β-Arrestin and Mdm2, Unsuspected Partners in Signaling from the Cell Surface
β-Arrestin and Mdm2, Unsuspected Partners in Signaling from the Cell Surface
复制标题
DOI：
10.1126/stke.2001.110.pe41
复制
发表时间：
2001-11
期刊：
影响因子：
--
通讯作者：
G. Strous;Julia Schantl
中科院分区：
文献类型：
--
作者：
G. Strous;Julia Schantl
MDM2是一种泛素-蛋白连接酶，可泛化P53，通过泛素-蛋白酶体系统促进其降解。Shenoy和他的同事发现，MDM2可以通过与β-arrestin相互作用，在细胞表面β-肾上腺素能受体(β-AR)的隔离中发挥关键作用。Stous和Schantl讨论了MDM2可能是如何通过G蛋白偶联受体(GPCRs)将细胞外信号连接到P53及其在细胞凋亡和细胞周期进展中的功能的开关。
Mdm2 is a ubiquitin-protein ligase known to ubiquitinate p53, promoting its degradation by the ubiquitin-proteasome system. Shenoy and co-workers showed that Mdm2 can act as a key factor in the sequestration of the cell surface β2-adrenergic receptor (β-AR) through interactions with β-arrestin. Strous and Schantl discuss how Mdm2 may be a switch connecting extracellular signals mediated through G protein-coupled receptors (GPCRs) to p53 and its functions in apoptosis and cell cycle progression.