RIPK3 is cleaved by CASP8

Stable Identifier
R-HSA-9686930
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Caspase-8 (CASP8) in human and rodent cells facilitates the cleavage of receptor-interacting protein kinases RIPK1 and RIPK3 and prevents RIPK1/RIPK3-dependent regulated necrosis (Lin Y et al. 1999; Hopkins-Donaldson S et al. 2000). These cleavage sites are identified to be Asp324 in RIPK1 and Asp328 in RIPK3 in humans (Lin Y et al. 1999; Feng S et al. 2007). The lack of CASP8 proteolytic activity in the presence of viral (e.g. CrmA and vICA) or pharmacological caspase inhibitors results in necroptosis induction via RIPK1 and RIPK3 (Tewari M & Dixit VM 1995; Fliss PM & Brune W 2012; Hopkins-Donaldson S et al. 2000).
Literature References
PubMed ID Title Journal Year
17644308 Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain

Ma, L, Castanares, M, Yang, Y, Hoti, N, Wu, M, Mei, Y, Feng, S, Zhu, DE

Cell. Signal. 2007
Participants
Participates
Catalyst Activity

cysteine-type endopeptidase activity of active caspase-8 [cytosol]

Orthologous Events
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