RapamycinFungusV1, Main, Exploration, bibRecord, 000C66

Methylglyoxal activates the target of rapamycin complex 2-protein kinase C signaling pathway in Saccharomyces cerevisiae.

Identifieur interne : 000C66 ( Main/Exploration ); précédent : 000C65; suivant : 000C67

Methylglyoxal activates the target of rapamycin complex 2-protein kinase C signaling pathway in Saccharomyces cerevisiae.

Auteurs : Wataru Nomura [Japon] ; Yoshiharu Inoue [Japon]

Source :

Molecular and cellular biology [ 1098-5549 ] ; 2015.

RBID : pubmed:25624345

Descripteurs français

English descriptors

KwdEn :
- Enzyme Activation (MeSH), Mechanistic Target of Rapamycin Complex 2 (MeSH), Mitogen-Activated Protein Kinases (metabolism), Multiprotein Complexes (metabolism), Phosphorylation (MeSH), Protein Kinase C (metabolism), Pyruvaldehyde (metabolism), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), TOR Serine-Threonine Kinases (metabolism).
MESH :
- chemical , metabolism : Mitogen-Activated Protein Kinases, Multiprotein Complexes, Protein Kinase C, Pyruvaldehyde, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases.
- chemical : Mechanistic Target of Rapamycin Complex 2.
- cytology : Saccharomyces cerevisiae.
- enzymology : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Enzyme Activation, Phosphorylation, Signal Transduction.

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.

DOI: 10.1128/MCB.01118-14
PubMed: 25624345
PubMed Central: PMC4355542

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Mitogen-Activated Protein Kinases (métabolisme)</term>
<term>Méthylglyoxal (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">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. </div>
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Methylglyoxal activates the target of rapamycin complex 2-protein kinase C signaling pathway in Saccharomyces cerevisiae.

Methylglyoxal activates the target of rapamycin complex 2-protein kinase C signaling pathway in Saccharomyces cerevisiae.

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