《生命科学》 2014, 26(8): 852-857

O-GlcNAc修饰对蛋白质泛素化降解途径的影响

周　丰1，刘晓燕2，王玉秋2，张连文2*

(1 天津大学药物科学与技术学院，天津 300072；2 南开大学药学院，天津 300071)

摘　要：摘　要：O-GlcNAc 修饰是一种特殊的糖基化修饰，几乎参与生物体内所有细胞过程的调控。该修饰与泛素化作为两种重要的蛋白质翻译后修饰形式，都与2 型糖尿病、神经退行性疾病、癌症等疾病密切相关。O-GlcNAc 修饰对蛋白质泛素化降解途径的影响主要体现在4 个方面：(1) O-GlcNAc 修饰能够抑制26S 蛋白酶体的ATPase 活性；(2) O-GlcNAc 修饰会减少某些底物蛋白的泛素化降解；(3) O-GlcNAc 修饰泛素化相关酶并调节其功能；(4) 某些蛋白质( 包括调控因子) 发生O-GlcNAc 修饰后间接影响蛋白质泛素化。

O-GlcNAcylation influences ubiquitin proteasome degradation of protein

ZHOU Feng1， LIU Xiao-Yan2， WANG Yu-Qiu2， ZHANG Lian-Wen2*

(1 School of Pharmaceutical Science and Technology， Tianjin Universtiy， Tianjin 300072， China;2 College of Pharmacy， Nankai University， Tianjin 300071， China)

Abstract: Abstract: O-GlcNAcylation is a special protein glycosylation， which plays crucial roles in various cellular events.Both O-GlcNAcylation and ubiquitination are important post-translational modification. They are closely related to type 2 diabetes， neurodegenerative diseases， cancer and other diseases. The cross-talk between O-GlcNAcylation and ubiquitination could be divided into four categories: (1) O-GlcNAcylaion of the 26S proteasome regulatory subunit inhibits its ATPase activity; (2) O-GlcNAcylaion on some proteins could decrease their ubiquitin proteasome degradation; (3) O-GlcNAcylation of ubiquitination enzymes regulates their functions; (4) O-GlcNAcylation on some protein (including regulatory factors) affects ubiquitination process indirectly.