Reactome | The NLRP1 inflammasome

The NLRP1 inflammasome

Stable Identifier

R-HSA-844455

Type

Pathway

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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NLRP1 is activated by MDP (Faustin et al. 2007). The NLRP1 inflammasome was the first to be characterized. It was described as a complex containing NALP1, ASC, caspase-1 and caspase-5 (Martinon et al. 2002). Unlike NLRP3, NLRP1 has a C-terminal extension containing a CARD domain, which has been reported to interact directly with procaspase-1, obviating a requirement for ASC (Faustin et al. 2007), though ASC was found to augment the interaction. Mouse NLRP1 has no PYD domain and would therefore not be expected to interact directly with procaspase-1. Like the NLRP3 inflammasome, K+ efflux appears to be essential for caspase-1 activation (Wickliffe et al. 2008). Ribonucleoside triphosphates (NTPs) are required for NALP1-mediated caspase-1 activation with ATP being the most efficient, Mg2+ was also required (Faustin et al. 2007). The human NLRP1 gene has 3 paralogues in mouse that are highly polymorphic. Differences between mouse strains underlie susceptibility to anthrax lethal toxin (Boyden & Dietrich 2006).

Literature References

PubMed ID	Title	Journal	Year
17349957	Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation Lartigue, L, Reed, JC, Rouiller, I, Bruey, JM, Faustin, B, Sergienko, E, Volkmann, N, Luciano, F, Bailly-Maitre, B, Hanein, D	Mol Cell	2007
12191486	The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta Burns, K, Martinon, F, Tschopp, J	Mol Cell	2002