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Related Concept Videos

Internal Receptors01:31

Internal Receptors

Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.
Types of Receptors: Internal Receptors01:07

Types of Receptors: Internal Receptors

Many cellular signals are hydrophilic and cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind intracellular receptors that reside within the cell cytoplasm or nucleus. Many mammalian steroid hormones and nitric oxide (NO) gas use this cell signaling mechanism.
Similar to membrane-bound receptors, the binding of a ligand to the intracellular receptor of causes a conformational change in the...
Intracellular Hormone Receptors01:08

Intracellular Hormone Receptors

Lipid-soluble hormones diffuse across the plasma and nuclear membrane of target cells to bind to their specific intracellular receptors. These receptors act as transcription factors that regulate gene expression and protein synthesis in the target cell
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:

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Related Experiment Video

Updated: Jun 18, 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

Estradiol-induced estrogen receptor-alpha trafficking.

Galyna Bondar1, John Kuo, Naheed Hamid

  • 1Department of Neurobiology, Laboratory of Neuroendocrinology and Brian Research Institute, David Geffen School of Medicine, University of California, Los Angeles, California 90095, USA.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
|December 4, 2009
PubMed
Summary

Estradiol rapidly acts in the brain via membrane estrogen receptors (ERs), influencing cell signaling. This study shows ERalpha is in the membrane, with estradiol regulating its levels and trafficking.

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Last Updated: Jun 18, 2026

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

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Published on: December 19, 2018

An In Vivo Estrogen Deficiency Mouse Model for Screening Exogenous Estrogen Treatments of Cardiovascular Dysfunction After Menopause
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An In Vivo Estrogen Deficiency Mouse Model for Screening Exogenous Estrogen Treatments of Cardiovascular Dysfunction After Menopause

Published on: August 13, 2019

Area of Science:

  • Neuroendocrinology
  • Cellular Signaling
  • Molecular Neuroscience

Background:

  • Rapid, non-genomic actions of estradiol in the central nervous system (CNS) are mediated by membrane estrogen receptors (ERs).
  • These membrane-initiated signals interact with metabotropic glutamate receptors (mGluRs) to influence intracellular pathways, including calcium flux and neuroprogesterone synthesis in astrocytes.

Purpose of the Study:

  • To investigate the presence and function of ERalpha at the cell membrane.
  • To elucidate the role of estradiol and mGluR1a in regulating membrane ERalpha trafficking and activation.

Main Methods:

  • Surface biotinylation assays to identify and quantify membrane-bound ERalpha.
  • Immunoblotting with specific antibodies to detect ERalpha variants.
  • Assessment of receptor internalization as a marker of activation.
  • Pharmacological inhibition of ER and mGluR1a to study signaling interactions.

Main Results:

  • ERalpha was detected in the cell membrane, including a full-length 66 kDa form and a 52 kDa variant with an extracellular portion.
  • Estradiol rapidly increased membrane levels and internalization of both ERalpha forms within minutes.
  • Estradiol also promoted trafficking and internalization of mGluR1a, suggesting a functional interaction.
  • Inhibition of ER or mGluR1a blocked ERalpha membrane trafficking, and estradiol enhanced calcium flux.

Conclusions:

  • ERalpha is present in the plasma membrane with an extracellular domain, mediating rapid cellular responses.
  • Estradiol dynamically regulates membrane ERalpha levels and trafficking, influenced by mGluR1a.
  • These findings reveal a mechanism by which fluctuating estradiol levels modulate membrane-initiated signaling pathways in the CNS.