Caspase-2 is resistant to inhibition by inhibitor of apoptosis proteins (IAPs) and can activate caspase-7.
Caspases are a family of cysteine proteases with roles in cytokine maturation or apoptosis. Caspase-2 was the first pro-apoptotic caspase identified, but its functions in apoptotic signal transduction are still being elucidated. This study examined the regulation of the activity of caspase-2 using recombinant proteins and a yeast-based system. Our data suggest that for human caspase-2 to be active its large and small subunits must be separated. For maximal activity its prodomain must also be removed. Consistent with its proposed identity as an upstream caspase, caspase-2 could provoke the activation of caspase-7. Caspase-2 was not subject to inhibition by members of the IAP family of apoptosis inhibitors.
Ho
Po-Ki
PK
Murdoch Children's Research Institute, Parkville, Australia.
Jabbour
Anissa M
AM
Ekert
Paul G
PG
Hawkins
Christine J
CJ
D000818:Animals; D017209:Apoptosis / Q000502:physiology*; D053143:Caspase 2; D053179:Caspase 7; D061945:Caspase Inhibitors; D020169:Caspases / Q000378:metabolism*; D004789:Enzyme Activation; D051034:Inhibitor of Apoptosis Proteins; D008322:Mammals; D011506:Proteins / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction
D061945:Caspase Inhibitors; D051034:Inhibitor of Apoptosis Proteins; D011506:Proteins; D011994:Recombinant Proteins; C505520:CASP7 protein, human; D053143:Caspase 2; D053179:Caspase 7; D020169:Caspases