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Mol Cell. 2009 Jan 16;33(1):1-13. doi: 10.1016/j.molcel.2008.12.013.

Protein arginine methylation in mammals: who, what, and why.

Author information

1
The University of Texas M.D. Anderson Cancer Center, Science Park-Research Division, P.O. Box 389, Smithville, TX 78957, USA. mtbedford@mdanderson.org

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.

PMID:
19150423
PMCID:
PMC3372459
DOI:
10.1016/j.molcel.2008.12.013
[Indexed for MEDLINE]
Free PMC Article

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