MAP kinase binds to the NH2-terminal activation domain of c-Myc

FEBS Lett. 1994 Oct 24;353(3):281-5. doi: 10.1016/0014-5793(94)01052-8.


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

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphate / pharmacology
  • Amino Acid Sequence
  • Binding Sites
  • Enzyme Activation
  • Mitogen-Activated Protein Kinase 1
  • Molecular Sequence Data
  • Mutation / physiology
  • Phosphorylation
  • Protein Binding / drug effects
  • Protein-Serine-Threonine Kinases / genetics
  • Protein-Serine-Threonine Kinases / metabolism*
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism*
  • Proto-Oncogene Proteins c-myc / chemistry
  • Proto-Oncogene Proteins c-myc / metabolism*
  • Recombinant Fusion Proteins / metabolism


  • Proto-Oncogene Proteins c-myc
  • Recombinant Fusion Proteins
  • Adenosine Triphosphate
  • Protein-Tyrosine Kinases
  • Protein-Serine-Threonine Kinases
  • Mitogen-Activated Protein Kinase 1