A novel EID family member, EID-3, inhibits differentiation and forms a homodimer or heterodimer with EID-2

Biochem Biophys Res Commun. 2005 Aug 5;333(3):969-75. doi: 10.1016/j.bbrc.2005.06.013.


The EID family members, i.e., E1A-like inhibitor of differentiation-1 (EID-1) and EID-1-like inhibitor of differentiation-2 (EID-2), were identified as negative regulators of cellular differentiation. EID-1 seems to inhibit differentiation by blocking histone acetyltransferase activity and EID-2 possibly inhibits differentiation through binding to class I histone deacetylases (HDACs). Here, we report a novel inhibitor of differentiation exhibiting homology with EID-2 termed EID-3 (EID-2-like inhibitor of differentiation-3). Like EID-2, EID-3 inhibited MyoD- and GRalpha-dependent transcription and blocked muscle differentiation in cultured cells by binding to class I HDACs. Unlike that of EID-2, the C-terminus, but not the N-terminus, of EID-3 was required for nuclear localization. EID-3 formed a homodimer or heterodimer with EID-2. These results suggest that EID-3 inhibits differentiation by blocking transcription as a complex in cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyltransferases / antagonists & inhibitors
  • Acetyltransferases / metabolism
  • Amino Acid Sequence
  • Animals
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism
  • Carrier Proteins / physiology*
  • Cell Differentiation / physiology*
  • Cell Line, Tumor
  • Cell Nucleus / metabolism
  • Cloning, Molecular
  • Dimerization
  • Histone Acetyltransferases
  • Mice
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry*
  • Protein Binding
  • Sequence Homology, Amino Acid


  • Carrier Proteins
  • EID-2 protein, mouse
  • EID3 protein, human
  • Nuclear Proteins
  • Acetyltransferases
  • Histone Acetyltransferases