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Literature summary for 3.4.22.63 extracted from

  • van Raam, B.J.; Salvesen, G.S.
    Proliferative versus apoptotic functions of caspase-8 hetero or homo: the caspase-8 dimer controls cell fate (2012), Biochim. Biophys. Acta, 1824, 113-122.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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

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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
no activity in Mus musculus
-
-
-

Posttranslational Modification

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

Source Tissue Comment Organism Textmining
lymphocyte
-
Homo sapiens
-

Subunits

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

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