当前位置: X-MOL 学术Structure › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Ringing the changes: Regulation of Parkin activity by different ubiquitin and ubiquitin-like proteins
Structure ( IF 4.4 ) Pub Date : 2024-11-07 , DOI: 10.1016/j.str.2024.10.015
Shalini Iyer, Chittaranjan Das

Phosphorylation of ubiquitin and the ubiquitin-like domain of Parkin, mediated by the kinase PINK1, is essential for the liberation of the E3 ligase from its autoinhibited state. In this issue of Structure, Lenka et al.1 provide the structural basis for the specificity and stronger Parkin activation by phospho-NEDD8 compared to phospho-ubiquitin.

中文翻译:


敲响变化:不同泛素和泛素样蛋白对 Parkin 活性的调节



由激酶 PINK1 介导的泛素和 Parkin 泛素样结构域的磷酸化对于 E3 连接酶从其自身抑制状态中释放至关重要。在本期 Structure 中,Lenka 等人1 为磷酸化泛素相比,磷酸化 NEDD8 的特异性和更强的 Parkin 激活提供了结构基础。
更新日期:2024-11-07
down
wechat
bug