Structural and biophysical characterization of the interactions between calmodulin and the pleckstrin homology domain of Akt

Academic Article

Abstract

  • © 2015 by The American Society for Biochemistry and Molecular Biology, Inc. 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.
  • Published In

    Digital Object Identifier (doi)

    Author List

  • Agamasu C; Ghanam RH; Saad JS
  • Start Page

  • 27403
  • End Page

  • 27413
  • Volume

  • 290
  • Issue

  • 45