Acylglycerol Kinase Maintains Metabolic State and Immune Responses of CD8+ T Cells

Cell Metab. 2019 Aug 6;30(2):290-302.e5. doi: 10.1016/j.cmet.2019.05.016. Epub 2019 Jun 13.

Abstract

CD8+ T cell expansions and functions rely on glycolysis, but the mechanisms underlying CD8+ T cell glycolytic metabolism remain elusive. Here, we show that acylglycerol kinase (AGK) is required for the establishment and maintenance of CD8+ T cell metabolic and functional fitness. AGK deficiency dampens CD8+ T cell antitumor functions in vivo and perturbs CD8+ T cell proliferation in vitro. Activation of phosphatidylinositol-3-OH kinase (PI3K)-mammalian target of rapamycin (mTOR) signaling, which mediates elevated CD8+ T cell glycolysis, is tightly dependent on AGK kinase activity. Mechanistically, T cell antigen receptor (TCR)- and CD28-stimulated recruitment of PTEN to the plasma membrane facilitates AGK-PTEN interaction and AGK-triggered PTEN phosphorylation, thereby restricting PTEN phosphatase activity in CD8+ T cells. Collectively, these results demonstrate that AGK maintains CD8+ T cell metabolic and functional state by restraining PTEN activity and highlight a critical role for AGK in CD8+ T cell metabolic programming and effector function.

Keywords: AGK; CD8+ T cells; PI3K-mTOR; PTEN; glycolysis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CD8-Positive T-Lymphocytes / immunology*
  • Female
  • Male
  • Melanoma, Experimental / immunology*
  • Melanoma, Experimental / metabolism*
  • Melanoma, Experimental / pathology
  • Mice
  • Mice, Transgenic
  • Phosphotransferases (Alcohol Group Acceptor) / immunology*
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism*

Substances

  • Phosphotransferases (Alcohol Group Acceptor)
  • acylglycerol kinase