犹素化修饰在内质网功能调控中的作用机制研究OA
Research on the mechanism of UFMylation in regulating endoplasmic reticulum function
内质网承担蛋白质合成运输与折叠、脂质与类固醇合成、碳水化合物代谢及钙储存等重要功能,受到多种质量控制机制的持续监测,包括内质网自噬(ER-phagy)、内质网相关降解(ER-associated degradation,ERAD)和未折叠蛋白反应(unfolded protein response,UPR)等.类泛素化修饰是一种典型的蛋白质翻译后修饰,对维持内质网稳态至关重要.泛素折叠修饰因子1(ubiquitin-fold modifier 1,UFM1)通过犹素化修饰(UFMylation)与细胞内蛋白共价偶联,类似于泛素化.犹素化修饰系统主要包括UFM1、UBA5、UFC1、UFL1和DDRGK1等.犹素化修饰对内质网应激、内质网相关降解、选择性自噬和内质网相关核糖体质量控制(ER-RQC)至关重要.
The endoplasmic reticulum(ER)is responsible for crucial functions such as protein synthesis,transport,folding,lipid and steroid synthesis,carbohydrate metabolism,and calcium storage.Its function is constantly monitored by multiple quality control mechanisms,including ER-phagy,ER-associated degradation(ERAD),and unfolded protein response(UPR).The ubiquitin-like modification is a typical form of post-translational modification essential for maintaining ER homeostasis.Ubiquitin-fold modifier 1(UFM1)covalently conjugates with intracellular proteins through UFMylation,analogous to ubiquitination.The UFMylation system primarily comprises UFM1,UBA5,UFC1,UFL1,and DDRGK1.UFMylation plays a critical role in ER stress,ERAD,selective autophagy,and endoplasmic reticulum-associated ribosome quality control(ER-RQC).
万飘飘;赵新;艾易;郑康
杭州师范大学生命与环境科学学院,浙江杭州杭州师范大学生命与环境科学学院,浙江杭州杭州师范大学生命与环境科学学院,浙江杭州杭州师范大学生命与环境科学学院,浙江杭州
生物科学
犹素化修饰内质网应激内质网自噬内质网相关核糖体质量控制
UFMylationendoplasmic reticulum stressER-phagyendoplasmic reticulum-associated ribosome quality control
《杭州师范大学学报（自然科学版）》 2026 (2)
120-127,144,9
国家自然科学基金项目(32371022)浙江省基础公益研究计划项目(LY22C090002)
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