Ringing the changes: Regulation of Parkin activity by different ubiquitin and ubiquitin-like proteins
Shalini Iyer1, Chittaranjan Das1
1Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
Structure (London, England : 1993)
|November 8, 2024
Abstract:
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.
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