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- W2169128412 abstract "Methylglyoxal is a typical 2-oxoaldehyde derived from glycolysis. We show here that methylglyoxal activates the Pkc1-Mpk1 mitogen-activated protein (MAP) kinase cascade in a target of rapamycin complex 2 (TORC2)-dependent manner in the budding yeast Saccharomyces cerevisiae. We demonstrate that TORC2 phosphorylates Pkc1 at Thr1125 and Ser1143. Methylglyoxal enhanced the phosphorylation of Pkc1 at Ser1143, which transmitted the signal to the downstream Mpk1 MAP kinase cascade. We found that the phosphorylation status of Pkc1T1125 affected the phosphorylation of Pkc1 at Ser1143, in addition to its protein levels. Methylglyoxal activated mammalian TORC2 signaling, which, in turn, phosphorylated Akt at Ser473. Our results suggest that methylglyoxal is a conserved initiator of TORC2 signaling among eukaryotes." @default.
- W2169128412 created "2016-06-24" @default.
- W2169128412 creator A5007715914 @default.
- W2169128412 creator A5054627899 @default.
- W2169128412 date "2015-04-01" @default.
- W2169128412 modified "2023-10-11" @default.
- W2169128412 title "Methylglyoxal Activates the Target of Rapamycin Complex 2-Protein Kinase C Signaling Pathway in <i>Saccharomyces cerevisiae</i>" @default.
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- W2169128412 doi "https://doi.org/10.1128/mcb.01118-14" @default.
- W2169128412 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4355542" @default.
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