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

• 来源期刊: 中国科学:化学（英文版）
• 年，卷（期）: 2020,（3）
• 页码范围: 341-346
• 页数: 6页
• 语种: 英文

摘要

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 phosphoramidate (P-N) bond.Emerging evidences suggest that N-phosphorylation may extensively exist in eukaryotes and play crucial roles.We report a phosphoproteomic workflow,which allows for the first time revealing 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 pArg phosphorylation motif and gene ontology hint a possible cellular function of arginine phosphorylation which may regulate the favorability of propeptide convertase substrate,The obtained pArg dataset paves a way for a better understanding of the biological functions of eukaryotic pArg in the future.