Protein Arginine Methylation in Mammals: Who, What, and Why

Mark T. Bedford; Steven G. Clarke

doi:10.1016/j.molcel.2008.12.013

Protein Arginine Methylation in Mammals: Who, What, and Why

Mark T. Bedford, Steven G. Clarke

Epigenetics & Molecular Carcinogenesis

Research output: Contribution to journal › Review article › peer-review

1374 Scopus citations

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.

Original language	English (US)
Pages (from-to)	1-13
Number of pages	13
Journal	Molecular cell
Volume	33
Issue number	1
DOIs	https://doi.org/10.1016/j.molcel.2008.12.013
State	Published - Jan 16 2009

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/j.molcel.2008.12.013

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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.",

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note = "Funding Information: We apologize to those researchers whose original work could not be cited due to space constraints. M.T.B. is supported by NIH grant no. DK62248. S.G.C. is supported by NIH grant no. GM026020. We would like to thank the following people for reading over this review: St{\'e}phane Richard, Laurie Read, Adam Frankel, and members of the Clarke and Bedford Laboratories.",

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AB - 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.

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Protein Arginine Methylation in Mammals: Who, What, and Why

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