Protein interfaces in signaling regulated by arginine methylation.
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.
Boisvert
François-Michel
FM
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.
Chénard
Carol Anne
CA
Richard
Stéphane
S
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
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