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. 2020 Dec 23;8:610022. doi: 10.3389/fcell.2020.610022

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Copyright © 2020 Brown-Suedel and Bouchier-Hayes.

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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BID, Golgin-160, and MDM2 are established caspase-2 substrates. The potential downstream functions of caspase-2-mediated cleavage of these substrates are shown. Cleavage of BID (left panel) promotes permeabilization of the outer mitochondrial membrane, releasing cytochrome c and activating downstream executioner caspases inducing apoptosis. Cleavage of Golgin-160 (center panel) induces Golgi fragmentation during apoptosis. MDM2 cleavage by caspase-2 (right panel) leads to the stabilization of p53 and promotion of cell cycle arrest.