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Mitochondrial fission controls DNA fragmentation by regulating endonuclease G.

Authors: Li, J  Zhou, J  Li, Y  Qin, D  Li, P 
Citation: Li J, etal., Free Radic Biol Med. 2010 Aug 15;49(4):622-31. doi: 10.1016/j.freeradbiomed.2010.05.021. Epub 2010 Jun 1.
Pubmed: (View Article at PubMed) PMID:20594982
DOI: Full-text: DOI:10.1016/j.freeradbiomed.2010.05.021

Mitochondria constantly undergo fusion and fission that are necessary for the maintenance of organelle fidelity. However, growing evidence has shown that abnormal mitochondrial fusion and fission participate in the regulation of apoptosis. Mitochondrial fusion is able to inhibit apoptosis, whereas mitochondrial fission is involved in the initiation of apoptosis. It remains elusive as to whether mitochondrial fission can regulate DNA fragmentation during apoptosis. Mitochondrial fission is triggered by dynamin-related protein-1 (Drp1), whereas mitofusin 1 (Mfn 1) is able to induce mitochondrial fusion. Here, we report that Drp1 is required for the release of endonuclease G from mitochondria. Knockdown of Drp1 can attenuate DNA fragmentation. Our data further show that Mfn 1 prevents endonuclease G release from mitochondria and the consequent DNA fragmentation. Intriguingly, Mfn 1 could inhibit the activation of caspase-3 and caspase-9, which are necessary for endonuclease G translocation to the nucleus. Our results provide novel evidence that DNA fragmentation is regulated by the mitochondrial fission machinery.


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CRRD Object Information
CRRD ID: 9685387
Created: 2015-01-06
Species: All species
Last Modified: 2015-01-06
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.