FEBS Lett 2002,
Dubbelhuis, Peter F; Meijer, Alfred J
It has become increasingly clear in recent years that amino acids can stimulate a signal transduction pathway resulting in the phosphorylation of mammalian target of rapamycin downstream targets. We have now found that amino acid-dependent phosphorylation of p70S6 kinase and of S6 in hepatocytes is prevented when AMP-dependent protein kinase (AMPK) is activated by either the purine ribonucleoside analogue AICAriboside, fructose or glycerol. Insulin-dependent phosphorylation of protein kinase B is not affected by AMPK activation. Protein synthesis is strongly inhibited when AMPK is activated. It is concluded that amino acid-dependent signaling, a protein-anabolic signal, can be effectively antagonized by activation of AMPK.
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Text Mining Data
protein kinase B → Insulin: " Insulin
dependent phosphorylation of protein kinase B
is not affected by AMPK activation "
protein kinase B — AMPK: " Insulin dependent phosphorylation of protein kinase B is not affected by AMPK activation "
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