Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element.

@article{Arnold1995PhosphorylationOT,
  title={Phosphorylation of tyrosine 537 on the human estrogen receptor is required for binding to an estrogen response element.},
  author={Stevan F Arnold and Daria P Vorojeikina and A C Notides},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 50},
  pages={30205-12}
}
We report here that the phosphorylation of tyrosine 537 on the human estrogen receptor (hER) controls the receptor's dimerization and DNA binding ability. The DNA-binding form of both the hER from human MCF-7 mammary carcinoma cells and the hER overexpressed in Sf9 insect cells was isolated using estrogen response element (ERE) affinity chromatography. Western blot analyses demonstrated that the DNA-binding form of the hER from MCF-7 or Sf9 cells was (i) phosphorylated at tyrosine 537, (ii… CONTINUE READING
31 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 31 extracted citations

Similar Papers

Loading similar papers…