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Sci. STKE, 15 February 2005
Vol. 2005, Issue 271, p. re2
Protein Interfaces in Signaling Regulated by Arginine Methylation
Carol Anne Chénard, and
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.