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

REVIEWS

Protein Interfaces in Signaling Regulated by Arginine Methylation

François-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.

Abstract: Posttranslational modifications are well-known effectors of signal transduction. Arginine methylation is a covalent modification that results in the addition of methyl groups to the nitrogen atoms of the arginine side chains. A probable role of arginine methylation in signal transduction is emerging with the identification of new arginine-methylated proteins. However, the functional consequences of arginine methylation and its mode of regulation remain unknown. The identification of the protein arginine methyltransferase family and the development of methylarginine-specific antibodies have raised renewed interest in this modification during the last decade. Arginine methylation was mainly observed on abundant proteins such as RNA-binding proteins and histones, but recent advances have revealed a plethora of arginine-methylated proteins implicated in a variety of cellular processes, including signaling by interferon and cytokines, and in T cell signaling. We discuss these recent advances and the role of arginine methylation in signal transduction.

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

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

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