A novel EID-1 family member, EID-2, associates with histone deacetylases and inhibits muscle differentiation.
An EID-1 (E1A-like inhibitor of differentiation-1) inhibits differentiation by blocking the histone acetyltransferase activity of p300. Here we report a novel inhibitor of differentiation exhibiting homology to EID-1, termed EID-2 (EID-1-like inhibitor of differentiation-2). EID-2 inhibited MyoD-dependent transcription and muscle differentiation. Unlike EID-1, EID-2 did not block p300 activity. Interestingly, ... EID-2 associated with class I histone deacetylases (HDACs). The N-terminal portion of EID-2 was required for the binding to HDACs. This region was also involved in the transcriptional repression and nuclear localization, suggesting the importance of the involvement of HDACs in the EID-2 function. These results indicate a new family of differentiation inhibitors, although there are several differences in the biochemical mechanisms between EID-2 and EID-1.
Mesh Terms:
Adenovirus E1A Proteins, Amino Acid Sequence, Animals, Carrier Proteins, Cell Differentiation, Cell Line, Cloning, Molecular, Gene Expression Regulation, Histone Deacetylases, Humans, Intracellular Signaling Peptides and Proteins, Mice, Molecular Sequence Data, Muscle Cells, Nuclear Proteins, Repressor Proteins
Adenovirus E1A Proteins, Amino Acid Sequence, Animals, Carrier Proteins, Cell Differentiation, Cell Line, Cloning, Molecular, Gene Expression Regulation, Histone Deacetylases, Humans, Intracellular Signaling Peptides and Proteins, Mice, Molecular Sequence Data, Muscle Cells, Nuclear Proteins, Repressor Proteins
J. Biol. Chem.
Date: May. 09, 2003
PubMed ID: 12586827
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