Comprehensive identification of arginine methylation in primary T cells reveals regulatory roles in cell signalling

Vincent Geoghegan (), Ailan Guo, David Trudgian, Benjamin Thomas and Oreste Acuto ()
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Vincent Geoghegan: Laboratory of T cell signalling, Sir William Dunn School of Pathology, University of Oxford
Ailan Guo: Cell Signaling Technology Inc.
David Trudgian: Central Proteomics Facility, Sir William Dunn School of Pathology, University of Oxford
Benjamin Thomas: Central Proteomics Facility, Sir William Dunn School of Pathology, University of Oxford
Oreste Acuto: Laboratory of T cell signalling, Sir William Dunn School of Pathology, University of Oxford

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: Abstract The impact of protein arginine methylation on the regulation of immune functions is virtually unknown. Here, we apply a novel method—isomethionine methyl-SILAC—coupled with antibody-mediated arginine-methylated peptide enrichment to identify methylated peptides in human T cells by mass spectrometry. This approach allowed the identification of 2,502 arginine methylation sites from 1,257 tissue-specific and housekeeping proteins. We find that components of T cell antigen receptor signal machinery and several key transcription factors that regulate T cell fate determination are methylated on arginine. Moreover, we demonstrate changes in arginine methylation stoichiometry during cellular stimulation in a subset of proteins critical to T cell differentiation. Our data suggest that protein arginine methyltransferases exert key regulatory roles in T cell activation and differentiation, opening a new field of investigation in T cell biology.

Date: 2015
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DOI: 10.1038/ncomms7758

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