PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Akt activity and mediates cellular invasion

J Biol Chem. 2004 Apr 16;279(16):16441-51. doi: 10.1074/jbc.M312175200. Epub 2004 Feb 3.

Abstract

Akt/PKB is a crucial regulator of diverse cellular processes and contributes to cancer progression. Activation of Akt is essentially dependent on phosphatidylinositol (PI) 3-kinase signaling. Here, we describe a novel mediator of Akt that is independent of PI 3-kinase. This mediator, PIKE-A, is a PIKE isoform and contains GTPase, pleckstrin homology, ArfGAP, and ankyrin repeats domains. PIKE-A directly binds to activated Akt but not PI 3-kinase in a guanine nucleotide-dependent way and stimulates the kinase activity of Akt. Overexpression of PIKE-A enhances Akt activity and promotes cancer cell invasion, whereas dominant-negative PIKE-A and PIKE-A knockdown markedly inhibit these processes. Our results demonstrate that PIKE-A is a physiologic regulator of Akt and an oncogenic effector of cell invasion.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cell Line, Tumor
  • Enzyme Activation / genetics
  • GTP-Binding Proteins / genetics*
  • GTP-Binding Proteins / physiology
  • GTPase-Activating Proteins / genetics*
  • GTPase-Activating Proteins / physiology
  • Glycogen Debranching Enzyme System / genetics
  • Humans
  • Neoplasm Invasiveness / genetics*
  • Protein Serine-Threonine Kinases / physiology
  • Proto-Oncogene Proteins / physiology
  • Proto-Oncogene Proteins c-akt
  • Signal Transduction

Substances

  • GTPase-Activating Proteins
  • Glycogen Debranching Enzyme System
  • Proto-Oncogene Proteins
  • 4 alpha-glucanotransferase
  • AKT1 protein, human
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt
  • AGAP2 protein, human
  • GTP-Binding Proteins