WBP2 Protein, Human (His)

NLRP1 protein acts as the sensor component of the NLRP1 inflammasome, a crucial mediator of inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis. As a recognition receptor, NLRP1 identifies specific pathogens and damage-associated signals, initiating the formation of the inflammasome polymeric complex composed of NLRP1, CASP1, and PYCARD/ASC. Upon pathogen-associated signals, the N-terminal part of NLRP1 is degraded, releasing the cleaved C-terminal part, which polymerizes and associates with PYCARD/ASC. This complex recruits pro-caspase-1, promoting caspase-1 activation and subsequently cleaving and activating inflammatory cytokines IL1B and IL18, along with gasdermin-D (GSDMD), leading to pyroptosis. In the absence of GSDMD, the NLRP1 inflammasome recruits and activates CASP8, leading to gasdermin-E (GSDME) activation. NLRP1 activation is also required for HMGB1 secretion, stimulating inflammatory responses. Recognizing pathogen-associated signals like human rhinoviruses, positive-strand RNA viruses, and muramyl dipeptide, NLRP1 plays a pivotal role in antiviral immunity and inflammation. Additionally, UV-B irradiation induces ribosome collisions, activating NLRP1 through MAP3K20-dependent phosphorylation and leading to pyroptosis. NLRP1 constitutes the precursor of the NLRP1 inflammasome, undergoing autoproteolytic processing within the FIIND domain in response to pathogens and damage-associated signals.