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<p>Caspases (CASPs) are vital regulators of apoptosis and pyroptosis. Apoptotic caspases are classified into the initiator and effector caspases, the former activating the latter to execute apoptosis. Pyroptosis is executed by gasdermins, which are activated by caspase cleavage to release the N-terminal (NT) pyroptotic domain. To date, except for four effector-like caspases from jellyfish <i>Aurelia coerulea</i> (AcCCaspA/B and AcCaspA/B), knowledge is limited about the caspases or gasdermin in jellyfish. By using gene cloning, phylogenetic analysis, transfection, microscopy, and immunoblotting, we identified and characterized an <i>A. coerulea</i> initiator caspase, AcCCaspC, and an <i>A. coerulea</i> gasdermin (AcGSDME). Results show that AcCCaspC was phylogenetically close to mammalian CASP9 and possessed the conserved CASc and CARD motifs. AcCCaspC was unable to cause apoptosis, but specifically cleaved AcCCaspA to induce apoptosis. AcCCaspC was in turn cleaved by AcCCaspA to remove the CARD. Although AcCCaspC could not cleave AcGSDME, AcCCaspA/B cleaved AcGSDME to release the NT domain, it lacked pyroptotic activity. These results indicate that AcCCaspC acts as a key initiator caspase, by which both apoptosis and GSDME can be regulated in a manner that is feedback regulated by its substrate caspase.</p>

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Characterization of jellyfish (Aurelia coerulea) caspases: reciprocal regulations and their effects on apoptosis activation and GSDME cleavage

  • 期刊论文

  • 发表日期：

    2026年6月29日

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  • Yuan Chen,
  • Hang Xu,
  • Li Sun

摘要

Caspases (CASPs) are vital regulators of apoptosis and pyroptosis. Apoptotic caspases are classified into the initiator and effector caspases, the former activating the latter to execute apoptosis. Pyroptosis is executed by gasdermins, which are activated by caspase cleavage to release the N-terminal (NT) pyroptotic domain. To date, except for four effector-like caspases from jellyfish Aurelia coerulea (AcCCaspA/B and AcCaspA/B), knowledge is limited about the caspases or gasdermin in jellyfish. By using gene cloning, phylogenetic analysis, transfection, microscopy, and immunoblotting, we identified and characterized an A. coerulea initiator caspase, AcCCaspC, and an A. coerulea gasdermin (AcGSDME). Results show that AcCCaspC was phylogenetically close to mammalian CASP9 and possessed the conserved CASc and CARD motifs. AcCCaspC was unable to cause apoptosis, but specifically cleaved AcCCaspA to induce apoptosis. AcCCaspC was in turn cleaved by AcCCaspA to remove the CARD. Although AcCCaspC could not cleave AcGSDME, AcCCaspA/B cleaved AcGSDME to release the NT domain, it lacked pyroptotic activity. These results indicate that AcCCaspC acts as a key initiator caspase, by which both apoptosis and GSDME can be regulated in a manner that is feedback regulated by its substrate caspase.