Death and survival from executioner caspase activation

Executioner caspases are evolutionarily conserved regulators of cell death under apoptotic stress. Activated executioner caspases drive apoptotic cell death through cleavage of diverse protein substrates or pyroptotic cell death in the presence of gasdermin E. On the other hand, activation of executioner caspases can also trigger prosurvival and pro-proliferation signals. In recent years, a growing body of studies have demonstrated that cells can survive from executioner caspase activation in response to stress and that the survivors undergo molecular and phenotypic alterations. This review focuses on death and survival from executioner caspase activation, summarizing the role of executioner caspases in apoptotic and pyroptotic cell death and discussing the potential mechanism and consequences of survival from stress-induced executioner caspase activation.

Automated summary

Executioner caspases play a crucial role in regulating cell death under apoptotic stress, driving cell death while also triggering survival and proliferation signals. Recent studies have shown that cells can survive from activation of executioner caspases under stress, leading to molecular and phenotypic alterations in the survivors.