| Literature DB >> 19150423 |
Mark T Bedford1, Steven G Clarke.
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.Entities:
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Year: 2009 PMID: 19150423 PMCID: PMC3372459 DOI: 10.1016/j.molcel.2008.12.013
Source DB: PubMed Journal: Mol Cell ISSN: 1097-2765 Impact factor: 17.970