A novel EID family member, EID-3, inhibits differentiation and forms a homodimer or heterodimer with EID-2.
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.
Mesh Terms:
Acetyltransferases, Amino Acid Sequence, Animals, Carrier Proteins, Cell Differentiation, Cell Line, Tumor, Cell Nucleus, Cloning, Molecular, Dimerization, Histone Acetyltransferases, Mice, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Sequence Homology, Amino Acid
Acetyltransferases, Amino Acid Sequence, Animals, Carrier Proteins, Cell Differentiation, Cell Line, Tumor, Cell Nucleus, Cloning, Molecular, Dimerization, Histone Acetyltransferases, Mice, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Sequence Homology, Amino Acid
Biochem. Biophys. Res. Commun.
Date: Aug. 05, 2005
PubMed ID: 15970276
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