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

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.
Yuka Sasajima 1,  Hiroyuki Tanaka,  Satoshi Miyake,  Yasuhito Yuasa
Affiliations

Affiliation

  • 1 Department of Molecular Oncology, Graduate School of Medicine and Dentistry, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8519, Japan.
PMID: 15970276 DOI: 10.1016/j.bbrc.2005.06.013
Abstract

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.

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