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

Author

Listed:
  • Vincent Geoghegan

    (Laboratory of T cell signalling, Sir William Dunn School of Pathology, University of Oxford
    Present address: Biomedical and Life Sciences, Lancaster University, Lancaster, UK)

  • Ailan Guo

    (Cell Signaling Technology Inc.)

  • David Trudgian

    (Central Proteomics Facility, Sir William Dunn School of Pathology, University of Oxford
    Present address: Biochemistry Department and Proteomics Core, University of Texas Southwestern Medical Center, Dallas, Texas, USA)

  • 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)

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.

Suggested Citation

  • Vincent Geoghegan & Ailan Guo & David Trudgian & Benjamin Thomas & Oreste Acuto, 2015. "Comprehensive identification of arginine methylation in primary T cells reveals regulatory roles in cell signalling," Nature Communications, Nature, vol. 6(1), pages 1-8, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7758
    DOI: 10.1038/ncomms7758
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    1. Lei Shen & Xiaokuang Ma & Yuanyuan Wang & Zhihao Wang & Yi Zhang & Hoang Quoc Hai Pham & Xiaoqun Tao & Yuehua Cui & Jing Wei & Dimitri Lin & Tharindumala Abeywanada & Swanand Hardikar & Levon Halabeli, 2024. "Loss-of-function mutation in PRMT9 causes abnormal synapse development by dysregulation of RNA alternative splicing," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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