AKT refers to the serine/threonine protein kinases, AKT-1, AKT-2 and AKT-3, which are involved in the cellular processes of glucose metabolism, cell proliferation, apoptosis, transcription and cell migration. The peptide Arg-Pro-Arg-Ala-Ala-Thr-Phe may be a relatively specific substrate for PKBα (AKT-1) because, unlike other substrates, it is not phosphorylated by p70 S6 kinase or MAP kinase activated protein (MAPKAP) kinase-1.
Elevated expression of Akt-1 (PKBalpha) has been noted in a significant percentage of primary human breast cancers. Another frequent event in the genesis of human breast cancers is amplification and overexpression of the ErbB-2 receptor tyrosine kinase, an event which
The substrate specificity of protein kinase-B alpha (PKBalpha, also known as RAC kinase or Akt) was investigated using synthetic peptide substrates related to the sequence surrounding the phosphorylation site on glycogen synthase kinase-3 (GSK3). The minimum sequence motif required for
The Journal of biological chemistry, 274(24), 17179-17183 (1999-06-08)
Protein kinase B lies "downstream" of phosphatidylinositide (PtdIns) 3-kinase and is thought to mediate many of the intracellular actions of insulin and other growth factors. Here we show that FKHR, a human homologue of the DAF16 transcription factor in Caenorhabditis
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