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1 Are Required for NF-
B Activation and Lipid Raft Recruitment of Protein Kinase C
Induced by T Cell Costimulation1
Divisions of
* Immunochemistry and
Immunogenetics, German Cancer Research Center (Deutsches Krebsforschungszentrum), Im Neuenheimer Feld, Heidelberg, Germany
The NF-
B activation pathway induced by T cell costimulation uses
various molecules including Vav1 and protein kinase C (PKC)
. Because
Vav1 inducibly associates with further proteins including phospholipase
C (PLC)
1 and Src homology 2 domain-containing leukocyte
phosphoprotein of 76 kDa (SLP-76), we investigated their role for
NF-B activation in Jurkat leukemia T cell lines deficient for
expression of these two proteins. Cells lacking SLP-76 or PLC1
failed to activate NF-B in response to T cell costimulation. In
contrast, replenishment of SLP-76 or PLC1 expression restored
CD3/CD28-induced IB kinase (IKK) activity as well as NF-B DNA
binding and transactivation. PKC activated NF-B in SLP-76- and
PLC1-deficient cells, showing that PKC is acting further
downstream. In contrast, Vav1-induced NF-B activation was normal in
SLP-76- cells, but absent in PLC1- cells.
CD3/CD28-stimulated recruitment of PKC and IKK to lipid rafts was
lost in SLP-76- or PLC1-negative cells, while translocation of Vav1
remained unaffected. Accordingly, recruitment of PKC to the
immunological synapse strictly relied on the presence of SLP-76 and
PLC1, but synapse translocation of Vav1 identified in this study was
independent from both proteins. These results show the importance of
SLP-76 and PLC1 for NF-B activation and raft translocation of
PKC and IKK.
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