RRC ID 36189
Author Nomura W, Inoue Y.
Title Methylglyoxal activates the target of rapamycin complex 2-protein kinase C signaling pathway in Saccharomyces cerevisiae.
Journal Mol Cell Biol
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.
Volume 35(7)
Pages 1269-80
Published 2015-4-1
DOI 10.1128/MCB.01118-14
PII MCB.01118-14
PMID 25624345
PMC PMC4355542
MeSH Enzyme Activation* Mechanistic Target of Rapamycin Complex 2 Mitogen-Activated Protein Kinases / metabolism Multiprotein Complexes / metabolism* Phosphorylation Protein Kinase C / metabolism Pyruvaldehyde / metabolism* Saccharomyces cerevisiae / cytology Saccharomyces cerevisiae / enzymology* Saccharomyces cerevisiae / metabolism* Saccharomyces cerevisiae Proteins / metabolism Signal Transduction* TOR Serine-Threonine Kinases / metabolism*
IF 3.611
Times Cited 24
WOS Category BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY
Resource
Yeast YOC2573? BY21271 BY21276 BY21272 BY21270 BY21238 ?