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Publication : Control of the pericentrosomal H2O2 level by peroxiredoxin I is critical for mitotic progression.

First Author  Lim JM Year  2015
Journal  J Cell Biol Volume  210
Issue  1 Pages  23-33
PubMed ID  26150388 Mgi Jnum  J:227306
Mgi Id  MGI:5700135 Doi  10.1083/jcb.201412068
Citation  Lim JM, et al. (2015) Control of the pericentrosomal H2O2 level by peroxiredoxin I is critical for mitotic progression. J Cell Biol 210(1):23-33
abstractText  Proteins associated with the centrosome play key roles in mitotic progression in mammalian cells. The activity of Cdk1-opposing phosphatases at the centrosome must be inhibited during early mitosis to prevent premature dephosphorylation of Cdh1-an activator of the ubiquitin ligase anaphase-promoting complex/cyclosome-and the consequent premature degradation of mitotic activators. In this paper, we show that reversible oxidative inactivation of centrosome-bound protein phosphatases such as Cdc14B by H2O2 is likely responsible for this inhibition. The intracellular concentration of H2O2 increases as the cell cycle progresses. Whereas the centrosome is shielded from H2O2 through its association with the H2O2-eliminating enzyme peroxiredoxin I (PrxI) during interphase, the centrosome-associated PrxI is selectively inactivated through phosphorylation by Cdk1 during early mitosis, thereby exposing the centrosome to H2O2 and facilitating inactivation of centrosome-bound phosphatases. Dephosphorylation of PrxI by okadaic acid-sensitive phosphatases during late mitosis again shields the centrosome from H2O2 and thereby allows the reactivation of Cdk1-opposing phosphatases at the organelle.
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