自噬关键蛋白的翻译后修饰对自噬水平的快速调控至关重要，而SUMO化修饰在自噬中的调控作用及其靶分子还不清楚。ATG7为自噬过程的关键蛋白，其敲除后自噬不能发生，ATG7基因敲除小鼠出现新生儿代谢过渡障碍和死亡，故研究ATG7蛋白功能的调控对于理解自噬的发生有重要的意义。虽然ATG7的氧化修饰和乙酰化修饰已被报道，但这些修饰发挥功能的生理条件、具体分子机制还未可知，且并非自噬发生所必须的。我们的前期工作发现，ATG7可发生SUMO化修饰，且在饥饿诱导自噬时，其SUMO化修饰水平明显增强，同时发现其可能的SUMO修饰位点（K413位点）对其蛋白功能是必需的，对新生小鼠的早期存活至关重要。因此本项目旨在对ATG7的K413位点及其介导的SUMO化修饰对自噬调控的具体分子机制做深入探索，对理解自噬发生的分子机理及自噬调控有重要意义。

The post-translational modification of key autophagic proteins are critical for the rapid regulation of autophagy, but the regulatory role of SUMOylation in autophagy and its target molecules are unclear. ATG7 is a key protein in the autophagy process. Autophagy cannot occur after ATG7 gene knockout. ATG7 gene knockout mice have metabolic transitional disorders and death in the newborn. Therefore, studying the regulation of ATG7 protein function is important for understanding the occurrence of autophagy. Although oxidation and acetylation of ATG7 have been reported, the physiological conditions and specific molecular mechanisms are as yet unknown, and they are not necessary for autophagy. Our previous work found that ATG7 can undergo SUMO modification, which was significantly enhanced during starvation-induced autophagy, suggesting that the degree of ATG7 SUMOylation is related to the level of autophagy. We also found that K413 was the potential site of ATG7 SUMOylation, which was necessary for its protein function and the early survival of newborn mice. Therefore, this project aims to further explore the specific molecular mechanism in it, which has an important meaning for understanding the molecular mechanism and the regulation of autophagy.