{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nNLRP1 is a critical innate immune sensor that nucleates the assembly of inflammasome complexes to trigger caspase‐1 activation and the processing of proinflammatory cytokines such as interleukin‐1β and interleukin‐18. Structurally, NLRP1 contains an N‐terminal PYRIN domain, a nucleotide‐binding domain, leucine‐rich repeats, and a function‐to‐find (FIIND) domain that autoprocesses to release a CARD‐containing fragment—the active moiety that drives downstream signaling. Widely expressed in immune cells and barrier tissues, NLRP1 thereby plays an essential role in host defense and the initiation of inflammation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nActivation of NLRP1 is tightly regulated by proteolytic events initiated by pathogen‐derived enzymes and danger signals. Cleavage by factors such as anthrax lethal toxin protease and viral proteases—as well as direct sensing of double‐stranded RNA—triggers proteasome‐mediated degradation of its inhibitory N-terminal domains, liberating the active C-terminal fragment. Recent structural and biochemical studies demonstrate that NLRP1 can form distinct oligomeric assemblies (including 2:1 complexes with regulatory proteins like DPP9), which serve as checkpoints to quench low‐level activation and fine-tune inflammasome output."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "17"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in inflammasome assembly, NLRP1 is implicated in a wide spectrum of human diseases. Gain‐of‐function mutations and single nucleotide polymorphisms in NLRP1 are associated with autoimmune and autoinflammatory disorders—including vitiligo, Addison’s disease, rheumatoid arthritis, systemic lupus erythematosus, psoriasis, and systemic sclerosis—highlighting its contribution to immune homeostasis. In the nervous system, aberrant NLRP1 activation has been linked to neuroinflammatory processes observed in Alzheimer’s disease, stroke, and even epilepsy. In peripheral tissues, it modulates keratinocyte responses to environmental insults, contributes to gastrointestinal inflammation and tumorigenesis, and mediates innate immune responses to pathogens such as Toxoplasma gondii, HIV, and other microbes. Together, these observations underscore NLRP1’s dual roles in both protective host defense and pathological inflammation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "42"}]}, {"type": "t", "text": ""}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nEmerging work further reveals that NLRP1 also functions as a direct sensor of viral enzymatic activities in epithelial and pulmonary tissues. 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