EC Number   |
General Information |
Reference |
|---|
   3.4.22.63 | evolution |
human caspase-10 and caspase-8, EC 3.4.22.61, are highly homologous in their protein sequence, 46% identical in the catalytic domain, and their genes are on the same region of human chromosome 2q33-34 suggesting that they have a common ancestor |
717252 |
| 3.4.22.63 | 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 |
717282 |
| 3.4.22.63 | malfunction |
addition of a caspase-10 inhibitor totally blocks PTK7-knockdown-induced apoptosis |
718261 |
| 3.4.22.63 | malfunction |
apoptosis is totally prevented when caspase-10 is specifically inhibited in the cells |
732406 |
| 3.4.22.63 | malfunction |
caspase-10 silencing in neuroblastoma is cell-type related. Downregulation of individual or all caspase-10 isoforms in SH-EP cells does not affect TRAIL sensitivity |
717459 |
| 3.4.22.63 | malfunction |
mutations or deficiencies in caspase-10 are associated with autoimmune lymphoproliferative syndrome |
717282 |
| 3.4.22.63 | metabolism |
apoptosis is a form of programmed cell death that requires members of a family of aspartate-specific cysteine proteases, called caspases, to both initiate and execute the apoptotic phenotype |
717252 |
| 3.4.22.63 | more |
autophagy is associated to human caspase-10-induced cell death in yeast, a specific process that depends on an intact MAPK pathway, the Factor-arrest (Far) protein family, and the autophagy machinery, overview. Far11 coordinates a death-promoting signal and regulates both autophagy and the DNA damage response. The expression of human caspase-10 in Saccharomyces cerevisiae activates an intracellular death signal that depends on the Far protein complex. Expression of initiator caspase-10 is toxic in yeast and induces a lethal phenotype with most of the principal hallmarks of apoptosis and autophagy, which include the production of ROS, chromatin condensation, phosphatidylserine externalization, and increased vacuolization. The MAP kinases Fus3, Kss1, and Slt2 are activated after the expression of caspase-10 in yeast cells |
732065 |
| 3.4.22.63 | more |
isozymes caspase-10B and -10A/B are protected from CHX-mediated degradation by lactacystin treatment |
717459 |
| 3.4.22.63 | more |
residue D297 is essential for autocleavage, while even though the sequence surrounding D319 is compatible for cleavage by caspase-10, its location close to the compact core makes it unavailable for cleavage |
717252 |
