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.
Zhi-Feng Lin  1 ,  Hong-Bing Xu ,  Jian-Yun Wang ,  Qiang Lin ,  Zhen Ruan ,  Fa-Bing Liu ,  Wang Jin ,  Hai-Hua Huang ,  Xi Chen
Affiliations
  • 1. Department of Thoracic Surgery, Shanghai First People's Hospital, Shanghai Jiaotong University, Shanghai 200080, China.
PMID: 24140062 DOI: 10.1016/j.bbrc.2013.10.033
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.