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Inactivation of Peroxiredoxin I by Phosphorylation Allows Localized H2O2 Accumulation for Cell Signaling

Title
Inactivation of Peroxiredoxin I by Phosphorylation Allows Localized H2O2 Accumulation for Cell Signaling
Authors
Woo H.A.Yim S.H.Shin D.H.Kang D.Yu D.-Y.Rhee S.G.
Ewha Authors
이서구신동해임선희강동민우현애
SCOPUS Author ID
이서구scopusscopus; 신동해scopus; 강동민scopus; 우현애scopus
Issue Date
2010
Journal Title
Cell
ISSN
0092-8674JCR Link
Citation
vol. 140, no. 4, pp. 517 - 528
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Despite its toxicity, H2O2 is produced as a signaling molecule that oxidizes critical cysteine residues of effectors such as protein tyrosine phosphatases in response to activation of cell surface receptors. It has remained unclear, however, how H2O2 concentrations above the threshold required to modify effectors are achieved in the presence of the abundant detoxification enzymes peroxiredoxin (Prx) I and II. We now show that PrxI associated with membranes is transiently phosphorylated on tyrosine-194 and thereby inactivated both in cells stimulated via growth factor or immune receptors in vitro and in those at the margin of healing cutaneous wounds in mice. The localized inactivation of PrxI allows for the transient accumulation of H2O2 around membranes, where signaling components are concentrated, while preventing the toxic accumulation of H2O2 elsewhere. In contrast, PrxII was inactivated not by phosphorylation but rather by hyperoxidation of its catalytic cysteine during sustained oxidative stress. © 2010 Elsevier Inc. All rights reserved.
DOI
10.1016/j.cell.2010.01.009
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일반대학원 > 생명·약학부 > Journal papers
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