Figure: The non-canonical inflammasome mediated by CASP4 upon lipopolysaccharide-binding (Human)ΒΆ
The diagram illustrates the non-canonical inflammasome pathway mediated by CASP4 in human cells. The pathway is initiated when bacterial lipid A binds to cytosolic CASP4, triggering its auto-activation. Active CASP4 then cleaves and activates GSDMD, which translocates to the plasma membrane to form pores. These pores facilitate IL-18 secretion into the extracellular space, promoting inflammatory signaling. The diagram also depicts NLRP3 and PYCARD contributing to inflammasome assembly. Color-coding distinguishes between different proteins and their functional states throughout the pathway.
Feedback from AI on figure:
{"feedback":"This diagram effectively illustrates the non-canonical inflammasome pathway mediated by CASP4 upon lipopolysaccharide binding in a clear, scientifically accurate manner suitable for a high-impact journal publication. The molecular interactions are well-represented with appropriate spatial organization showing cellular compartmentalization between cytosol and extracellular space. The use of consistent color-coding and a comprehensive legend enhances interpretability, while the clear labeling of proteins and processes allows readers to easily follow the signaling cascade from lipid A binding through to IL-18 secretion.","necessary_changes":null,"optional_changes":"For future iterations, considering adding more detailed representation of the membrane pore structure formed by GSDMD and possibly include numerical references to relevant literature sources within the diagram to enhance its academic utility."}