Dissociation of DIABLO:XIAP from the apoptosome complex

Stable Identifier
Reaction [dissociation]
Homo sapiens
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X linked inhibitor of apoptosis protein (XIAP) associates with the active caspase 9 (CASP9) within APAF1 apoptosome complex. Binding of DIABLO (SMAC) to XIAP promotes the release of caspase-9 from XIAP (Du et al. 2000). XIAP consists of three baculoviral IAP repeat (BIR) domains and a COOH terminal RING domain (Duckett CS et al. 1996). The BIR3 region binds to the amino terminus of the linker peptide on the small subunit of CASP9, which becomes exposed after proteolytic processing of procaspase 9 at Asp315 (Srinivasula SM et al. 2001). SMAC (DIABLO) competes with CASP9 for binding to BIR3 domain of XIAP promoting the release of XIAP from the CASP9:apoptosome complex (Du et al. 2000; Srinivasula SM et al. 2001).

Literature References
PubMed ID Title Journal Year
10929711 Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition

Du, C, Fang, M, Li, Y, Li, L, Wang, X

Cell 2000
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