| Synonyms |
Caspase recruitment domain-containing protein 7, Death effector filament-forming ced-4-like apoptosis protein, Nucleotide-binding domain and caspase recruitment domain | CARD7, DEFCAP, KIAA0926, NAC, NALP1 |
| Function |
As the sensor component of the NLRP1 inflammasome, plays a crucial role in innate immunity and inflammation. Inflammasomes are supramolecular complexe ...
View Mores that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. In response to pathogens and other damage-associated signals, initiates the formation of the inflammasome polymeric complex, made of NLRP1, CASP1, and possibly PYCARD. Recruitment of proCASP1 to the inflammasome promotes its activation and CASP1-catalyzed IL1B and IL18 maturation and secretion in the extracellular milieu (PubMed:33093214). Activation of NLRP1 inflammasome is also required for HMGB1 secretion. The active cytokines and HMGB1 stimulate inflammatory responses. Inflammasomes can also induce pyroptosis, an inflammatory form of programmed cell death (PubMed:22665479, PubMed:17418785). May be activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, in a NOD2-dependent manner (PubMed:18511561). Binds ATP and shows ATPase activity (PubMed:11113115, PubMed:15212762, PubMed:33243852). Plays an important role in antiviral immunity and inflammation in the human airway epithelium. Upon infection by human rhinoviruses 14 and 16 (HRV-14 and HRV-16), NLRP1 is cleaved and activated which triggers NLRP1-dependent inflammasome activation and IL18 secretion (PubMed:33093214). Contrary to its mouse ortholog, not activated by Bacillus anthracis lethal toxin (PubMed:19651869). Acts as a direct sensor for long dsRNA and thus RNA virus infection (PubMed:33243852). Positive-strand RNA viruses such as Semliki forest virus and long dsRNA activate the NLRP1 inflammasome, triggering IL1B release in a NLRP1-dependent fashion (PubMed:33243852).
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3.0
NLRP1
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binding