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Mediates a Selective T Cell Survival Signal Via Phosphorylation of BAD1
Division of Cell Biology, La Jolla Institute for Allergy and Immunology, San Diego, CA 92121
Protein kinase C (PKC)-activating phorbol esters protect T cells
from Fas-induced apoptosis. However, the mechanism of this protective
effect and the identity of the relevant PKC isoform(s) are poorly
understood. Here, we show that PKC
plays a selective and important
role in this protection. Fas triggering led to a selective
caspase-3-dependent cleavage of the enzyme and proteasome-mediated
degradation and inactivation of its catalytic fragment. These events
preceded the onset of apoptosis. Pharmacological inhibition of PKC
promoted Fas-mediated apoptosis in three different types of T cells.
Conversely, constitutively active PKC (and, to a lesser degree,
PKC
) selectively protected T cells from Fas-induced apoptosis. We
provide evidence that the distant Bcl-2 family member, BAD, is a PKC
substrate, is phosphorylated by TCR stimulation, and can mediate at
least in part the anti-apoptotic effect of
PKC.
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