Caspase-2 is a member of cysteine aspartate protease family that generally involved in stress-induced apoptosis recruited in large protein complex in which the molecular composition remains inexplicable.
Caspase-2 activation occurs in intricate that contains death domain containing protein whose expression induced by p53 and the adaptor protein RAIDD. It acts both aspositive and negative cell death effectors depending on cell lineage and stage development.
Caspase-2 shares substrates specificity that has no visible activity in its monomeric form regardless of its cleavage position while retains up to 20% of enzymes activity on its dimeric form, once the dimerized caspase go through, these enzymes become fully active wherein dimerization is the initiating step in caspase-2 activation.
Caspase-2 is restricted all over the cell but more intense in Golgi apparatus and nucleus which is activated in the cytosol in response to different stress including heat shock, DNA damage and cytoskeletal disruption as painstaking by molecular fluorescence complementation. In the nucleus caspase-2 function independently of its enzymatic activity which response to conditions that do not usually result in apoptosis.
Gene name: CASP2
Protein name: Caspase-2