title: Protein arginine methylation in mammals: who, what, and why.
abstract: The covalent marking of proteins by methyl group addition to arginine residues can promote their recognition by binding partners or can modulate their biological activity. A small family of gene products that catalyze such methylation reactions in eukaryotes (PRMTs) works in conjunction with a changing cast of associated subunits to recognize distinct cellular substrates. These reactions display many of the attributes of reversible covalent modifications such as protein phosphorylation or protein lysine methylation; however, it is unclear to what extent protein arginine demethylation occurs. Physiological roles for protein arginine methylation have been established in signal transduction, mRNA splicing, transcriptional control, DNA repair, and protein translocation.
authors.affiliation: The University of Texas M.D. Anderson Cancer Center, Science Park-Research Division, P.O. Box 389, Smithville, TX 78957, USA. mtbedford@mdanderson.org
authors.forename: Mark T
authors.initials: MT
authors.lastname: Bedford
authors.forename: Steven G
authors.initials: SG
authors.lastname: Clarke
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D008322:Mammals / Q000378:metabolism*; D008745:Methylation; D008969:Molecular Sequence Data; D011484:Protein-Arginine N-Methyltransferases / Q000737:chemistry / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D011506:Proteins; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases