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

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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. 1 — A Based on their described function, caspases are divided into inflammatory and apoptotic caspases. The apoptotic caspases are further subdivided into initiator and effector caspases. Caspases contain a small (S) and a large (L) subunit that together form the protease domain. In addition, inflammatory and apoptotic initiator caspases contain an N-terminal long prodomain harbouring DED or CARD domains, whereas apoptotic effector have short prodomains lacking specific protein domains. B Drosophila melanogaster carries three initiator caspases: Dredd, Dronc and Strica. In contrast to Dredd and Dronc, the atypical initiator caspase Strica does not contain DED or CARD domains, but harbours instead a Ser/Thr rich prodomain. In addition to the initiator caspases, Drosophila carries four effector caspases, Drice, Dcp-1, Decay and Damm. The length of the caspases in amino acids are indicated to the right of the proteins.