title: Protein interfaces in signaling regulated by arginine methylation.
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.
authors.affiliation: Terry Fox Molecular Oncology Group and Bloomfield Center for Research on Aging, Lady Davis Institute for Medical Research, Department of Oncology, McGill University, Montréal, Québec, Canada H3T 1E2.
authors.forename: François-Michel
authors.initials: FM
authors.lastname: Boisvert
authors.forename: Carol Anne
authors.initials: CA
authors.lastname: Chénard
authors.forename: Stéphane
authors.initials: S
authors.lastname: Richard
mesh_terms: D000818:Animals; D001120:Arginine / Q000737:chemistry*; D016384:Consensus Sequence; D029721:Drosophila Proteins / Q000502:physiology; D005057:Eukaryotic Cells / Q000378:metabolism; D006801:Humans; D006860:Hydrogen Bonding; D006867:Hydrolases / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008745:Methylation; D050778:NFATC Transcription Factors / Q000378:metabolism; D010802:Phylogeny; D010940:Plant Proteins / Q000502:physiology; D011485:Protein Binding; D025941:Protein Interaction Mapping; D011499:Protein Processing, Post-Translational; D000080002:Protein-Arginine Deiminase Type 4; D000076342:Protein-Arginine Deiminases; D011484:Protein-Arginine N-Methyltransferases / Q000145:classification / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology*; D013379:Substrate Specificity
chemical_list: D029721:Drosophila Proteins; D050778:NFATC Transcription Factors; D010940:Plant Proteins; D029701:Saccharomyces cerevisiae Proteins; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases; D006867:Hydrolases; C000629235:PADI4 protein, human; D000080002:Protein-Arginine Deiminase Type 4; D000076342:Protein-Arginine Deiminases