Protein arginine phosphorylation in organisms.

Biling Huang, Zhixing Zhao, Yufen Zhao, Shaohua Huang

Journal: International journal of biological macromolecules 2021;171():414-422

PMID: 33428953

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Abstract

Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of "high-energy" phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging. Recently, the progress in identifying prokaryotic protein arginine kinase/phosphatase and assigning hundreds of pArg proteins and phosphosites has been made, which is arousing scientists' interest and passions. It shows that pArg is tightly connected to bacteria stress response and pathogenicity, and is probably implied in human diseases. In this review, we highlight the strategies for investigation of this mysterious modification and its momentous physiological functions, and also prospect for the potentiality of drugs development targeting pArg-relative pathways.

Address: Institute of Drug Discovery Technology, Ningbo University, Ningbo 315211, PR China. Electronic address: [email protected].; MOE Key Laboratory of Spectrochemical Analysis & Instrumentation, Department of Chemistry, College of Chemistry and Chemical Engineering, Xiamen University, Xiamen 361005, PR China.; Institute of Drug Discovery Technology, Ningbo University, Ningbo 315211, PR China; Department of Chemical Biology, College of Chemistry and Chemical Engineering, Key Laboratory for Chemical Biology of Fujian Province, Xiamen University, Xiamen 361005, PR China; Key Lab of Bioorganic Phosphorus Chemistry & Chemical Biology, Department of Chemistry, Tsinghua University, Beijing 100084, PR China. Electronic address: [email protected].; Institute of Drug Discovery Technology, Ningbo University, Ningbo 315211, PR China. Electronic address: [email protected].

DOI: 10.1016/j.ijbiomac.2021.01.015

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MeSH Terms: Arginine, Bacterial Proteins, Endopeptidase Clp, Heat-Shock Proteins, Humans, Mass Spectrometry, Phosphates, Phosphoproteins, Phosphorylation, Protein Kinases, Protein Processing, Post-Translational, Signal Transduction, Stress, Physiological, Transcription, Genetic, Virulence