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. 2020 May 15;27(7):2037–2047. doi: 10.1038/s41418-020-0556-6

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© The Author(s), under exclusive licence to ADMC Associazione Differenziamento e Morte Cellulare 2020

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Fig. 1 — a Full-length PIDD1 undergoes autoprocessing at specific residues S446 and S588 (red arrows) to generate two C-terminal fragments with distinct functions, PIDD-C and PIDD-CC. The former has been implicated in NFκB signaling while the latter interacts with the death domain (DD) of RAIDD to form the PIDDosome. The caspase activation and recruitment domain (CARD) of RAIDD interacts with procaspase-2. b The core of the PIDDosome complex is formed by 5:5 PIDD-CC:RAIDD molecules interact via the DDs, and two additional RAIDD entities are placed on top protruding in diametric orientation (based on the protein database structure 2OF5). Binding of RAIDD to procaspase-2 promotes proximity-induced dimerization and autocleavage of caspase-2, critical for its activation.