Death-associated protein kinase 1 (DAPK1) is a positive mediator of apoptosis induced by g-interferon. Activation of DAPK occurs via dephosphorylation of Ser-308 and subsequent association of calcium/calmodulin. DAPK is rapidly dephosphorylated in response to tumor necrosis factor or ceramide and then subsequently degraded via proteasome activity. The decline in DAPK expression is paralleled with increased caspase activity and cell apoptosis. Studies suggest that the apoptosis regulatory activities mediated by DAPK are controlled both by phosphorylation status and protein stability.
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Assignment of DAP1 and DAPK--genes that positively mediate programmed cell death triggered by IFN-gamma--to chromosome regions 5p12.2 and 9q34.1, respectively.
Programmed cell death is often triggered by the interaction of some cytokines with their cell surface receptors. Here, we report that gamma interferon (IFN-gamma) induced in HeLa cells a type of cell death that had cytological characteristics of programmed cell
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