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FEBS Lett 2002, PMID: 12067722

Hepatic amino acid-dependent signaling is under the control of AMP-dependent protein kinase.

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.

Document information provided by NCBI PubMed

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 "

Manually curated Databases

No curated data.