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- W4385798535 abstract "The gasdermin family represents a type of membrane pore-forming proteins. The gasdermin family is extensively characterized as the executioner of pyroptotic cell death in mammals; recent studies suggest that gasdermin-like pore-forming proteins are also present in bacteria and fungi. In humans, gasdermin D (GSDMD) is activated through inter-domain cleavage by caspase-1 in the canonical inflammasome pathway and cytosolic LPS-activated caspase-4 or caspase-5. The cleavage disrupts the autoinhibition of GSDMD and liberates the N-terminal gasdermin-N domain that binds to membrane lipids and forms pores of an inner diameter of ~18 nm on the membrane, responsible for cell pyroptosis. Here, we describe the methods of determining the phospholipid-binding and pore-forming activity of gasdermins in a robust in vitro system. We also introduce a method of specifically detecting the caspase-cleaved form of GSDMD in pyroptotic cells." @default.
- W4385798535 created "2023-08-15" @default.
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- W4385798535 date "2023-01-01" @default.
- W4385798535 modified "2023-09-26" @default.
- W4385798535 title "Determination of Gasdermin Pores" @default.
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- W4385798535 doi "https://doi.org/10.1007/978-1-0716-3350-2_11" @default.
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