{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNLRP12 (also known as Monarch‑1 or PYPAF7) is a member of the NOD‑like receptor family that functions as a key intracellular regulator of inflammation. At the molecular level, NLRP12 attenuates inflammatory signaling by suppressing both the canonical and non‑canonical NF‑κB pathways. It does so through mechanisms including the promotion of proteasome‑mediated degradation of NF‑κB–inducing kinase and the inhibition of IRAK‑1 hyperphosphorylation. In addition, NLRP12 binds and hydrolyzes ATP via conserved Walker A and B motifs that are critical for its oligomerization and subsequent regulatory functions, while its pyrin domain adopts a classical death domain fold to engage in protein–protein interactions (for example, with molecular chaperones such as Hsp90 and with apoptotic components like FAF‑1). These mechanistic insights, aided by structural studies showing dimerization through disulfide bonds, underpin NLRP12’s role in buffering excessive inflammation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nGenetic and clinical studies have implicated alterations in NLRP12 in a wide spectrum of autoinflammatory and immune‑mediated disorders. Mutations and polymorphisms in NLRP12 are associated with periodic fever syndromes, familial cold autoinflammatory syndrome, and the broader entity designated as NLRP12‑associated autoinflammatory disease. Dysfunctional NLRP12 leads to dysregulated production of pro‑inflammatory cytokines (notably interleukin‑1β), and such defects have been linked with conditions including common variable immunodeficiency, atopic dermatitis, and even mood and vascular disorders. Moreover, NLRP12 influences intestinal homeostasis by modulating host–microbiota interactions and is relevant to the pathogenesis of inflammatory bowel disease and polymyalgia rheumatica. These findings underscore how perturbation in NLRP12 activity can disrupt immune balance and favor chronic inflammatory pathology."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}, {"type": "fg_fs", "start_ref": "9", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its immunomodulatory role, NLRP12 significantly contributes to host defense against pathogens and to tumor suppression. In infectious disease settings, NLRP12 facilitates antimicrobial responses by modulating caspase‑1 activation and interleukin‑1β production during malaria, dengue, and other flavivirus infections, and it interacts with viral components (such as the SARS‑CoV‑2 M protein) to regulate TRAF‑mediated signaling and cytokine release. In cancer, NLRP12 acts as a tumor suppressor by inhibiting key oncogenic pathways—including the Wnt/β‑catenin axis in colorectal cancer and JNK signaling in hepatocellular carcinoma—and its expression levels are emerging as potential prognostic markers in gliomas. Recent discoveries also illustrate how NLRP12 mutations can influence chronic inflammatory conditions such as refractory Crohn’s disease via aberrant ERK/NLRP3/IL‑1β signaling, further highlighting its versatile role in regulating both immunity and cell growth."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "34"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Lin Wang, Gulam A Manji, Jill M Grenier, et al. 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