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. 2022 Feb 10;9:790117. doi: 10.3389/fcell.2021.790117

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Copyright © 2022 Zhuang, Xie and Zheng.

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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Structural features of caspases, Apaf-1, and the Bcl-2 family. (A) Master initiator caspases, caspase-2, caspase-8, and caspase-9, are characterized by N-terminal domain(s) including DED or CARD. The effector caspases have caspase-3, caspase-6, and caspase-7 for apoptosis. Apaf-1 is a main scaffold protein for recruitment of Cyt c and caspase-9. Bcl-2 itself plays anti-apoptotic roles whereas the Bax/Bak members of the Bcl-2 family are pro-apoptotic. BH3-only protein is an intrinsic apoptosis initiator. (B) Another clade contains inflammatory caspases, including human caspase-1, -4, and -5 and mouse caspase-11, have the N-terminal CARD domains.