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The molecular mechanism and evolutionary divergence of caspase 3/7-regulated gasdermin E activation

Elife. 2024-03; 
Hang Xu, Zihao Yuan, Kunpeng Qin, Shuai Jiang , Li Sun
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Proteins, Expression, Isolation and Analysis Immunoblotting was performed as reported previously (Zhao and Sun, 2022). Briefly, the samples were fractionated in 12% SDS-PAGE (GenScript, Piscataway, NJ). Get A Quote

摘要

Caspase (CASP) is a family of proteases involved in cleavage and activation of gasdermin, the executor of pyroptosis. In humans, CASP3 and CASP7 recognize the same consensus motif DxxD, which is present in gasdermin E (GSDME). However, human GSDME is cleaved by CASP3 but not by CASP7. The underlying mechanism of this observation is unclear. In this study, we identified a pyroptotic pufferfish GSDME that was cleaved by both pufferfish CASP3/7 and human CASP3/7. Domain swapping between pufferfish and human CASP and GSDME showed that the GSDME C-terminus and the CASP7 p10 subunit determined the cleavability of GSDME by CASP7. p10 contains a key residue that governs CASP7 substrate discrimination. This key residue ... More

關(guān)鍵詞

caspase 3; caspase 7; evolution; evolutionary biology; gasdermin E; immunology; inflammation; pufferfish; pyroptosis.
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