Figure: The non-canonical inflammasome mediated by Casp11 upon lipopolysaccharide-binding (Mouse)¶
This figure illustrates the non-canonical inflammasome pathway mediated by Casp11 (Casp4) in response to bacterial lipopolysaccharide (LPS). When bacterial LPS (lipid A) enters the cytosol, it binds to Casp4, activating its cysteine-type endopeptidase activity. Activated Casp4 then cleaves Gasdermin D (GSDMD), resulting in its maturation into an active form. Cleaved GSDMD binds to phosphatidylinositol-4,5-bisphosphate (PIP2) in the plasma membrane, forming wide pores that lead to pyroptotic cell death. Concurrently, Casp4 signals to NLRP3, which promotes inflammasome complex assembly, contributing to the overall defense response to bacterial infection.
Feedback from AI on figure:
{"feedback":"The diagram effectively illustrates the non-canonical inflammasome pathway mediated by Casp11/Casp4 in response to bacterial lipopolysaccharide. The pathway is presented in a clear, logical flow from LPS binding to downstream effects including pyroptosis and inflammasome complex formation. The use of color coding with a comprehensive legend helps distinguish different components of the pathway. Text labels are appropriately sized and positioned to ensure readability. The inclusion of cellular compartments (cytosol, plasma membrane) provides important spatial context for the molecular events. The figure maintains scientific accuracy while presenting the information in a visually appealing format suitable for publication in high-impact journals.","necessary_changes":null,"optional_changes":null}