2017 September ; 27(9): 673–684. | Stephen B. Kovacs and Edward A. Miao
Pyroptosis is a form of programmed cell death initiated by inflammasomes, which detect cytosolic contamination or perturbation. This triggers the activation of caspase-1 or caspase-11/4/5, leading to the cleavage of gasdermin D. Gasdermin D is composed of an N-terminal pore-forming domain (PFD) and a C-terminal repressor domain (RD). Upon cleavage, the PFD oligomerizes to form large pores in the membrane, causing cell swelling and membrane rupture. Gasdermin D is one of six gasdermin family members, and several other gasdermins have also been shown to form pores that cause pyroptosis after cleavage. Gasdermin E, for example, is activated by caspase-3 cleavage. The review discusses the current understanding of pyroptosis and the gasdermin family, highlighting their roles in defending against intracellular infections and their potential involvement in various diseases.Pyroptosis is a form of programmed cell death initiated by inflammasomes, which detect cytosolic contamination or perturbation. This triggers the activation of caspase-1 or caspase-11/4/5, leading to the cleavage of gasdermin D. Gasdermin D is composed of an N-terminal pore-forming domain (PFD) and a C-terminal repressor domain (RD). Upon cleavage, the PFD oligomerizes to form large pores in the membrane, causing cell swelling and membrane rupture. Gasdermin D is one of six gasdermin family members, and several other gasdermins have also been shown to form pores that cause pyroptosis after cleavage. Gasdermin E, for example, is activated by caspase-3 cleavage. The review discusses the current understanding of pyroptosis and the gasdermin family, highlighting their roles in defending against intracellular infections and their potential involvement in various diseases.