The EVES motif mediates both intermolecular and intramolecular regulation of c-Myb.

The c-Myb transcription factor is a proto-oncoprotein whose latent transforming activity can be unmasked by truncation of either terminus. Because both ends of Myb are involved in negative regulation, we tested whether they could associate in a two-hybrid assay and identified a carboxy-terminal motif that interacts with the amino-terminal DNA-binding ...
domain. The EVES motif is highly conserved in vertebrate c-Myb proteins and contains a known site of phosphorylation previously implicated in the negative regulation of c-Myb. Interestingly, a related EVES motif is present in p100, a ubiquitously expressed transcriptional coactivator found in diverse species. We show that p100 interacts with and influences the activity of c-Myb, implicating it in the regulation of c-Myb, differentiation, and cell growth. Our results suggest that Myb is regulated by a novel mechanism in which intramolecular interactions and conformational changes control the intermolecular associations among Myb, p100, and the transcriptional apparatus.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Binding, Competitive, Conserved Sequence, DNA-Binding Proteins, Gene Expression Regulation, Neoplastic, Homeostasis, Humans, Molecular Sequence Data, Nuclear Proteins, Phosphorylation, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-myb, Recombinant Proteins, Trans-Activators, Transcription Factors, Transcription, Genetic, Yeasts
Genes Dev.
Date: Aug. 01, 1996
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