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Title: Methylglyoxal activates the target of rapamycin complex 2-protein kinase C signaling pathway in Saccharomyces cerevisiae.
Authors: Nomura, Wataru  kyouindb  KAKEN_id
Inoue, Yoshiharu  kyouindb  KAKEN_id
Author's alias: 井上, 善晴
Issue Date: Apr-2015
Publisher: American Society for Microbiology
Journal title: Molecular and cellular biology
Volume: 35
Issue: 7
Start page: 1269
End page: 1280
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 Thr(1125) and Ser(1143). Methylglyoxal enhanced the phosphorylation of Pkc1 at Ser(1143), which transmitted the signal to the downstream Mpk1 MAP kinase cascade. We found that the phosphorylation status of Pkc1(T1125) affected the phosphorylation of Pkc1 at Ser(1143), in addition to its protein levels. Methylglyoxal activated mammalian TORC2 signaling, which, in turn, phosphorylated Akt at Ser(473). Our results suggest that methylglyoxal is a conserved initiator of TORC2 signaling among eukaryotes.
Rights: Copyright © American Society for Microbiology, Mol Cell Biol 35:1269–1280. doi:10.1128/MCB.01118-14
DOI(Published Version): 10.1128/MCB.01118-14
PubMed ID: 25624345
Appears in Collections:Journal Articles

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