3.4.22.55 additional information DNA damage induced by gamma-radiation triggers the phosphorylation of nuclear caspase-2 at S122 site within the prodomain leading to its cleavage and activation 711715, 711820 3.4.22.55 phosphoprotein - 731596 3.4.22.55 phosphoprotein calcium/calmodulin regulated protein kinase II phosphorylates caspase-2 at Ser-135 732592 3.4.22.55 phosphoprotein phosphorylation at Ser-340 732220 3.4.22.55 phosphoprotein regulatory phosphorylations of (pro)caspase-2 713566 3.4.22.55 proteolytic modification caspase-2 processing occurs in goniothalamin-treated Jurkat cells, cleavage to its active subunit (33 kDa) occurs as early as 3 h 713545 3.4.22.55 proteolytic modification caspase-2 undergoes autocatalytic activation to remove the prodomain and linker region to generate a stable dimer consisting of the large subunit p19 and the small subunit p12. This p19/p12 dimer self-associates to form the active caspase-2, forming a dimer, a tetramer, or a dimer-of-dimers 717846 3.4.22.55 proteolytic modification pattern of caspase-2 processing differs between its autocatalytic and caspase-8-mediated cleavage 713152 3.4.22.55 proteolytic modification PIDD (p53-induced protein with a death domain [DD]), together with the bipartite adapter protein RAIDD (receptor-interacting protein-associated ICH-1/CED-3 homologous protein with a DD), is implicated in the activation of pro–caspase-2 in a high molecular weight complex called the PIDDosome during apoptosis induction after DNA damage. Processing of caspase-2 is readily detected in the absence of PIDDosome formation in primary lymphocytes 712540 3.4.22.55 proteolytic modification the activation site of the caspase is DQQD-/- (P4,P3,P2,P1) 647429 3.4.22.55 proteolytic modification the enzyme is activated during apoptosis by a caspase-3 (CPP32)-like protease. When cells are induced to undergo apoptosis, endogenous caspase-2 is first cleaved into three fragments of 32000-33000 Da and 14000 Da, which are then further processed into 18000 Da and 12000 Da active subunits 647763 3.4.22.55 proteolytic modification the initial activation of caspase 2 seems to be mediated by dimerization not processing, this generates a partially active enzyme that is further activated by autoprocessing (self cleavage). Additional processing, which is presumably mediated by active effector caspases (caspases 3 and 7) results in the generation of caspase 2 p19 and p12 subunits. Given that caspase 2 can be processed by caspases 3 and 7, and that loss or inhibition of these caspases or their upstream activators (caspase 9 and APAF1) leads to an inhibition of caspase 2 cleavage 713092 3.4.22.55 proteolytic modification the topoisomerase-II inhibitor etoposide induces processing of procaspase-2 717457 3.4.22.55 sumoylation - 711697