Insulin regulates the activity of forkhead transcription factor Hnf-3beta/Foxa-2 by Akt-mediated phosphorylation and nuclear/cytosolic localization

Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11624-9. doi: 10.1073/pnas.1931483100. Epub 2003 Sep 19.

Abstract

Hepatocyte nuclear factors 3 alpha, beta, and gamma (Foxa-1, -2, and -3) are transcriptional activators of important metabolic genes in the liver that are suppressed by the actions of insulin. Here, we show that the activation of phosphatidylinositol 3-kinase-Akt by insulin induces Foxa-2 phosphorylation, nuclear exclusion, and inhibition of Foxa-2-dependent transcriptional activity. Foxa-2 physically interacts with Akt, a key mediator of the phosphatidylinositol 3-kinase pathway and is phosphorylated at a single conserved site (T156) that is absent in Foxa-1 and Foxa-3 proteins. This Akt phosphorylation site in Foxa-2 is highly conserved from mammals to insects. Mutant Foxa-2T156A is resistant to Akt-mediated phosphorylation, nuclear exclusion, and transcriptional inactivation of Foxa-2-regulated gene expression. These results implicate an evolutionarily conserved mechanism in the regulation of Foxa-2-dependent transcriptional control by extracellular signals such as insulin.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Cell Line
  • Cell Nucleus / enzymology
  • Cell Nucleus / metabolism*
  • Cytosol / enzymology
  • Cytosol / metabolism*
  • DNA-Binding Proteins / metabolism
  • DNA-Binding Proteins / physiology*
  • Enzyme Activation
  • Hepatocyte Nuclear Factor 3-beta
  • Humans
  • Insulin / physiology*
  • Molecular Sequence Data
  • Nuclear Proteins / metabolism
  • Nuclear Proteins / physiology*
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphorylation
  • Protein Serine-Threonine Kinases*
  • Protein Transport
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-akt
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Transcription Factors*
  • Transcription, Genetic / physiology

Substances

  • DNA-Binding Proteins
  • FOXA2 protein, human
  • Insulin
  • Nuclear Proteins
  • Proto-Oncogene Proteins
  • Recombinant Proteins
  • Transcription Factors
  • Hepatocyte Nuclear Factor 3-beta
  • AKT1 protein, human
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-akt