Disruption of diacylglycerol metabolism impairs the induction of T cell anergy (original) (raw)

• Mathis, D. & Benoist, C. Back to central tolerance. Immunity 20, 509–516 (2004).
  Article CAS Google Scholar
• Bouneaud, C., Kourilsky, P. & Bousso, P. Impact of negative selection on the T cell repertoire reactive to a self-peptide: a large fraction of T cell clones escapes clonal deletion. Immunity 13, 829–840 (2000).
  Article CAS Google Scholar
• Schwartz, R.H. T cell anergy. Annu. Rev. Immunol. 21, 305–334 (2003).
  Article CAS Google Scholar
• Kopp, E. & Medzhitov, R. Recognition of microbial infection by Toll-like receptors. Curr. Opin. Immunol. 15, 396–401 (2003).
  Article CAS Google Scholar
• Heissmeyer, V. et al. Calcineurin imposes T cell unresponsiveness through targeted proteolysis of signaling proteins. Nat. Immunol. 5, 255–265 (2004).
  Article CAS Google Scholar
• Safford, M. et al. Egr-2 and Egr-3 are negative regulators of T cell activation. Nat. Immunol. 6, 472–480 (2005).
  Article CAS Google Scholar
• Gajewski, T.F., Qian, D., Fields, P. & Fitch, F.W. Anergic T-lymphocyte clones have altered inositol phosphate, calcium, and tyrosine kinase signaling pathways. Proc. Natl. Acad. Sci. USA 91, 38–42 (1994).
  Article CAS Google Scholar
• Wells, A.D. et al. Regulation of T cell activation and tolerance by phospholipase C γ-1-dependent integrin avidity modulation. J. Immunol. 170, 4127–4133 (2003).
  Article CAS Google Scholar
• Kang, S.M. et al. Transactivation by AP-1 is a molecular target of T cell clonal anergy. Science 257, 1134–1138 (1992).
  Article CAS Google Scholar
• Li, W., Whaley, C.D., Mondino, A. & Mueller, D.L. Blocked signal transduction to the ERK and JNK protein kinases in anergic CD4+ T cells. Science 271, 1272–1276 (1996).
  Article CAS Google Scholar
• Fields, P.E., Gajewski, T.F. & Fitch, F.W. Blocked Ras activation in anergic CD4+ T cells. Science 271, 1276–1278 (1996).
  Article CAS Google Scholar
• Acuto, O., Mise-Omata, S., Mangino, G. & Michel, F. Molecular modifiers of T cell antigen receptor triggering threshold: the mechanism of CD28 costimulatory receptor. Immunol. Rev. 192, 21–31 (2003).
  Article CAS Google Scholar
• Frauwirth, K.A. & Thompson, C.B. Regulation of T lymphocyte metabolism. J. Immunol. 172, 4661–4665 (2004).
  Article CAS Google Scholar
• Lindstein, T., June, C.H., Ledbetter, J.A., Stella, G. & Thompson, C.B. Regulation of lymphokine messenger RNA stability by a surface-mediated T cell activation pathway. Science 244, 339–343 (1989).
  Article CAS Google Scholar
• Blanchet, F., Cardona, A., Letimier, F.A., Hershfield, M.S. & Acuto, O. CD28 costimulatory signal induces protein arginine methylation in T cells. J. Exp. Med. 202, 371–377 (2005).
  Article CAS Google Scholar
• Shapiro, V.S., Truitt, K.E., Imboden, J.B. & Weiss, A. CD28 mediates transcriptional upregulation of the interleukin-2 (IL-2) promoter through a composite element containing the CD28RE and NF-IL-2B AP-1 sites. Mol. Cell. Biol. 17, 4051–4058 (1997).
  Article CAS Google Scholar
• Cory, S. & Adams, J.M. The Bcl2 family: regulators of the cellular life-or-death switch. Nat. Rev. Cancer 2, 647–656 (2002).
  Article CAS Google Scholar
• Fox, C.J., Hammerman, P.S. & Thompson, C.B. Fuel feeds function: energy metabolism and the T-cell response. Nat. Rev. Immunol. 5, 844–852 (2005).
  Article CAS Google Scholar
• Jenkins, M.K., Pardoll, D.M., Mizuguchi, J., Chused, T.M. & Schwartz, R.H. Molecular events in the induction of a nonresponsive state in interleukin 2-producing helper T-lymphocyte clones. Proc. Natl. Acad. Sci. USA 84, 5409–5413 (1987).
  Article CAS Google Scholar
• Macian, F. et al. Transcriptional mechanisms underlying lymphocyte tolerance. Cell 109, 719–731 (2002).
  Article CAS Google Scholar
• Su, B. et al. JNK is involved in signal integration during costimulation of T lymphocytes. Cell 77, 727–736 (1994).
  Article Google Scholar
• Harhaj, E.W. & Sun, S.C. IκB kinases serve as a target of CD28 signaling. J. Biol. Chem. 273, 25185–25190 (1998).
  Article CAS Google Scholar
• Lyakh, L., Ghosh, P. & Rice, N.R. Expression of NFAT-family proteins in normal human T cells. Mol. Cell. Biol. 17, 2475–2484 (1997).
  Article CAS Google Scholar
• Dolmetsch, R.E., Lewis, R.S., Goodnow, C.C. & Healy, J.I. Differential activation of transcription factors induced by Ca2+ response amplitude and duration. Nature 386, 855–858 (1997).
  Article CAS Google Scholar
• Dower, N.A. et al. RasGRP is essential for mouse thymocyte differentiation and TCR signaling. Nat. Immunol. 1, 317–321 (2000).
  Article CAS Google Scholar
• Luo, B., Regier, D.S., Prescott, S.M. & Topham, M.K. Diacylglycerol kinases. Cell. Signal. 16, 983–989 (2004).
  Article CAS Google Scholar
• Zhong, X.P. et al. Enhanced T cell responses due to diacylglycerol kinase-ζ deficiency. Nat. Immunol. 4, 882–890 (2003).
  Article CAS Google Scholar
• Zhong, X.P. et al. Regulation of T cell receptor-induced activation of the Ras-ERK pathway by diacylglycerol kinase ζ. J. Biol. Chem. 277, 31089–31098 (2002).
  Article CAS Google Scholar
• Berney, S.M. & Atkinson, T.P. Phosphatidylinositol hydrolysis in freshly isolated human T lymphocytes. J. Immunol. Methods 186, 71–77 (1995).
  Article CAS Google Scholar
• Antony, P. et al. B-cell antigen receptor activates transcription factors NFAT (nuclear factor of activated T-cells) and NF-κB (nuclear factor κB) via a mechanism that involves diacylglycerol. Biochem. Soc. Trans. 32, 113–115 (2004).
  Article CAS Google Scholar
• Rellahan, B.L., Jones, L.A., Kruisbeek, A.M., Fry, A.M. & Matis, L.A. In vivo induction of anergy in peripheral Vβ8+ T cells by staphylococcal enterotoxin B. J. Exp. Med. 172, 1091–1100 (1990).
  Article CAS Google Scholar
• Kawabe, Y. & Ochi, A. Selective anergy of Vβ8+,CD4+ T cells in staphylococcus enterotoxin B-primed mice. J. Exp. Med. 172, 1065–1070 (1990).
  Article CAS Google Scholar
• Jiang, Y., Sakane, F., Kanoh, H. & Walsh, J.P. Selectivity of the diacylglycerol kinase inhibitor 3-[2-(4-[bis-(4-fluorophenyl)methylene]-1-piperidinyl)ethyl]-2, 3-dihydro-2-thioxo-4(1H)quinazolinone (R59949) among diacylglycerol kinase subtypes. Biochem. Pharmacol. 59, 763–772 (2000).
  Article CAS Google Scholar
• Jones, D.R., Sanjuan, M.A., Stone, J.C. & Merida, I. Expression of a catalytically inactive form of diacylglycerol kinase α induces sustained signaling through RasGRP. FASEB J. 16, 595–597 (2002).
  Article CAS Google Scholar
• Merida, I., Williamson, P., Smith, K. & Gaulton, G.N. The role of diacylglycerol kinase activation and phosphatidate accumulation in interleukin-2-dependent lymphocyte proliferation. DNA Cell Biol. 12, 473–479 (1993).
  Article CAS Google Scholar
• Williamson, P., Merida, I. & Gaulton, G. Protein and lipid kinase activation cascades in interleukin-2 receptor signalling. Semin. Immunol. 5, 337–344 (1993).
  Article CAS Google Scholar
• Flores, I., Casaseca, T., Martinez, A.C., Kanoh, H. & Merida, I. Phosphatidic acid generation through interleukin 2 (IL-2)-induced α-diacylglycerol kinase activation is an essential step in IL-2-mediated lymphocyte proliferation. J. Biol. Chem. 271, 10334–10340 (1996).
  Article CAS Google Scholar
• Jones, D.R., Flores, I., Diaz, E., Martinez, C. & Merida, I. Interleukin-2 stimulates a late increase in phosphatidic acid production in the absence of phospholipase D activation. FEBS Lett. 433, 23–27 (1998).
  Article CAS Google Scholar
• Flores, I. et al. Diacylglycerol kinase inhibition prevents IL-2-induced G1 to S transition through a phosphatidylinositol-3 kinase-independent mechanism. J. Immunol. 163, 708–714 (1999).
  CAS PubMed Google Scholar
• Boonen, G.J. et al. CD28 induces cell cycle progression by IL-2-independent down-regulation of p27kip1 expression in human peripheral T lymphocytes. Eur. J. Immunol. 29, 789–798 (1999).
  Article CAS Google Scholar
• Jenkins, M.K. The role of cell division in the induction of clonal anergy. Immunol. Today 13, 69–73 (1992).
  Article CAS Google Scholar
• Topham, M.K. & Prescott, S.M. Mammalian diacylglycerol kinases, a family of lipid kinases with signaling functions. J. Biol. Chem. 274, 11447–11450 (1999).
  Article CAS Google Scholar
• English, D. Phosphatidic acid: a lipid messenger involved in intracellular and extracellular signalling. Cell. Signal. 8, 341–347 (1996).
  Article CAS Google Scholar
• Avila-Flores, A., Santos, T., Rincon, E. & Merida, I. Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid. J. Biol. Chem. 280, 10091–10099 (2005).
  Article CAS Google Scholar
• Jones, G.A. & Carpenter, G. The regulation of phospholipase C-γ1 by phosphatidic acid. Assessment of kinetic parameters. J. Biol. Chem. 268, 20845–20850 (1993).
  CAS PubMed Google Scholar
• Luo, B., Prescott, S.M. & Topham, M.K. Diacylglycerol kinase ζ regulates phosphatidylinositol 4-phosphate 5-kinase Iα by a novel mechanism. Cell. Signal. 16, 891–897 (2004).
  Article CAS Google Scholar
• Lauener, R., Shen, Y., Duronio, V. & Salari, H. Selective inhibition of phosphatidylinositol 3-kinase by phosphatidic acid and related lipids. Biochem. Biophys. Res. Commun. 215, 8–14 (1995).
  Article CAS Google Scholar
• Sanjuan, M.A. et al. T cell activation in vivo targets diacylglycerol kinase α to the membrane: a novel mechanism for Ras attenuation. J. Immunol. 170, 2877–2883 (2003).
  Article CAS Google Scholar
• Fukunaga-Takenaka, R. et al. Importance of chroman ring and tyrosine phosphorylation in the subtype-specific translocation and activation of diacylglycerol kinase α by D-α-tocopherol. Genes Cells 10, 311–319 (2005).
  Article CAS Google Scholar
• Ali, H. et al. Selective translocation of diacylglycerol kinase ζ in hippocampal neurons under transient forebrain ischemia. Neurosci. Lett. 372, 190–195 (2004).
  Article CAS Google Scholar
• D'Santos, C.S., Clarke, J.H., Irvine, R.F. & Divecha, N. Nuclei contain two differentially regulated pools of diacylglycerol. Curr. Biol. 9, 437–440 (1999).
  Article CAS Google Scholar
• Topham, M.K. et al. Protein kinase C regulates the nuclear localization of diacylglycerol kinase-ζ. Nature 394, 697–700 (1998).
  Article CAS Google Scholar
• Abramovici, H., Hogan, A.B., Obagi, C., Topham, M.K. & Gee, S.H. Diacylglycerol kinase-zeta localization in skeletal muscle is regulated by phosphorylation and interaction with syntrophins. Mol. Biol. Cell 14, 4499–4511 (2003).
  Article CAS Google Scholar
• Cipres, A. et al. Regulation of diacylglycerol kinase α by phosphoinositide 3-kinase lipid products. J. Biol. Chem. 278, 35629–35635 (2003).
  Article CAS Google Scholar
• Luo, B., Prescott, S.M. & Topham, M.K. Protein kinase C α phosphorylates and negatively regulates diacylglycerol kinase ζ. J. Biol. Chem. 278, 39542–39547 (2003).
  Article CAS Google Scholar
• Vakoc, C.R., Mandat, S.A., Olenchock, B.A. & Blobel, G.A. Histone H3 lysine 9 methylation and HP1γ are associated with transcription elongation through mammalian chromatin. Mol. Cell 19, 381–391 (2005).
  Article CAS Google Scholar