Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis.

Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme.

The proteolytic cleavage of this protein is induced by a variety of apoptotic stimuli.

[8] Together with RAIDD and p53-induced protein with a death domain ([PIDD])(LRDD), caspase 2 has been shown to form the so-called PIDDosome,[9] which may serve as an activation platform for the protease, although it may also be activated in the absence of PIDD.

[11][12] Caspase 2 has been shown to interact with: This article incorporates text from the United States National Library of Medicine, which is in the public domain.