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Department of Immunology and Oncology, Centro Nacional de Biotecnología, Campus de Cantoblanco, Madrid, Spain
Stimulation via IL-2R ligation causes T lymphocytes to transit
through the cell cycle. Previous experiments by our group have
demonstrated that, in human T cells, IL-2 binding induces phosphatidic
acid production through activation of the 
isoform of diacylglycerol
kinase. In this study, using the IL-2-dependent mouse T cell line
CTLL-2, we demonstrate that pharmacological inhibition of IL-2-induced
diacylglycerol kinase activation is found to block IL-2-induced late
G1 to S transition without affecting cell viability.
Herein, we demonstrate that diacylglycerol kinase inhibition has a
profound effect on the induction of the protooncogenes c-myc, c-fos,
and c-raf by IL-2, whereas expression of bcl-2 and bcl-xL
are not affected. When the IL-2-regulated cell cycle control
checkpoints are examined in detail, we demonstrate that inhibition of
diacylglycerol kinase activation prevents IL-2 induction of cyclin D3
without affecting p27 down-regulation. The strict control of cell
proliferation exerted by phosphatidic acid through activation of
diacylglycerol kinase is independent of other well-characterized
IL-2R-derived signals, such as the phosphatidylinositol-3 kinase/Akt
pathway, indicating the existence of a different and important
mechanism to control cell division.
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