[HTML][HTML] Control of death-associated protein kinase (DAPK) activity by phosphorylation and proteasomal degradation
Y Jin, EK Blue, PJ Gallagher - Journal of biological chemistry, 2006 - ASBMB
Activation of death-associated protein kinase (DAPK) occurs via dephosphorylation of Ser-
308 and subsequent association of calcium/calmodulin. In this study, we confirmed the
existence of the alternatively spliced human DAPK-β, and we examined the levels of DAPK
autophosphorylation and DAPK catalytic activity in response to tumor necrosis factor or
ceramide. It was found that DAPK is rapidly dephosphorylated in response to tumor necrosis
factor or ceramide and then subsequently degraded via proteasome activity …
308 and subsequent association of calcium/calmodulin. In this study, we confirmed the
existence of the alternatively spliced human DAPK-β, and we examined the levels of DAPK
autophosphorylation and DAPK catalytic activity in response to tumor necrosis factor or
ceramide. It was found that DAPK is rapidly dephosphorylated in response to tumor necrosis
factor or ceramide and then subsequently degraded via proteasome activity …