| First Author | Kil IS | Year | 2015 |
| Journal | Mol Cell | Volume | 59 |
| Issue | 4 | Pages | 651-63 |
| PubMed ID | 26236015 | Mgi Jnum | J:226098 |
| Mgi Id | MGI:5695788 | Doi | 10.1016/j.molcel.2015.06.031 |
| Citation | Kil IS, et al. (2015) Circadian Oscillation of Sulfiredoxin in the Mitochondria. Mol Cell 59(4):651-63 |
| abstractText | Hydrogen peroxide (H2O2) released from mitochondria regulates various cell signaling pathways. Given that H2O2-eliminating enzymes such as peroxiredoxin III (PrxIII) are abundant in mitochondria, however, it has remained unknown how such release can occur. Active PrxIII-SH undergoes reversible inactivation via hyperoxidation to PrxIII-SO2, which is then reduced by sulfiredoxin. We now show that the amounts of PrxIII-SO2 and sulfiredoxin undergo antiphasic circadian oscillation in the mitochondria of specific tissues of mice maintained under normal conditions. Cytosolic sulfiredoxin was found to be imported into the mitochondria via a mechanism that requires formation of a disulfide-linked complex with heat shock protein 90, which is promoted by H2O2 released from mitochondria. The imported sulfiredoxin is degraded by Lon in a manner dependent on PrxIII hyperoxidation state. The coordinated import and degradation of sulfiredoxin provide the basis for sulfiredoxin oscillation and consequent PrxIII-SO2 oscillation in mitochondria and likely result in an oscillatory H2O2 release. |
