Small ubiquitin-like modifier 1 (SUMO1) is a member of the superfamily of ubiquitin-like proteins. Despite its structural similarity with ubiquitin, SUMO1 does not seem to play any role in protein degradation and its precise biological function is poorly understood. During our studies on heat-shock responses, we found that heat-shock stress increased SUMO1 conjugation in a dose-dependent manner. Intriguingly, SUMO1 conjugation resulted in decrease of intracellular ROS generation and protection cells from death under heat-shock stress. We showed that NADPH oxidase 2 (NOX2) is a target protein of sumoylation by SUMO1 using immunoprecipitation and is colocalized with SUMO1 at plasma membrane. Additionally, we demonstrated that the attenuation in intracellular ROS generation resulted from inhibition of NADPH oxidase complex (NOX) activity. These results suggested that SUMO1 plays an important role in modulation of NOX activity required for ROS generation.
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - 8 Jul 2011|
Bibliographical noteFunding Information:
This work was supported through the Center for Cell Signaling Research and Drug Discovery Research (CCSDDR, R15-2006-020 ) at Ewha Womans University from the National Core Research Center (NCRC) program and by WCU project ( R31-2008-000-10010-0 ). J Yun and J Lee were supported by Brain Korea (BK21). H J Kim was supported by RP-Grant 2009 of Ewha Womans University.
- NADPH oxidase complex (NOX)
- Reactive oxygen species (ROS)