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Blood, 15 September 2000, Vol. 96, No. 6, pp. 2181-2190
IMMUNOBIOLOGY
Signaling via LAT (linker for T-cell activation)
and Syk/ZAP70 is required for ERK
activation and NFAT transcriptional activation following
CD2 stimulation
Maria Paola Martelli,
Huamao Lin,
Weiguo Zhang,
Lawrence E. Samelson, and
Barbara E. Bierer
From the Laboratory of Lymphocyte Biology, National
Heart, Lung, and Blood Institute, Laboratory of Cellular and Molecular
Biology, National Cancer Institute, National Institutes of Health,
Bethesda, MD.
Activation of T cells can be initiated through cell surface
molecules in addition to the T-cell receptor-CD3 (TCR-CD3) complex. In
human T cells, ligation of the CD2 molecule by mitogenic pairs of
anti-CD2 monoclonal antibodies activates T cells via biochemical signaling pathways similar but not identical to those elicited on TCR
engagement. This study describes a key role for the p36/38 membrane
adapter protein linker for T cell activation (LAT) in CD2-mediated
T-cell activation. Following ligation of CD2 on the surface of the
Jurkat T-cell line and human purified T cells, LAT was tyrosine
phosphorylated and shown to associate in vivo with a number of other
tyrosine phosphorylated proteins including PLC -1, Grb-2, and
SLP-76. Using Jurkat cell lines deficient in ZAP70/Syk (P116) or LAT
(ANJ3) expression, CD2-dependent PLC-1 and SLP-76 tyrosine
phosphorylation required expression both of ZAP70 or Syk and of LAT. As
predicted, the absence of either LAT or ZAP70/Syk kinases
correlated with a defect in the induction of nuclear factor of
activated T cells (NFAT) transcriptional activity, activation of the
interleukin-2 promoter, and ERK phosphorylation following CD2
stimulation. These data suggest that LAT is an adapter protein
important for the regulation of CD2-mediated T-cell activation.
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