Nontraditional translation is the key to UFMylation and beyond

作者：Mengjia Lin, Xiaoyun Zheng, Jianping Jin · 发表于：Journal of Biological Chemistry · 年份：2022 · DOI：10.1016/j.jbc.2022.102431 · 被引用次数：4 · 研究领域：Cancer-related gene regulation、Insect Resistance and Genetics、Mechanical stress and fatigue analysis

The Ubiquitin-fold modifier 1 (Ufm1) is a ubiquitin-like protein that can also be conjugated to protein substrates and subsequently alter their fates. Both UFMylation and de-UFMylation are mediated by Ufm1-specific proteases (UFSPs). In humans, it is widely believed that UFSP2 is the only active Ufm1 protease involved in Ufm1 maturation and de-UFMylation, whereas UFSP1 is thought to be inactive. Here, Liang et al. provide strong evidence showing that human UFSP1 is also an active Ufm1 protease. These results solve an age-old mystery in the human Ufm1 conjugation system and could have a greater impact not only on Ufm1 biology but also on the translation of genes employing nontraditional start codons.