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Phosphorylation and regulation of Raf by Akt (protein kinase B).
Journal article

Phosphorylation and regulation of Raf by Akt (protein kinase B).

  • Zimmermann S Institute of Medical Virology, University of Zurich, Gloriastrasse 30/32, CH-8028 Zurich, Switzerland.
  • Moelling K
  • 1999-11-27
Published in:
  • Science (New York, N.Y.). - 1999
Cell Division
Cell Line
Chromones
Cyclin-Dependent Kinase Inhibitor p21
Cyclins
Enzyme Activation
Enzyme Inhibitors
Epidermal Growth Factor
Flavonoids
Humans
MAP Kinase Signaling System
Morpholines
Phosphatidylinositol 3-Kinases
Phosphoinositide-3 Kinase Inhibitors
Phosphorylation
Phosphoserine
Protein-Serine-Threonine Kinases
Proto-Oncogene Proteins
Proto-Oncogene Proteins c-akt
Proto-Oncogene Proteins c-raf
Recombinant Fusion Proteins
Signal Transduction
Somatomedins
Tetradecanoylphorbol Acetate
Tumor Cells, Cultured
ras Proteins
English Activation of the protein kinase Raf can lead to opposing cellular responses such as proliferation, growth arrest, apoptosis, or differentiation. Akt (protein kinase B), a member of a different signaling pathway that also regulates these responses, interacted with Raf and phosphorylated this protein at a highly conserved serine residue in its regulatory domain in vivo. This phosphorylation of Raf by Akt inhibited activation of the Raf-MEK-ERK signaling pathway and shifted the cellular response in a human breast cancer cell line from cell cycle arrest to proliferation. These observations provide a molecular basis for cross talk between two signaling pathways at the level of Raf and Akt.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/218956
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