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. 2023 Jan 18;13:1109938. doi: 10.3389/fimmu.2022.1109938

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Copyright © 2023 Zhan, Li, Xu, Xiao and Bai

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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NLRP3 inflammasome. (A) Domain organization of NLRP3, ASC, and caspase-1. NLRP3 contains an aminoterminal PYRIN (PYD) domain, a nucleotidebinding NACHT domain, and a carboxyterminal leucinerich repeat (LRR) domain. The PYD domain is important for recruitment of ASC; the NACHT domain contains ATPase activity required for NLRP3 conformational change and oligomerization. The LRR domain is important for the formation of the NLRP3 cage, which is required to disperse the trans-Golgi network at the early stage of NLRP3 inflammasome activation. (B) NLRP3 inflammasome assembly. Upon activation, NLRP3 recruits ASC via PYD-PYD interactions and ASC recruits caspase-1 via CARD-CARD interactions.