Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS
Volume 1839, Issue 8, Pages 702-710Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagrm.2014.02.015
Keywords
Arginine methylation; Tudor domain; CARM1; PRMT1; Histone code
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Funding
- CPRIT [RP110471]
- NIH [DK062248]
- Center for Cancer Epigenetics (CCE) at MD Anderson Cancer Center
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Arginine methylation is a common posttranslational modification (PTM) that alters roughly 0.5% of all arginine residues in the cells. There are three types of arginine methylation: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA), and symmetric dimethylarginine (SDMA). These three PTMs are enriched on RNA-binding proteins and on histones, and also impact signal transduction cascades. To date, over thirty arginine methylation sites have been cataloged on the different core histones. These modifications alter protein structure, impact interactions with DNA, and also generate docking sites for effector molecules. The primary readers of methylarginine marks are Tudor domain-containing proteins. The complete family of thirty-six Tudor domain-containing proteins has yet to be fully characterized, but at least ten bind methyllysine motifs and eight bind methylarginine motifs. In this review, we will highlight the biological roles of the Tudor domains that interact with arginine methylated motifs, and also address other types of interactions that are regulated by these particular PTMs. (C) 2014 Elsevier B.V. All rights reserved.
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