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Biochem Biophys Res Commun. 2013 Nov 8;441(1):191-5. doi: 10.1016/j.bbrc.2013.10.033. Epub 2013 Oct 16.

SIRT5 desuccinylates and activates SOD1 to eliminate ROS.

Author information

1
Department of Thoracic Surgery, Shanghai First People's Hospital, Shanghai Jiaotong University, Shanghai 200080, China.

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.

KEYWORDS:

Antioxidation; Cell growth; ROS; SIRT5; Succinylation

PMID:
24140062
DOI:
10.1016/j.bbrc.2013.10.033
[Indexed for MEDLINE]

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