DIABLO promotes apoptosis by removing MIHA/XIAP from processed caspase 9
PG Ekert, J Silke, CJ Hawkins, AM Verhagen… - The Journal of cell …, 2001 - rupress.org
MIHA is an inhibitor of apoptosis protein (IAP) that can inhibit cell death by direct interaction
with caspases, the effector proteases of apoptosis. DIABLO is a mammalian protein that can
bind to IAPs and antagonize their antiapoptotic effect, a function analogous to that of the
proapoptotic Drosophila molecules, Grim, Reaper, and HID. Here, we show that after UV
radiation, MIHA prevented apoptosis by inhibiting caspase 9 and caspase 3 activation.
Unlike Bcl-2, MIHA functioned after release of cytochrome c and DIABLO from the …
with caspases, the effector proteases of apoptosis. DIABLO is a mammalian protein that can
bind to IAPs and antagonize their antiapoptotic effect, a function analogous to that of the
proapoptotic Drosophila molecules, Grim, Reaper, and HID. Here, we show that after UV
radiation, MIHA prevented apoptosis by inhibiting caspase 9 and caspase 3 activation.
Unlike Bcl-2, MIHA functioned after release of cytochrome c and DIABLO from the …
MIHA is an inhibitor of apoptosis protein (IAP) that can inhibit cell death by direct interaction with caspases, the effector proteases of apoptosis. DIABLO is a mammalian protein that can bind to IAPs and antagonize their antiapoptotic effect, a function analogous to that of the proapoptotic Drosophila molecules, Grim, Reaper, and HID. Here, we show that after UV radiation, MIHA prevented apoptosis by inhibiting caspase 9 and caspase 3 activation. Unlike Bcl-2, MIHA functioned after release of cytochrome c and DIABLO from the mitochondria and was able to bind to both processed caspase 9 and processed caspase 3 to prevent feedback activation of their zymogen forms. Once released into the cytosol, DIABLO bound to MIHA and disrupted its association with processed caspase 9, thereby allowing caspase 9 to activate caspase 3, resulting in apoptosis.
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