Related Experiment Video

Updated: Jul 5, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
09:07

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

Switching of chromatin-remodelling complexes for oestrogen receptor-alpha

Maiko Okada1, Shin-ichiro Takezawa, Yoshihiro Mezaki

  • 1The Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.

EMBO Reports
|May 3, 2008
PubMed

Insights

Oestrogen

Area of Science:

  • Endocrinology and Molecular Biology

Background:

  • Oestrogen (estrogen) is a key hormone regulating cell growth and differentiation via nuclear oestrogen receptors (ERs).
  • Ligand-dependent ER transactivation relies on nuclear co-regulator complexes, but their cell-cycle dynamics are unclear.

Purpose of the Study:

  • To investigate the cell-cycle dependency of ERalpha transactivation and its association with co-regulator complexes.

Main Methods:

  • Utilized a cell synchronization system to analyze ERalpha function across the cell cycle.
  • Employed biochemical approaches to identify ERalpha-associated protein complexes.

Main Results:

  • ERalpha transactivation function is reduced during the G2/M phase of the cell cycle.
  • ERalpha interacts with distinct ATP-dependent chromatin-remodelling complexes in a cell-cycle-specific manner.
  • NuRD complex components act as G2/M-phase-specific co-repressors for ERalpha.

Conclusions:

  • ERalpha's transcriptional activity is modulated by the cell cycle.
  • Cell-cycle-dependent recruitment of chromatin-remodelling complexes, like NuRD, regulates ERalpha function.

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