Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2015 Jul 17;34:30. doi: 10.1186/s40880-015-0030-x

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© Zeng et al. 2015

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

PMC Copyright notice

The apoptotic mechanism of RIPs. RIPs may trigger the death receptor pathway by facilitating the combination of the death ligand and its receptor. Caspase-8 is recruited and activated by death domain proteins such as Fas-associated protein with death domain (FADD). C/EBP homologous protein (CHOP) and immunoglobulin-binding protein (Bip) are increased under RIP-induced endoplasmic reticulum stress, in which activated caspase-4 contributes to capase-8 activation. The release of second mitochondria-derived activator of caspases (Smac) and cytochrome c, which can be increased by Bax or decreased by Bcl-2, is promoted by RIP. Cytochrome c aggregates with apoptotic protease-activating factor 1 (Apaf-1) and becomes an apoptotic body that activates caspase-9, which in turn activates caspase-3 and caspase-8. Activated caspase-3 cleaves poly(ADP-ribose) polymerase (PARP), resulting in DNA fragmentation and apoptosis. Smac protects caspase-3 from inhibitor of apoptosis protein (IAP) inhibition. Caspase-8 cuts Bid into tBid, which is necessary for Bax oligomerization in the mitochondrial outer membrane. The inhibition of tBid insertion into the mitochondrial membrane by Bcl-2 prevents cytochrome c release [31].