Activation of procaspase-9 by Apaf-1 in the cytochrome c/dATP-dependent pathway requires proteolytic cleavage to generate the mature caspase molecule. Deletion of the Apaf-1 WD-40 repeats makes Apaf-1 constitutively active and capable of processing procaspase-9 independent of cytochrome c an dATP. Apaf-1-mediated processing of procaspase-9 occurs at Asp-315 by an intrinsic autocatalytic activity of procaspase-9 itself. Apaf-1 can form oligomers and may facilitate procaspase-9 autoactivation by oligomerizing its precursor molecules. Once activated, caspase-9 can initiate a caspase cascade involving the downstream executioners caspase-3, -6, and -7.
25 kDa caspase-9 dominant negative protein; APAF-3; apoptosis-related cysteine protease; apoptotic protease activating factor 3; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; cas9; CASP-9; caspase 9; caspase 9, apoptosis-related cysteine peptidase; Caspase-9; caspase-9 dominant negative form; caspase-9-carboxyl-terminal divergent; ICE-LAP6; ICE-like apoptotic protease 6; protein phosphatase 1, regulatory subunit 56
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