Rapid activation of the interferon-gamma signal transduction pathway by inhibitors of tyrosine phosphatases.

@article{Lamb1994RapidAO,
  title={Rapid activation of the interferon-gamma signal transduction pathway by inhibitors of tyrosine phosphatases.},
  author={Peter Kasim Lamb and J. Haslam and L V Kessler and H. Martin Seidel and Robert B. Stein and Jon Rosen},
  journal={Journal of interferon research},
  year={1994},
  volume={14 6},
  pages={365-73}
}
Induction of gene expression by interferon-gamma involves the activation of a latent cytoplasmic transcription factor, p91, by phosphorylation on a single tyrosyl residue. This phosphorylation triggers dimerization, nuclear translocation, and the binding of p91 to interferon-gamma response elements present in the promoters of induced genes. Phosphorylation of p91 requires the activation of two tyrosine kinases, JAK1 and JAK2, that themselves become phosphorylated on tyrosyl residues shortly… CONTINUE READING

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