Dissociation of DIABLO:XIAP from the apoptosome complex

Stable Identifier
R-HSA-114440
Type
Reaction [dissociation]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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Dissociation of DIABLO:XIAP from the apoptosome complex
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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

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

Cell 2000
Participants
Input
Output
Participates
as an event of
Inferred From
Dissociation of Caspase-7 from DIABLO:XIAP:Caspase-7 (Homo sapiens)
Authored
Alnemri, E  (2004-02-17)
Reviewed
Matthews, L  (2018-11-05)
Created
Alnemri, E  (2004-02-17)
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