SIRT5 desuccinylates and activates SOD1 to eliminate ROS.
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Lin ZF, Xu HB, Wang JY, Lin Q, Ruan Z, Liu FB, Jin W, Huang HH, Chen X
SIRT5 desuccinylates and activates SOD1 to eliminate ROS.
Biochem Biophys Res Commun. 2013 Nov 8;441(1):191-5. doi: 10.1016/j.bbrc.2013.10.033. Epub 2013 Oct 16.
- PubMed ID
- 24140062 [ View in PubMed]
- Abstract
Cu/Zn superoxide dismutase (SOD1) is a key antioxidant enzyme. Deficiency of SOD1 is associated with various human diseases, including cancer. Here, we report that SOD1 is succinylated and that succinylation decreases its activity. SIRT5 binds to, desuccinylates and activates SOD1. SOD1-mediated ROS reduction is increased when SIRT5 is co-expressed. Furthermore, mutation of the SOD1 succinylation site inhibits the growth of lung tumor cells. These results reveal a novel post-translational regulation of SOD1 by means of succinylation and SIRT5-dependent desuccinylation, which is important for the growth of lung tumor cells.