Switches.ELM

Switch #:

SWTI000527

Switch type:
Binary

Switch subtype:
Physicochemical compatibility

Description:
Binding of the BIR domain-binding motif of Caspase-9 (CASP9) to the BIR domains of Baculoviral IAP repeat-containing protein 4 (XIAP) requires cleavage of Caspase-9 (CASP9) at D315, since this results in a functional neo N-terminal motif. BIR domains are found in Inhibitor of Apoptosis Proteins (IAPs) that suppress the activity of activated caspases, either by directly inhibiting caspase catalytic activity, or by targeting caspases for degradation by ubiquitin modification.

Participants:
(1) Caspase-9 (CASP9)
(2) Baculoviral IAP repeat-containing protein 4 (XIAP)

Interactions

Interaction #1 CASP9 - XIAP

Interfaces
(1) LIG_BIR_III_2 motif (₃₁₅DATPF₃₁₉) in Caspase-9 (CASP9)
(2) Inhibitor of Apoptosis domain_(268-331) in Baculoviral IAP repeat-containing protein 4 (XIAP)

Interaction Regulation
PTM-dependent Induction (Proteolytic cleavage at D₃₁₅ on Caspase-9 (CASP9)) of the Caspase-9 (CASP9) LIG_BIR_III_2 motif - Baculoviral IAP repeat-containing protein 4 (XIAP) Inhibitor of Apoptosis domain interaction

Additional Information
Structural information: 1NW9

Context

Switch localisation
ELM curated: Cytoplasm, cytosol, mitochondrion

Inferred: nucleus

Switch pathways

Inferred: Apoptosis

References

(1) Mechanism of XIAP-mediated inhibition of caspase-9.
Shiozaki et al. Mol. Cell (2003)