Widespread arginine phosphorylation in human cells - a novel protein PTM revealed by mass spectrometry [article]

Songsen Fu, Chuan Fu, Quan Zhou, Rongcan Lin, Han Ouyang, Minning Wang, Ying Sun, Yan Liu, Yufen Zhao
2019 bioRxiv   pre-print
Arginine phosphorylation (pArg) is recently discovered as a ubiquitous protein N-phosphorylation in bacteria. However, its prevalence and roles in mammalian cells remain largely unknown due to the lack of established workflow and the inherent lability of the phosphoramidate (P-N) bond. Emerging evidence suggests that N-phosphorylation may extensively exist in eukaryotes and play crucial roles. We report an experimental phosphoproteomic workflow, which for the first time allowed to reveal the
more » ... ed to reveal the widespread occurrence of pArg in human cells by mass spectrometry. By virtue of this approach, we identified 152 high-confidence pArg sites derived from 118 proteins. Remarkably, the discovered phosphorylation motif and gene ontology of pArg hint a possible cellular function of arginine phosphorylation by regulating the favorability of propeptide convertase substrate. The generated extensive data set should enable a better understanding of the biological functions of eukaryotic pArg in the future.
doi:10.1101/725291 fatcat:p4kzk2wuajbjliate7opcmqepu