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Rawat SJ , Creasy CL , Peterson JR , Chernoff J
The tumor suppressor mst1 promotes changes in the cellular redox state by phosphorylation and inactivation of peroxiredoxin-1 protein
J Biol Chem. 2013 Mar 22;288(12) :8762-71
PMID: 23386615    PMCID: PMC3605693   
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Abstract
The serine/threonine protein kinases Mst1 and Mst2 can be activated by cellular stressors including hydrogen peroxide. Using two independent protein interaction screens, we show that these kinases associate, in an oxidation-dependent manner, with Prdx1, an enzyme that regulates the cellular redox state by reducing hydrogen peroxide to water and oxygen. Mst1 inactivates Prdx1 by phosphorylating it at Thr-90 and Thr-183, leading to accumulation of hydrogen peroxide in cells. These results suggest that hydrogen peroxide-stimulated Mst1 activates a positive feedback loop to sustain an oxidizing cellular state.
Notes
Rawat, Sonali Jalan Creasy, Caretha L Peterson, Jeffrey R Chernoff, Jonathan United States J Biol Chem. 2013 Mar 22;288(12):8762-71. doi: 10.1074/jbc.M112.414524. Epub 2013 Feb 5.