Myristoylation is an integral part of apoptosis, or programmed cell death. Apoptosis is necessary for cell homeostasis and occurs when cells are under stress such as hypoxia or DNA damage. Apoptosis can proceed by either mitochondrial or receptor mediated activation. In receptor mediated apoptosis, apoptotic pathways are triggered when the cell binds a death receptor. In one such case, death receptor binding initiates the formation of the death-inducing signaling complex, a complex composed of numerous proteins including several caspases, including caspase 3. Caspase 3 cleaves a number of proteins that are subsequently myristoylated by NMT. The pro-apoptotic BH3-interacting domain death agonist (Bid) is one such protein that once myristoylated, translocates to the mitochondria where it prompts the release of cytochrome c leading to cell death.  Actin, gelsolin and p21-activated kinase 2 PAK2 are three other proteins that are myristoylated following cleavage by caspase 3, which leads to either the up-regulation or down-regulation of apoptosis.