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Importantly, NLRC4’s contribution to antimicrobial defense can be cell type–dependent, as studies in human macrophages show robust NLRC4 activation while certain epithelial cells preferentially use alternative pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nStructural and regulatory studies have further refined our understanding of NLRC4 inflammasome assembly. High‐resolution imaging reveals that NLRC4, via its caspase recruitment domain (CARD), polymerizes into defined helical structures that provide a platform for caspase‑1 recruitment. In parallel, NLRC4 expression and activity are modulated by several factors including p53, specific lncRNAs, and regulatory proteins such as PKCδ and HSC70—all of which can alter the kinetics or threshold for downstream caspase activation. These insights underscore that NLRC4 is not a mere on–off switch but a finely tuned sensor whose assembly is governed by both its intrinsic oligomerization properties and extrinsic modulatory signals."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of NLRC4—whether through gain‐of‐function mutations or aberrant activation—can precipitate pathological inflammation across a range of conditions. Genetic alterations that lead to its constitutive activation are linked to autoinflammatory syndromes (including familial cold autoinflammatory syndrome and neonatal enterocolitis), while aberrant NLRC4 activity also contributes to inflammatory damage in metabolic diseases (e.g. diabetic nephropathy) and modulates cancer progression (as seen in breast cancer and glioma). 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