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- Title
Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery.
- Authors
Phalen, Timothy J; Weirather, Kelly; Deming, Paula B; Anathy, Vikas; Howe, Alan K; van der Vliet, Albert; Jönsson, Thomas J; Poole, Leslie B; Heintz, Nicholas H
- Abstract
Inactivation of eukaryotic 2-Cys peroxiredoxins (Prxs) by hyperoxidation has been proposed to promote accumulation of hydrogen peroxide (H2O2) for redox-dependent signaling events. We examined the oxidation and oligomeric states of PrxI and -II in epithelial cells during mitogenic signaling and in response to fluxes of H2O2. During normal mitogenic signaling, hyperoxidation of PrxI and -II was not detected. In contrast, H2O2-dependent cell cycle arrest was correlated with hyperoxidation of PrxII, which resulted in quantitative recruitment of approximately 66- and approximately 140-kD PrxII complexes into large filamentous oligomers. Expression of cyclin D1 and cell proliferation did not resume until PrxII-SO2H was reduced and native PrxII complexes were regenerated. Ectopic expression of PrxI or -II increased Prx-SO2H levels in response to oxidant exposure and failed to protect cells from arrest. We propose a model in which Prxs function as peroxide dosimeters in subcellular processes that involve redox cycling, with hyperoxidation controlling structural transitions that alert cells of perturbations in peroxide homeostasis.
- Publication
The Journal of cell biology, 2006, Vol 175, Issue 5, p779
- ISSN
0021-9525
- Publication type
Journal Article
- DOI
10.1083/jcb.200606005