泛素化和磷酸化协同作用调控蛋白质降解  

Ubiquitination and Phosphorylation Cooperate to Regulate the Degradation of Protein

作　　者：易艳萍[1] 曹诚[1] 马清钧[1] 

机构地区：[1]军事医学科学院生物工程研究所,北京100850

出　　处：《生物技术通讯》2006年第4期618-620,共3页Letters in Biotechnology

摘　　要：在真核细胞中,泛素化和磷酸化是2种常见的蛋白质修饰方式。泛素在蛋白酶体降解途径中发挥重要的靶向作用,细胞外信号严格调控着目的蛋白的泛素化。在很多情况下,这种调控依赖于蛋白质的磷酸化。由磷酸化影响的调控步骤可能与E3泛素连接酶对底物的识别有关,也可能与实际的交联反应有关。这种调控是通过对底物或E3连接酶本身的磷酸化实现的。Ubiquitination and phosphorylation are two common protein modification modes in all eukaryotes. Ubiquitination functions in targeting proteins for proteasomal degradation and ubiquitination are tightly regulated in response to extracellular signal.In many cases, this regulation depends on protein phosphorylation. The regulatory step affected by phosphorylation could involve either recognition of the substrate by an E3 ubiquitin ligase or the actual conjugation reaction. Regulation occurs through phosphorylation of either the substrates or the E3 ligases themselves.

关 键 词：泛素化 磷酸化 

分 类 号：Q75[生物学—分子生物学]