[A]rginine methylation adds a layer of regulation to important molecular interactions.
Arginine methylation of RNA-binding proteins regulates cell function and differentiation†
Article first published online: 23 JAN 2012
Copyright © 2011 Wiley Periodicals, Inc.
Molecular Reproduction and Development
Volume 79, Issue 3, pages 163–175, March 2012
How to Cite
Blackwell, E. and Ceman, S. (2012), Arginine methylation of RNA-binding proteins regulates cell function and differentiation. Mol. Reprod. Dev., 79: 163–175. doi: 10.1002/mrd.22024
- Issue published online: 17 FEB 2012
- Article first published online: 23 JAN 2012
- Accepted manuscript online: 29 DEC 2011 03:23PM EST
- Manuscript Accepted: 26 DEC 2011
- Manuscript Received: 3 AUG 2011
- National Institutes of Health, University of Illinois at Urbana-Champaign Developmental Psychobiology and Neurobiology Training. Grant Number: 2T32HD007333-21
- Spastic Paralysis Research Foundation
Arginine methylation is a post-translational modification that regulates protein function. RNA-binding proteins are an important class of cell-function mediators, some of which are methylated on arginine. Early studies of RNA-binding proteins and arginine methylation are briefly introduced, and the enzymes that mediate this post-translational modification are described. We review the most common RNA-binding domains and briefly discuss how they associate with RNAs. We address the following groups of RNA-binding proteins: hnRNP, Sm, Piwi, Vasa, FMRP, and HuD. hnRNPs were the first RNA-binding proteins found to be methylated on arginine. The Sm proteins function in RNA processing and germ cell specification. The Piwi proteins are largely germ cell specific and are also required for germ cell production, as is Vasa. FMRP participates in germ cell formation in Drosophila, but is more widely known for its neuronal function. Similarly, HuD plays a role in nervous system development and function. We review the effects of arginine methylation on the function of each protein, then conclude by addressing remaining questions and future directions of arginine methylation as an important and emerging area of regulation. Mol. Reprod. Dev. 79: 163–175, 2012. © 2011 Wiley Periodicals, Inc.