Inactivation of peroxiredoxin I by phosphorylation allows localized H2O2 accumulation for cell signaling

Cited 493 time in scopus
Metadata Downloads
Title
Inactivation of peroxiredoxin I by phosphorylation allows localized H2O2 accumulation for cell signaling
Author(s)
H A Woo; S H Yim; D H Shin; D Kang; Dae Yeul Yu; S G Rhee
Bibliographic Citation
Cell, vol. 140, no. 4, pp. 517-528
Publication Year
2010
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.
Keyword
PROTEINSSIGNALING
ISSN
0092-8674
Publisher
Elsevier-Cell Press
DOI
http://dx.doi.org/10.1016/j.cell.2010.01.009
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.