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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery.

Inactivation of eukaryotic 2-Cys peroxiredoxins (Prxs) by hyperoxidation has been proposed to promote accumulation of hydrogen peroxide (H(2)O(2)) 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 H(2)O(2). During normal mitogenic signaling, hyperoxidation of PrxI and -II was not detected. In contrast, H(2)O(2)-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-SO(2)H was reduced and native PrxII complexes were regenerated. Ectopic expression of PrxI or -II increased Prx-SO(2)H 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.[1]

References

  1. Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery. Phalen, T.J., Weirather, K., Deming, P.B., Anathy, V., Howe, A.K., van der Vliet, A., J??nsson, T.J., Poole, L.B., Heintz, N.H. J. Cell Biol. (2006) [Pubmed]
 
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