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
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
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。