Erythropoietin induces the tyrosine phosphorylation, nuclear translocation, and DNA binding of STAT1 and STAT5 in erythroid cells.

@article{Penta1995ErythropoietinIT,
  title={Erythropoietin induces the tyrosine phosphorylation, nuclear translocation, and DNA binding of STAT1 and STAT5 in erythroid cells.},
  author={Kalyani Penta and Stephen T. Sawyer},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 52},
  pages={31282-7}
}
We have investigated whether Signal Transducing and Activators of Transcription (STAT) proteins become activated following the binding of erythropoietin (EPO) to immature erythroid cells from the spleens of mice infected with the anemia strain of Friend virus. STAT1 and STAT5 proteins are phosphorylated and translocated to the nucleus in EPO-treated cells. STAT1 and STAT5 DNA binding activities were also activated in an EPO-dependent manner. The presence of these STAT proteins in the DNA… CONTINUE READING