Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 15 February 2005
Vol. 2005, Issue 271, p. re2
[DOI: 10.1126/stke.2712005re2]


Protein Interfaces in Signaling Regulated by Arginine Methylation

Francois-Michel Boisvert, Carol Anne Chénard, and Stéphane Richard*

Terry Fox Molecular Oncology Group and Bloomfield Center for Research on Aging, Lady Davis Institute for Medical Research, Departments of Oncology and Medicine, McGill University, Montréal, Québec, Canada H3T 1E2.

Gloss: Posttranslational covalent modifications of proteins provide a major mechanism for cellular signal transduction. Arginine methylation is a covalent modification that results in the addition of methyl groups on the arginine side chains catalyzed by members of the protein arginine methyltransferase (PRMT) family. Identification of several arginine-methylated proteins indicates that arginine methylation influences several signaling pathways. Involvement of PRMT1, the major arginine methyltransferase, in T cell signaling, in response to lipopolysaccharides, in the stabilization of tumor necrosis factor–α mRNA, and in cytokine responses implicates this posttranslational modification in regulation of cell proliferation and antiviral responses. Arginine methylation can regulate protein-protein interactions. SH3 domains that normally associate with polyproline-rich ligands fail to do so when the neighboring arginine is dimethylated. Many other examples have now been documented, including protein interactions that are positively regulated by arginine methylation. This review focuses on how arginine methylation is implicated in protein-protein interactions that influence cell signaling.

*Corresponding author. E-mail: stephane.richard{at}

Citation: F.-M. Boisvert, C. A. Chénard, S. Richard, Protein Interfaces in Signaling Regulated by Arginine Methylation. Sci. STKE 2005, re2 (2005).

Transcriptional repression of hypoxia-inducible factor-1 (HIF-1) by the protein arginine methyltransferase PRMT1.
V. N. Lafleur, S. Richard, and D. E. Richard (2014)
Mol. Biol. Cell 25, 925-935
   Abstract »    Full Text »    PDF »
Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations.
M. L. Tradewell, Z. Yu, M. Tibshirani, M.-C. Boulanger, H. D. Durham, and S. Richard (2012)
Hum. Mol. Genet. 21, 136-149
   Abstract »    Full Text »    PDF »
Protein Arginine Methylation in Parasitic Protozoa.
J. C. Fisk and L. K. Read (2011)
Eukaryot. Cell 10, 1013-1022
   Abstract »    Full Text »    PDF »
TbPRMT6 Is a Type I Protein Arginine Methyltransferase That Contributes to Cytokinesis in Trypanosoma brucei.
J. C. Fisk, C. Zurita-Lopez, J. Sayegh, D. L. Tomasello, S. G. Clarke, and L. K. Read (2010)
Eukaryot. Cell 9, 866-877
   Abstract »    Full Text »    PDF »
Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA.
E. Blackwell, X. Zhang, and S. Ceman (2010)
Hum. Mol. Genet. 19, 1314-1323
   Abstract »    Full Text »    PDF »
Arginine Methylation Regulates Telomere Length and Stability.
T. R. H. Mitchell, K. Glenfield, K. Jeyanthan, and X.-D. Zhu (2009)
Mol. Cell. Biol. 29, 4918-4934
   Abstract »    Full Text »    PDF »
Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function.
A. E. McBride, A. K. Conboy, S. P. Brown, C. Ariyachet, and K. L. Rutledge (2009)
Nucleic Acids Res. 37, 4322-4330
   Abstract »    Full Text »    PDF »
TDRD3, a novel Tudor domain-containing protein, localizes to cytoplasmic stress granules.
I. Goulet, S. Boisvenue, S. Mokas, R. Mazroui, and J. Cote (2008)
Hum. Mol. Genet. 17, 3055-3074
   Abstract »    Full Text »    PDF »
KH-type splicing regulatory protein interacts with survival motor neuron protein and is misregulated in spinal muscular atrophy.
H. Tadesse, J. Deschenes-Furry, S. Boisvenue, and J. Cote (2008)
Hum. Mol. Genet. 17, 506-524
   Abstract »    Full Text »    PDF »
PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation.
D. Hyllus, C. Stein, K. Schnabel, E. Schiltz, A. Imhof, Y. Dou, J. Hsieh, and U.-M. Bauer (2007)
Genes & Dev. 21, 3369-3380
   Abstract »    Full Text »    PDF »
Regulation of the Nuclear Poly(A)-binding Protein by Arginine Methylation in Fission Yeast.
A. Perreault, C. Lemieux, and F. Bachand (2007)
J. Biol. Chem. 282, 7552-7562
   Abstract »    Full Text »    PDF »
delayed flowering1 Encodes a Basic Leucine Zipper Protein That Mediates Floral Inductive Signals at the Shoot Apex in Maize.
M. G. Muszynski, T. Dam, B. Li, D. M. Shirbroun, Z. Hou, E. Bruggemann, R. Archibald, E. V. Ananiev, and O. N. Danilevskaya (2006)
Plant Physiology 142, 1523-1536
   Abstract »    Full Text »    PDF »
Divergence of the Dof Gene Families in Poplar, Arabidopsis, and Rice Suggests Multiple Modes of Gene Evolution after Duplication.
X. Yang, G. A. Tuskan, and Z.-M. Cheng (2006)
Plant Physiology 142, 820-830
   Abstract »    Full Text »    PDF »
Methylation regulates the intracellular protein-protein and protein-RNA interactions of FMRP.
N. Dolzhanskaya, G. Merz, J. M. Aletta, and R. B. Denman (2006)
J. Cell Sci. 119, 1933-1946
   Abstract »    Full Text »    PDF »
Autoregulation of Ribosome Biosynthesis by a Translational Response in Fission Yeast.
F. Bachand, D. H. Lackner, J. Bahler, and P. A. Silver (2006)
Mol. Cell. Biol. 26, 1731-1742
   Abstract »    Full Text »    PDF »
Arginine Methylation of Yeast mRNA-binding Protein Npl3 Directly Affects Its Function, Nuclear Export, and Intranuclear Protein Interactions.
A. E. McBride, J. T. Cook, E. A. Stemmler, K. L. Rutledge, K. A. McGrath, and J. A. Rubens (2005)
J. Biol. Chem. 280, 30888-30898
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882