Regulation of Akt/PKB Ser473 Phosphorylation

Mol Cell. 2005 Apr 15;18(2):143-5. doi: 10.1016/j.molcel.2005.03.020.

Abstract

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.

Publication types

  • Comment

MeSH terms

  • Acid Phosphatase / chemistry
  • Acid Phosphatase / genetics
  • Acid Phosphatase / metabolism*
  • Enzyme Activation
  • Gene Expression Regulation, Enzymologic*
  • Models, Biological
  • Phosphorylation
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases / genetics
  • Protein-Serine-Threonine Kinases / metabolism*
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-akt
  • Serine / metabolism*

Substances

  • Proto-Oncogene Proteins
  • Serine
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt
  • Acid Phosphatase