Deficiency of N-myristoylation reveals calcineurin activity as regulator of IFN-γ-producing γδ T cells

J Leukoc Biol. 2017 Apr;101(4):1005-1014. doi: 10.1189/jlb.1A0616-264R. Epub 2017 Jan 6.

Abstract

γδ T cell subsets can be characterized, in part, by their secretion of select proinflammatory cytokines. The molecular mechanisms driving the diverse fates of γδ T cells have not been elucidated. We have previously shown that the attachment of myristic acid to the N-terminal glycine of proteins, termed N-myristoylation, is essential for αβ T cell development and activation. Here, we explore the potential role of this lipid modification on the activation of γδ T cells. In the absence of N-myristoylation, the CD27+ γδ T cell subset was dominantly affected. The cells produced high levels of IFN-γ upon stimulation. In addition, they were more sensitive to inhibition of the CaN-Nfat pathway than were γδ T cells with myristoylated CaN. N-Myristoylation was found to modulate activity of phosphatase CaN, a regulator of Nfat. In summary, the CaN-Nfat pathway regulates development and function of IFN-γ-producing γδ T cells, and its balanced activity is strongly dependent on CaN N-myristoylation.

Keywords: CD27+ γδ T cells; Calcineurin-Nfatc pathway; IFN-γ; IL-17A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Calcineurin / metabolism*
  • Cell Nucleus / metabolism
  • Interferon-gamma / metabolism*
  • Mice
  • Mice, Knockout
  • Myristic Acid / metabolism*
  • NFATC Transcription Factors / metabolism
  • Receptors, Antigen, T-Cell, gamma-delta / metabolism*
  • T-Box Domain Proteins / metabolism
  • Tumor Necrosis Factor Receptor Superfamily, Member 7

Substances

  • NFATC Transcription Factors
  • Receptors, Antigen, T-Cell, gamma-delta
  • T-Box Domain Proteins
  • T-box transcription factor TBX21
  • Tumor Necrosis Factor Receptor Superfamily, Member 7
  • Myristic Acid
  • Interferon-gamma
  • Calcineurin