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

@article{Gupta1994MAPKB,
  title={MAP kinase binds to the NH2‐terminal activation domain of c‐Myc},
  author={S. Gupta and R. Davis},
  journal={FEBS Letters},
  year={1994},
  volume={353}
}
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. 
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References

SHOWING 1-10 OF 38 REFERENCES
Cell cycle regulation of the c-Myc transcriptional activation domain.
  • 71
  • PDF
Signal transduction within the nucleus by mitogen-activated protein kinase.
  • 295
ERKs, extracellular signal-regulated MAP-2 kinases.
  • 133
...
1
2
3
4
...