MAP kinase binds to the NH2-terminal activation domain of c-Myc.
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.
Mesh Terms:
Adenosine Triphosphate, Amino Acid Sequence, Binding Sites, Enzyme Activation, Mitogen-Activated Protein Kinase 1, Molecular Sequence Data, Mutation, Phosphorylation, Protein Binding, Protein-Serine-Threonine Kinases, Protein-Tyrosine Kinases, Proto-Oncogene Proteins c-myc, Recombinant Fusion Proteins
Adenosine Triphosphate, Amino Acid Sequence, Binding Sites, Enzyme Activation, Mitogen-Activated Protein Kinase 1, Molecular Sequence Data, Mutation, Phosphorylation, Protein Binding, Protein-Serine-Threonine Kinases, Protein-Tyrosine Kinases, Proto-Oncogene Proteins c-myc, Recombinant Fusion Proteins
FEBS Lett.
Date: Oct. 24, 1994
PubMed ID: 7957875
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