[HTML][HTML] Phosphorylation of Tyrosine 537 on the Human Estrogen Receptor Is Required for Binding to an Estrogen Response Element (∗)
SF Arnold, DP Vorojeikina, AC Notides - Journal of Biological Chemistry, 1995 - ASBMB
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) localized in the nucleus of …
(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) localized in the nucleus of …