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. 2024 Sep 16;25(10):4153–4167. doi: 10.1038/s44319-024-00260-0

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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(A) Cycling cells typically contain a pair of centrioles, consisting of one daughter and one mature parent centriole decorated with distal appendages (indicated in red). The presence of extra mature centrioles leads to PIDD1 recruitment via ANKRD26 and its activation. The oligomerization of PIDD1, RAIDD and caspase-2 facilitates PIDDosome assembly and activates caspase-2. Caspase-2 cleaves either pro-apoptotic protein BID or MDM2 causing P53 stabilization and subsequent cell cycle arrest or apoptotic cell death. (B) Deubiquitination of PLK4 facilitates phosphorylation of NEK7, which in turn reduces NEK7-NLRP3 inflammasome interaction. NLRP3 release promotes oligomerization of NLRP3, ASC, and pro-caspase-1 into an active NLRP3 inflammasome. The inflammasome activates caspase-1, which in turn cleaves prointerleukin-1β (IL-1β) into its active form causing inflammation. Additionally, Gasdermin D (GSDMD) is cleaved by caspase-1 and forms a transmembrane pore leading to pyroptotic cell death.