Background: Akt translocation to the plasma membrane (PM) is modulated by calmodulin (CaM). Results: CaM forms a tight complex with the PHD of Akt, which represents a novel class of CaM-binding domains. Conclusion: The binding mode of CaM to Akt(PHD) suggests a synergistic role in membrane binding and subsequent activation. Significance: Characterization of Akt-CaM is critical for understanding Akt activation.
