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Nat Commun. 2015 Apr 7;6:6758. doi: 10.1038/ncomms7758.

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

Author information

1
Laboratory of T cell signalling, Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
2
Cell Signaling Technology Inc., Trask Lane, Danvers, Massachusetts 01923, USA.
3
Central Proteomics Facility, Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.

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.

PMID:
25849564
PMCID:
PMC4396391
DOI:
10.1038/ncomms7758
[Indexed for MEDLINE]
Free PMC Article

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