EID-2, a novel member of the EID family of p300-binding proteins inhibits transactivation by MyoD.

Skeletal muscle differentiation has been shown to be dependent on the expression of Rb and p300. We recently cloned a novel inhibitor of muscle differentiation called EID-1, which interacted with both of these factors. In a database search for related molecules, we have cloned and characterized a new EID-1 family ...
member, EID-2. This 28-kDa protein encodes a 236-amino-acid protein with significant similarity to EID-1 in its C-terminus. EID-2 displays developmentally regulated expression with high levels in adult heart and brain. Overexpression of EID-2 inhibits muscle-specific gene expression through inhibition of MyoD-dependent transcription. This inhibitory effect on gene expression can be explained by EID-2's ability to associate with and inhibit the acetyltransferase activity of p300. These data suggest that EID-1 and -2 represent a novel family of proteins that negatively regulate differentiation through a p300-dependent mechanism.
Mesh Terms:
Acetyltransferases, Actins, Adult, Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, Cell Line, Cell Line, Tumor, Cells, Cultured, Cloning, Molecular, DNA, Complementary, Female, Gene Expression, Histone Acetyltransferases, Humans, Inhibitor of Differentiation Protein 2, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Molecular Weight, Muscle, Skeletal, MyoD Protein, Myosin Heavy Chains, Nuclear Proteins, Protein Binding, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid, Trans-Activators, Transcription, Genetic, Transcriptional Activation
Gene
Date: Oct. 30, 2003
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