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MAP kinase binds to the NH2-terminal activation domain of c-Myc
1Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01605.
FEBS Letters
|October 24, 1994
Abstract:
The transcription factor c-Myc is a substrate for phosphorylation by MAP kinases. Here we demonstrate that MAP kinase binds to c-Myc. The NH2-terminal region (residues 1-100) is necessary and sufficient for this interaction. Binding to c-Myc is not dependent on the state of MAP kinase activation. However, the c-Myc/MAP kinase complex is disrupted by ATP. Together, these observations indicate that substrate binding interactions contribute to the specificity of phosphorylation by MAP kinases.