Activating Compound | Comment | Organism | Structure |
---|---|---|---|
FLIPL protein | heterodimerization with the long isoform of cFLIP, FLIPL, leads to activation of caspase-10. The heterodimer of caspase-10 with FLIPL still can cleave Bid and induce intrinsic apoptosis | Homo sapiens | |
additional information | caspase-10 is activated at the DISC, downstream of death-receptor signaling | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
V410I | the mutation in caspase-10, that is associated with autoimmune lymphoproliferative syndrome, ALPS, is a common polymorphism in the healthy Danish population | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
no activity in Mus musculus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | caspase-10 is activated at the DISC, downstream of death-receptor signaling. Caspases-8 and -10 are recruited to the DISC as intact monomers and recruitment of the caspases to the DISC subsequently leads to their dimerization and activation through induced proximity, mechanism, overview | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
lymphocyte | - |
Homo sapiens | - |
Subunits | Comment | Organism |
---|---|---|
dimer | caspases can only be active as dimers, since neither the active site dyad nor the substrate pocket can be formed in the monomeric form | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
evolution | initiator and executioner caspases, the pro-apoptotic members of the caspase family are subdivided in the initiators of apoptosis, i.e. caspases-8, -9 and -10 in humans, and the executioners of apoptosis, caspase-3, -6 and -7, phylogenetic tree of all the human caspases, overview. The initiators have a relatively large N-terminal dimerization domain, either a death effector domain, caspases-8 and -10, or a structurally related caspase recruitment domain, caspase-9. Caspase-18 and the ancestor of -8 and -10 called caspase-810 in this schematic are still found in fishes. Later on in evolution, caspase-8 and -10 branched off from caspase-810 | Homo sapiens |
malfunction | mutations or deficiencies in caspase-10 are associated with autoimmune lymphoproliferative syndrome | Homo sapiens |
additional information | the heterodimer of caspase-10 with FLIPL still can cleave Bid and induce intrinsic apoptosis | Homo sapiens |