细胞自噬在动物的生长发育中具有重要作用，细胞自噬的发生不仅受上游信号调控，也受自噬蛋白翻译后修饰的影响，它直接决定自噬蛋白复合体的功能，进而影响自噬的发生。申请者前期的研究发现：与果蝇和哺乳动物不尽相同，家蚕在细胞自噬时自噬起始蛋白复合体成员ATG1/ATG13分别发生磷酸化和去磷酸化修饰，参与自噬小体装配的ATG8–PE泛素样蛋白系统成员ATG3/ATG8的核定位平行减少，暗示发生去乙酰化修饰。为解析家蚕这两个自噬蛋白复合体翻译后修饰的分子作用，本项目将利用免疫沉淀技术结合磷酸化/乙酰化等蛋白组学分析，鉴定家蚕ATG1的磷酸化、ATG3和ATG8的乙酰化修饰位点和它们的结合蛋白，旨在揭示其翻译后修饰的分子机理和在自噬发生中的作用。本项目研究对阐明鳞翅目昆虫细胞自噬发生机制和认知其它动物细胞自噬具有重要的理论意义，也可为鳞翅目益虫利用和害虫防治提供候选分子靶标。

Autophagy is essential for the growth and development of animals. The occurrence of autophagy is not only regulated by upstream signals, but also influenced by the posttranslational modification of autophagy related (ATG) proteins, which determines the physiological function of ATG proteins and further the occurrence of autophagy. Our previous studies revealed that autophagy-initiation protein ATG1 was phosphorylated while ATG13 was dephosphorylated during autophagy in Bombyx, which is not all the same with their homologous proteins in Drosophila and mammals. Bombyx ATG3 and ATG8, the key components involved in the ATG8–PE ubiquitin-like protein system, were found to localize in the cell nucleus without autophagy, but decreased parallel when autophagy occurred, indicating the acetylation of them. On the basis of these findings, we will use the immunoprecipitation associated with the analysis by phosphoproteomics/ acetylation proteomics and other proteomics to identify the phosphorylation sites of ATG1, the acetylation sites of ATG3/ATG8 as well as the potential autophagy related proteins binding to this three proteins. This project is aimed to illustrate the mechanism and molecular function of the posttranslational modification of ATG1 and ATG3/ATG8 in Bombyx, which is of great significance for autophagy studying in lepidopteran insects and other species. This project also will provide the potential molecular targets for beneficial insects and pest control.