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Thioredoxin-1 functions as a molecular switch regulating the oxidative stress-induced activation of MST1

Authors
Chae, Ji SooHwang, Sang GilLim, Dae-SikChoi, Eui-Ju
Issue Date
15-12월-2012
Publisher
ELSEVIER SCIENCE INC
Keywords
MST1; Reactive oxygen species; Thioredoxin-1; TNF-alpha; Free radicals
Citation
FREE RADICAL BIOLOGY AND MEDICINE, v.53, no.12, pp.2335 - 2343
Indexed
SCIE
SCOPUS
Journal Title
FREE RADICAL BIOLOGY AND MEDICINE
Volume
53
Number
12
Start Page
2335
End Page
2343
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/106659
DOI
10.1016/j.freeradbiomed.2012.10.527
ISSN
0891-5849
Abstract
The mammalian STE20-like kinase-1 (MST1), a multifunctional serine-threonine kinase in mammalian cells, has been recently implicated in the mediation of oxidative stress-induced signaling processes that lead to cell death. However, the molecular mechanism by which oxidative stress induces the stimulation of MST1 remains unclear. In this study, we found that thioredoxin-1 was physically associated with MST1 in intact cells and that this interaction was abolished by H2O2. Thioredoxin-1, by binding to the SARAH domain of MST1, inhibited the homodimerization and autophosphorylation of MST1, thereby preventing its activation. Furthermore, TNF-alpha prevented the physical interaction between thioredoxin-1 and MST1 and promoted the homodimerization and activation of MST1. The effect of TNF-alpha. on MST1 activation was reversed by the reducing agent N-acetyl-L-cysteine. Taken together, our results suggest that thioredoxin-1 functions as a molecular switch to turn off the oxidative stress-induced activation of MST1. (C) 2012 Elsevier Inc. All rights reserved.
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