Caspase-9 exists as a pro-form (mw ~46 kDa) that is cleaved by the activity of Apaf-1 in the presence of cytosolic cytochrome c (Apaf-2) and dATP. The processing of pro-caspase-9 into a heterodimer consisting of a 35kDa and a 10 kDa chain activates the protease and induces the cascade leading to cleavage of caspase-3 and other apoptotic targets. The processing of caspase-9 may be blocked by the activity of bcl-x which physically interacts with the caspase-/Apaf-1 complex.
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