Size of inflammasome as a regulatory motif in caspase-1 activation

In immune networks, inflammasomes play a pivotal role in transmitting and regulating danger signals. These supramolecular, multimeric inflammasomes provide binding sites for a key protease, caspase-1, leading to its proximity-induced dimerization. Dimerized caspase-1 is capable of undergoing two stages of activation. In different activation stages, caspase-1 shows preference to triggering inflammation and cell suicide respectively. However, the presence of an unidentified regulatory motif likely governs continuous caspase-1 activation and serves to limit excessive inflammation. Recent advances in cryogenic electron microscopy have yielded high-resolution images, revealing that the number of reaction sites on inflammasomes varies with the inflammasome's size. In our study, we employ stochastic simulation models to explore the regulatory role of the number of activation sites for caspase-1. Further research is necessary to confirm whether inflammasome size indeed exhibits a preference for one caspase-1 stage over another. Such a preference may shed light on a cell decision-making mechanism guiding cell fate.