Regulation of Akt/PKB Ser473 phosphorylation.
For years the Akt/PKB research field has been in turmoil, trying to understand how the activating phosphorylation of Akt/PKB at Ser473 is regulated. In the past month, papers in a recent issue of Molecular Cell (Gao et al., 2005) and in Science (Sarbassov et al., 2005) may have identified the phosphatase and kinase acting on this residue.
Bayascas
Jose R
JR
School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland.
Alessi
Dario R
DR
D000135:Acid Phosphatase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004789:Enzyme Activation; D015971:Gene Expression Regulation, Enzymologic; D008954:Models, Biological; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011518:Proto-Oncogene Proteins / Q000235:genetics / Q000378:metabolism*; D051057:Proto-Oncogene Proteins c-akt; D012694:Serine / Q000378:metabolism*
D011518:Proto-Oncogene Proteins; D012694:Serine; D017346:Protein Serine-Threonine Kinases; D051057:Proto-Oncogene Proteins c-akt; D000135:Acid Phosphatase