Site-specific Disruption of the Oct4/Sox2 Protein Interaction Reveals Coordinated Mesendodermal Differentiation and the Epithelial-Mesenchymal Transition

J Biol Chem. 2016 Aug 26;291(35):18353-69. doi: 10.1074/jbc.M116.745414. Epub 2016 Jul 1.

Abstract

Although the Oct4/Sox2 complex is crucial for maintaining the pluripotency of stem cells, the molecular basis underlying its regulation during lineage-specific differentiation remains unknown. Here, we revealed that the highly conserved Oct4/Lys-156 is important for maintaining the stability of the Oct4 protein and the intermolecular salt bridge between Oct4/Lys-151 and Sox2/Asp-107 that contributes to the Oct4/Sox2 interaction. Post-translational modifications at Lys-156 and K156N, a somatic mutation detected in bladder cancer patients, both impaired the Lys-151-Asp-107 salt bridge and the Oct4/Sox2 interaction. When produced as a recombinant protein or overexpressed in pluripotent stem cells, Oct4/K156N, with reduced binding to Sox2, significantly down-regulated the stemness genes that are cooperatively controlled by the Oct4/Sox2 complex and specifically up-regulated the mesendodermal genes and the SNAIL family genes that promote the epithelial-mesenchymal transition. Thus, we conclude that Oct4/Lys-156-modulated Oct4/Sox2 interaction coordinately controls the epithelial-mesenchymal transition and mesendoderm specification induced by specific differentiation signals.

Keywords: cell signaling; differentiation; epithelial-mesenchymal transition (EMT); pluripotency; post-translational modification (PTM); stem cells; transcription factor; tumor cell biology.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aspartic Acid / genetics
  • Aspartic Acid / metabolism
  • Cell Line
  • Epithelial-Mesenchymal Transition / physiology*
  • Humans
  • Lysine / genetics
  • Lysine / metabolism
  • Mesoderm / cytology
  • Mesoderm / metabolism*
  • Octamer Transcription Factor-3 / genetics
  • Octamer Transcription Factor-3 / metabolism*
  • Pluripotent Stem Cells / cytology
  • Pluripotent Stem Cells / metabolism*
  • Protein Binding
  • SOXB1 Transcription Factors / genetics
  • SOXB1 Transcription Factors / metabolism*

Substances

  • Octamer Transcription Factor-3
  • POU5F1 protein, human
  • SOX2 protein, human
  • SOXB1 Transcription Factors
  • Aspartic Acid
  • Lysine

Associated data

  • PDB/1GT0
  • PDB/1O4X
  • PDB/3L1P