title: The story of protein arginine methylation: characterization, regulation, and function.
abstract: Arginine methylation is an important post-translational modification (PTM) in cells, which is catalyzed by a group of protein arginine methyltransferases (PRMTs). It plays significant roles in diverse cellular processes and various diseases. Misregulation and aberrant expression of PRMTs can provide potential biomarkers and therapeutic targets for drug discovery. Areas covered: Herein, we review the arginine methylation literature and summarize the methodologies for the characterization of this modification, as well as describe the recent insights into arginine methyltransferases and their biological functions in diseases. Expert commentary: Benefits from the enzyme-based large-scale screening approach, the novel affinity enrichment strategies, arginine methylated protein family is the focus of attention. Although a number of arginine methyltransferases and related substrates are identified, the catalytic mechanism of different types of PRMTs remains unclear and few related demethylases are characterized. Novel functional studies continuously reveal the importance of this modification in the cell cycle and diseases. A deeper understanding of arginine methylated proteins, modification sites, and their mechanisms of regulation is needed to explore their role in life processes, especially their relationship with diseases, thus accelerating the generation of potent, selective, cell-penetrant drug candidates.
authors.affiliation: a National Center for Protein Science (Shanghai), Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences , Chinese Academy of Sciences , Shanghai , China.|b Shanghai Science Research Center , Chinese Academy of Sciences , Shanghai , China.
authors.forename: Chao
authors.initials: C
authors.lastname: Peng
authors.affiliation: a National Center for Protein Science (Shanghai), Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences , Chinese Academy of Sciences , Shanghai , China.|b Shanghai Science Research Center , Chinese Academy of Sciences , Shanghai , China.
authors.forename: Catherine Cl
authors.initials: CC
authors.lastname: Wong
mesh_terms: D001120:Arginine / Q000378:metabolism*; D002318:Cardiovascular Diseases / Q000378:metabolism; D004260:DNA Repair; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D008745:Methylation; D009103:Multiple Sclerosis / Q000378:metabolism; D009134:Muscular Atrophy, Spinal / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011484:Protein-Arginine N-Methyltransferases / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D040901:Proteomics / Q000379:methods; D015398:Signal Transduction
chemical_list: D011506:Proteins; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases
keywords: PRMT; Protein arginine methylation; S-adenosylmethionine; post-translational modification; sDMA&aDMA; tandem mass spectrometry