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#cellbiology #apoptosis #cancer Caspase activation during apoptosis. An initiator caspase contains a protease domain in its carboxy-terminal region and a small protein interaction domain near its amino terminus. It is initially made in an inactive, monomeric form, sometimes called procaspase. Apoptotic signals trigger the assembly of adaptor proteins carrying multiple binding sites for the caspase amino-terminal domain. Upon binding to the adaptor proteins, the initiator caspases dimerize and are thereby activated, leading to cleavage of a specific site in their protease domains. Each protease domain is then rearranged into a large and small subunit. In some cases (not shown), the adaptor-binding domain of the initiator caspase is also cleaved (see Figure 18–5). Executioner caspases are initially formed as inactive dimers. Upon cleavage at a site in the protease domain by an initiator caspase, the executioner caspase dimer undergoes an activating conformational change. The executioner caspases then cleave a variety of key proteins, leading to the controlled death of the cell.