2012
DOI: 10.1016/j.molcel.2011.11.027
|View full text |Cite
|
Sign up to set email alerts
|

Inactivation of a Peroxiredoxin by Hydrogen Peroxide Is Critical for Thioredoxin-Mediated Repair of Oxidized Proteins and Cell Survival

Abstract: Eukaryotic 2-Cys peroxiredoxins (Prx) are abundant antioxidant enzymes whose thioredoxin peroxidase activity plays an important role in protecting against oxidative stress, aging, and cancer. Paradoxically, this thioredoxin peroxidase activity is highly sensitive to inactivation by peroxide-induced Prx hyperoxidation. However, any possible advantage in preventing Prx from removing peroxides under oxidative stress conditions has remained obscure. Here we demonstrate that, in cells treated with hydrogen peroxide… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

11
191
0
3

Year Published

2012
2012
2021
2021

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 188 publications
(205 citation statements)
references
References 40 publications
(78 reference statements)
11
191
0
3
Order By: Relevance
“…Interestingly, the 2-Cys Prx pool did not go through major redox state changes as the ACHT1 pool did during illumination of dark-adapted plants. These findings, which are reminiscent of the Yap1 oxidative sensing pathway (Delaunay et al, 2002) or of the Trx-Prx Tpx1 pathway in Schizosaccharomyces pombe (Day et al, 2012) and not of the circadian rhythmic biomarker 2-Cys Prxs , indicate that ACHT1 redox state changes are used for regulation. Conceivably, the additional proteins trapped in intermolecular disulfide complexes with ACHT1 ( Figure 4) could be ACHT1 targets regulated by ACHT1 redox state.…”
Section: Discussionmentioning
confidence: 93%
“…Interestingly, the 2-Cys Prx pool did not go through major redox state changes as the ACHT1 pool did during illumination of dark-adapted plants. These findings, which are reminiscent of the Yap1 oxidative sensing pathway (Delaunay et al, 2002) or of the Trx-Prx Tpx1 pathway in Schizosaccharomyces pombe (Day et al, 2012) and not of the circadian rhythmic biomarker 2-Cys Prxs , indicate that ACHT1 redox state changes are used for regulation. Conceivably, the additional proteins trapped in intermolecular disulfide complexes with ACHT1 ( Figure 4) could be ACHT1 targets regulated by ACHT1 redox state.…”
Section: Discussionmentioning
confidence: 93%
“…In particular, HP induces the formation of a transient disulphide complex between Tpx1 (Cys-48) and Sty1 (Cys-35) (Figure 4) (Veal et al, 2004). Additional redoxsensitive cysteine(s) present in the Sty1 protein or the reduced form of the thioredoxin Trx1 could further control the activation of Sty1 downstream of the SAPK pathway (Day et al, 2012;Veal et al, 2004).…”
Section: Activation Of Sty1 Results In Redirection Of Gene Expressionmentioning
confidence: 99%
“…However, a number of these isoforms can be inactivated, mediated by the oxidation of the catalytic site Cys to Cys‐sulfinic acid (SO 2 H) by high levels of H 2 O 2 . PRXs that have formed SO 2 H acids can be reduced by sulfiredoxin, and it has been proposed that this initial inactivation by its substrate plays a cellular signalling role by a ‘floodgate mechanism’ 148. It is particularly interesting that there are a number of protein families and isoforms within those families that have either peroxidase activity (GPXs, PRXs and CAT) or regulatory proteins that are sensitive to oxidation (Keap1, aconitase and PTP1B).…”
Section: Regulatory Reactive Oxygen and Nitrogen Species Enzymes Exprmentioning
confidence: 99%