A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur
Intracellular signaling adaptor proteins that contain DEATH EFFECTOR DOMAINS and bind to the cytoplasmic DEATH DOMAIN region found on DEATH DOMAIN RECEPTORS. Many of the proteins in this class take part in intracellular signaling involving TUMOR NECROSIS FACTOR RECEPTORS
