| First Author | Rampoldi F | Year | 2017 |
| Journal | J Leukoc Biol | Volume | 101 |
| Issue | 4 | Pages | 1005-1014 |
| PubMed ID | 28062573 | Mgi Jnum | J:273992 |
| Mgi Id | MGI:6295211 | Doi | 10.1189/jlb.1A0616-264R |
| Citation | Rampoldi F, et al. (2017) Deficiency of N-myristoylation reveals calcineurin activity as regulator of IFN-gamma-producing gammadelta T cells. J Leukoc Biol 101(4):1005-1014 |
| abstractText | gammadelta T cell subsets can be characterized, in part, by their secretion of select proinflammatory cytokines. The molecular mechanisms driving the diverse fates of gammadelta 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 alphabeta T cell development and activation. Here, we explore the potential role of this lipid modification on the activation of gammadelta T cells. In the absence of N-myristoylation, the CD27(+) gammadelta T cell subset was dominantly affected. The cells produced high levels of IFN-gamma upon stimulation. In addition, they were more sensitive to inhibition of the CaN-Nfat pathway than were gammadelta 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-gamma-producing gammadelta T cells, and its balanced activity is strongly dependent on CaN N-myristoylation. |
