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Fig. 1 | Journal of Hematology & Oncology

Fig. 1

From: Inflammasome inhibitors: promising therapeutic approaches against cancer

Fig. 1

Structures of the NLRP1, NLRP3, NLRC4, and AIM2 inflammasomes. NLRP1 interacts with ASC and caspase-1 via an N-terminal PYD and binds caspase-5 to the complex via the C-terminal CARD. Muramyl dipeptide, Bacillus anthracis lethal toxin, and Toxoplasma gondii induce the activation of the NLRP1 inflammasome. NLRP3 interacts with ASC through an N-terminal PYD domain, which recruits caspase-1. NLRP3 is activated by the recognition of mtDNA and cardiolipin. The NLRC4 inflammasome is activated by the NAIP family, and it can recruit caspase-1 directly via its CARD in an ASC-independent manner. However, it remains unclear how ASC interacts with the NLRC4 inflammasome complex. The AIM2 inflammasome recruits ASC and caspase-1 through its N-terminal PYD domain and is activated by direct binding with dsDNA via its HIN domain

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