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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / pharmacology
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Amino Acid Sequence
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Binding Sites
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Enzyme Activation
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Mitogen-Activated Protein Kinase 1
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Molecular Sequence Data
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Mutation / physiology
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Phosphorylation
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Protein Binding / drug effects
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Protein Serine-Threonine Kinases / genetics
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Protein Serine-Threonine Kinases / metabolism*
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Protein-Tyrosine Kinases / genetics
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Protein-Tyrosine Kinases / metabolism*
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Proto-Oncogene Proteins c-myc / chemistry
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Proto-Oncogene Proteins c-myc / metabolism*
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Recombinant Fusion Proteins / metabolism
Substances
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Proto-Oncogene Proteins c-myc
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Recombinant Fusion Proteins
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Adenosine Triphosphate
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Protein-Tyrosine Kinases
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Protein Serine-Threonine Kinases
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Mitogen-Activated Protein Kinase 1