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and NF-
B Activation in Response to Engagement of CD3 and CD28
,
,
*
Laboratory of Biological Chemistry, Gerontology Research Center, National Institute on Aging, National Institutes of Health, Baltimore, MD 21224;
Department of Cellular Injury, Walter Reed Army Institute of Research, Washington, DC 20307; and
Department of Medicine, Uniform Services University of the Health Sciences, Bethesda, MD 20814
The transcription factor NF-
B is a critical regulator of T cell
function that becomes strongly activated in response to coengagement of
TCR and CD28. Although events immediately proximal to NF-B
activation are well understood, uncertainty remains over which upstream
signaling pathways engaged by TCR and CD28 lead to NF-B activation.
By using Jurkat T cell lines that are deficient or replete for either
the protein tyrosine kinase ZAP-70 or the cytosolic adapter molecule
SLP-76, the role of these proteins in modulating NF-B activation was
examined. NF-B was not activated in response to coengagement of TCR
and CD28 in either the ZAP-70- or SLP-76-negative cells, whereas
stimuli that bypass these receptors (PMA plus A23187, or TNF-
)
activated NF-B normally. Protein kinase C (PKC) 
activation,
which is required for NF-B activation, also was defective in these
cells. Reexpression of ZAP-70 restored PKC and NF-B activation in
response to TCR and CD28 coengagement. p95vav
(Vav)-1 tyrosine phosphorylation was largely unperturbed in the
ZAP-70-negative cells; however, receptor-stimulated SLP-76/Vav-1
coassociation was greatly reduced. Wild-type SLP-76 fully restored
PKC and NF-B activation in the SLP-76-negative cells, whereas
3YF-SLP-76, which lacks the sites of tyrosine phosphorylation required
for Vav-1 binding, only partially rescued signaling. These data
illustrate the importance of the ZAP-70/SLP-76 signaling pathway in
CD3/CD28-stimulated activation of PKC and NF-B, and suggest that
Vav-1 association with SLP-76 may be important in this
pathway.
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