Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Estrogen receptor dimerization: ligand binding regulates dimer affinity and dimer dissociation rate.

Anobel Tamrazi1, Kathryn E Carlson, Jonathan R Daniels

  • 1Department of Chemistry, University of Illinois, 600 South Mathews Avenue, Urbana, IL 61801, USA.

Molecular Endocrinology (Baltimore, Md.)
|November 29, 2002
PubMed
Summary

Estrogen receptor dimers are very stable, with ligands slowing their dissociation. Antagonists stabilize these dimers more than agonists, offering a new method to assess ligand activity.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Seronegative Cryoglobulinemic Glomerulonephritis Coexisting With Primary Sjögren Syndrome and HBV Infection: A Diagnostic and Therapeutic Challenge.

Kidney medicine·2026
Same author

Multi-Center, Multi-National Outcomes Following Endoscopic Endonasal Resection of Nonfunctional Pituitary Adenomas.

Journal of neurological surgery. Part B, Skull base·2026
Same author

JAK/STAT1-interferon-ISGylation networks in breast cancer resistance to inhibitors of FOXM1 and CDK4/6.

NPJ breast cancer·2026
Same author

Evidence for cPLA2 activation in Alzheimer's disease synaptic pathology.

Acta neuropathologica communications·2026
Same author

A novel case of compound heterozygous GFPT1 congenital myasthenic syndrome with a coexisting heterozygous DYSF mutation: clinical and pathological insights.

Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology·2026
Same author

Targeting FOXM1 reshapes antitumor immunity to attenuate small cell lung cancer progression.

Cancer letters·2025

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Endocrinology

Background:

  • Nuclear receptors, including the estrogen receptor-alpha ligand-binding domain (ERalpha-LBD), function as transcription factors through dimer formation.
  • Ligand binding is hypothesized to influence the stability of these nuclear receptor dimers.

Purpose of the Study:

  • To develop and utilize fluorescence resonance energy transfer (FRET)-based methods for measuring the thermodynamic and kinetic stability of ERalpha-LBD dimers.
  • To assess how ligand binding affects ERalpha-LBD dimer stability and dissociation rates.

Main Methods:

  • Site-specific chemical labeling of ERalpha-LBD with a single fluorophore.
  • Utilizing FRET to directly measure the affinity and stability of ERalpha-LBD dimers.
  • Assessing dimer dissociation rates and the impact of various ligands and coactivator peptides.

Related Experiment Videos

Main Results:

  • Unliganded ERalpha-LBDs form highly stable dimers with a slow dissociation rate (t(1/2) = 39 ± 3 min at 28°C).
  • Ligand addition further slows dimer dissociation, with antagonists providing greater kinetic stabilization than agonists.
  • Coactivator peptides containing the LXXLL motif selectively stabilize agonist-bound ERalpha-LBD dimers.

Conclusions:

  • The developed FRET-based assays provide a functional in vitro method to measure the kinetic and thermodynamic stability of ER dimers.
  • These assays can be used to assess the agonist or antagonist character of novel ligands by evaluating their effect on ER dimer stability.