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. 2022 Jul 9;30(2):227–236. doi: 10.1038/s41418-022-01038-4

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© The Author(s) 2022

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — A Upon activation by DAP-type peptidoglycan, Imd and dFadd are recruited to the PGRP-LC receptor. Dredd binds to dFadd, is activated, and cleaves Imd. B Cleavage of Imd enables recruitment of Diap2 that also interacts directly with Dredd. Diap2 catalyses the formation of K63-linked ubiquitin chains on Dredd and Imd. C The K63-linked chains on Imd are thought to recruit the dTak1/dTab2 complex, and the chains on Dredd might function as a scaffold for additional proteins or protein complexes needed for downstream signalling. Ubiquitination of Dredd is, in addition, needed for proteolytic processing and nuclear translocation of Relish.