Related Experiment Video

Updated: Jun 4, 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

17β-estradiol regulates estrogen receptor α monoubiquitination

Piergiorgio La Rosa1, Maria Marino, Filippo Acconcia

  • 1Department of Biology, University Roma Tre, Viale Guglielmo Marconi, 446, Rome, Italy.

IUBMB Life
|February 1, 2011
PubMed

Insights

Estrogen receptor alpha (ERα) monoubiquitination is a newly discovered modification. This study found that 17β-estradiol (E2) negatively modulates ERα monoubiquitination, impacting cellular processes.

Area of Science:

  • Cellular biology
  • Molecular endocrinology
  • Post-translational modifications

Background:

  • Monoubiquitination is a key signaling mechanism in various physiological processes.
  • Estrogen receptor alpha (ERα) undergoes monoubiquitination, a recently identified post-translational modification.
  • The influence of 17β-estradiol (E2) on ERα monoubiquitination remains unexplored.

Purpose of the Study:

  • To investigate the E2-dependent modulation of ERα monoubiquitination.
  • To understand the role of E2 in regulating ERα post-translational modification.

Main Methods:

  • Studied ERα monoubiquitination in various cell lines.
  • Analyzed the effect of E2 on ERα modification.

Main Results:

  • ERα monoubiquitination is negatively modulated by E2.
  • E2 binding to ERα reduces its monoubiquitination.

Conclusions:

  • ERα monoubiquitination is a novel signaling modification.
  • This modification may play a role in regulating E2:ERα-mediated cellular processes.

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