期刊
CELL
卷 152, 期 1-2, 页码 224-235出版社
CELL PRESS
DOI: 10.1016/j.cell.2012.11.046
关键词
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资金
- JHU NIEHS center
- NIH R37 [GM50016]
- NIH NIGMS fellowship [F32 GM 093550]
Cu/Zn superoxide dismutase (SOD1) is an abundant enzyme that has been best studied as a regulator of antioxidant defense. Using the yeast Saccharomyces cerevisiae, we report that SOD1 transmits signals from oxygen and glucose to repress respiration. The mechanism involves SOD1-mediated stabilization of two casein kinase 1-gamma (CK1 gamma) homologs, Yck1p and Yck2p, required for respiratory repression. SOD1 binds a C-terminal degron we identified in Yck1p/Yck2p and promotes kinase stability by catalyzing superoxide conversion to peroxide. The effects of SOD1 on CK1 gamma stability are also observed with mammalian SOD1 and CK1 gamma and in a human cell line. Therefore, in a single circuit, oxygen, glucose, and reactive oxygen can repress respiration through SOD1/CK1 gamma signaling. Our data therefore may provide mechanistic insight into how rapidly proliferating cells and many cancers accomplish glucose-mediated repression of respiration in favor of aerobic glycolysis.
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