AI Article Synopsis
- The phosphorylation of ubiquitin and Parkin's ubiquitin-like domain by the kinase PINK1 is crucial for activating Parkin from its inactive form.
- Lenka et al. present findings that explain how phospho-NEDD8 activates Parkin more effectively than phospho-ubiquitin.
- The study provides valuable structural insights into the mechanisms of E3 ligase activation, which could have implications for understanding related cellular processes.
Article 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. provide the structural basis for the specificity and stronger Parkin activation by phospho-NEDD8 compared to phospho-ubiquitin.
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| http://dx.doi.org/10.1016/j.str.2024.10.015 | DOI Listing |
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