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There is now a CONTENT FREEZE for Mercury while we switch to a new platform. It began on Friday, March 10 at 6pm and will end on Wednesday, March 15 at noon. No new content can be created during this time, but all material in the system as of the beginning of the freeze will be migrated to the new platform, including users and groups. Functionally the new site is identical to the old one. webteam@gatech.edu
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Dr. Amit Reddi, Johns Hopkins University
A New Role for An Old Copper Enzyme in Glucose and Oxygen Sensing
Cu/Zn superoxide dismutase (SOD1) is a highly abundant SOD in eukaryotic cells and is in the frontline of defense against reactive oxygen species (ROS) by catalyzing the disproportionation of superoxide radicals into hydrogen peroxide and oxygen. Using the baker’s yeast (Saccharomyces cerevisiae) as a model organism, we now report a new role for SOD1 in transmitting signals from oxygen and glucose to repress respiration. The mechanism involves SOD1-mediated stabilization of two casein kinase 1-gamma (CK1γ) homologues required for respiratory repression. SOD1 binds a C-terminal degron identified in yeast CK1γ and promotes kinase stability by catalyzing superoxide conversion to peroxide. Our findings suggest that while the bulk of SOD1 is dispensable for antioxidant defense, it is required for metabolic control using signals from superoxide produced during aerobic glycolysis. Thus, in a single circuit, oxygen, glucose, and reactive oxygen can repress respiration through SOD1/ CK1γ signaling.
For more information contact Prof. Pamela Peralta-Yahya at (404-894-4228).
