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PMID: 15713950 Published · epublish English Journal Article Review

Protein interfaces in signaling regulated by arginine methylation.

Science's STKE : signal transduction knowledge environment ·Vol. 2005 ·No. 271 ·2005-02-15 ·Pages re2

Boisvert FM, Chénard CA, Richard S

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.

MeSH Terms
Animals Arginine/chemistry Consensus Sequence Drosophila Proteins/physiology Eukaryotic Cells/metabolism Humans Hydrogen Bonding Hydrolases/metabolism Hydrophobic and Hydrophilic Interactions Methylation NFATC Transcription Factors/metabolism Phylogeny Plant Proteins/physiology Protein Binding Protein Interaction Mapping Protein Processing, Post-Translational Protein-Arginine Deiminase Type 4 Protein-Arginine Deiminases Protein-Arginine N-Methyltransferases/classification,physiology Saccharomyces cerevisiae Proteins/physiology Signal Transduction/physiology Substrate Specificity
Chemicals
Drosophila Proteins NFATC Transcription Factors Plant Proteins Saccharomyces cerevisiae Proteins Arginine Protein-Arginine N-Methyltransferases Hydrolases PADI4 protein, human Protein-Arginine Deiminase Type 4 Protein-Arginine Deiminases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Boisvert François-Michel
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
Richard Stéphane
Article Info
Journal
Science's STKE : signal transduction knowledge environment
Abbr.
Sci STKE
ISSN
1525-8882
Published
2005-02-15
Epub
2005-00-15
Pages
re2
Language
English
Region
United States
NLM ID
100964423
Subset
IM
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