Protein arginine methylation in mammals: who, what, and why.
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.
Bedford
Mark T
MT
The University of Texas M.D. Anderson Cancer Center, Science Park-Research Division, P.O. Box 389, Smithville, TX 78957, USA. mtbedford@mdanderson.org
Clarke
Steven G
SG
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
D011506:Proteins; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases