的分子机制一直不清楚。在项目中，首先，我们将解析Munc13-1蛋白最小功能片段MUN分子结构，研究Munc13-1与上游蛋白质和下游磷脂分子的复合物晶体结构。其次，考察上游互作蛋白和下游磷脂分子与Munc13-1的相互作用关系，研究该相互作用与Munc13-1的分子结构和功能关系。最后，我们将以Munc13/unc13基因敲除的小鼠和线虫作为研究模型，结合体外膜融合实验，揭示Munc13-1和互作分子调控膜融合的分子机制。

In the process of neurotransmitter release, a series of proteins, phospholipids, and their complexes are reported to regulate synaptic vesicle fusion. As a protein having multi-domains and multi-functions, Munc13/unc13 plays a key role in membrane fusion. However, the mechanism of how Munc13/unc13 regulates membrane fusion is still unclear. In this project, we'll solve the crystal structure of MUN, which has the minimal activity of Munc13-1; and solve the crystal structures of Munc13-1/protein and Munc13-1/phospholipids complexes. Furthermore, we'll investigate the interaction relationships between Munc13-1 and its binding protein/phospholipids, study the interplay between the function and the structure dynamics of Munc13-1. Last, using Munc13/unc13 KO mice/c.elegans as the research model, combined with the in vitro fusion assay, we will study the function of Munc13-1 and its binding factors in membrane fusion.This work will shed a new light on the mechanism of Munc13/unc13 in neurotransmitter release.