Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Transducer Mechanism: Nuclear Receptors

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:

RNA Stability

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...

mRNA Stability and Gene Expression

mRNA Stability and Gene Expression

Internal Receptors

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.

Intracellular Hormone Receptors

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

G Protein-coupled Receptors

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...

You might also read

Related Articles

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

Sort by

Same author

Targeting the CCL2-CCR2 axis in cancer: insights into in vitro screening and humanized mice.

Journal of biochemistry·2026

Same author

Torsional flexibility of the thoracic spine is superior to that of the lumbar spine in cats: Implications for the falling cat problem.

Anatomical record (Hoboken, N.J. : 2007)·2026

Same author

Calcineurin in cancer signaling networks.

Nagoya journal of medical science·2025

Same author

Calcineurin-mediated dephosphorylation stabilizes E2F1 protein by suppressing binding of the FBXW7 ubiquitin ligase subunit.

Proceedings of the National Academy of Sciences of the United States of America·2024

Same author

Calcineurin/NFATc1 pathway represses cellular cytotoxicity by modulating histone H3 expression.

Scientific reports·2024

Same author

NFAT activation by FKBP52 promotes cancer cell proliferation by suppressing p53.

Life science alliance·2024

Search research articles

Related Experiment Video

Updated: Aug 26, 2025

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

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

Published on: December 19, 2018

Estrogen receptor α revised: Expression, structure, function, and stability.

Makoto Habara¹, Midori Shimada¹

¹Department of Veterinary Biochemistry, Yamaguchi University, Yamaguchi, Yamaguchi, Japan.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology

|October 3, 2022

Summary

Estrogen receptor alpha (ERα) is crucial in ERα-positive breast cancer. Understanding ERα regulation is key to overcoming endocrine therapy resistance and improving patient outcomes.

Keywords:

FKBP breast cancer calcineurin estrogen receptor α phosphorylation post-translational modification ubiquitination

More Related Videos

Profiling of Estrogen-regulated MicroRNAs in Breast Cancer Cells

Profiling of Estrogen-regulated MicroRNAs in Breast Cancer Cells

Published on: February 21, 2014

Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer

Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer

Published on: March 17, 2016

Related Experiment Videos

Last Updated: Aug 26, 2025

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

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

Published on: December 19, 2018

Profiling of Estrogen-regulated MicroRNAs in Breast Cancer Cells

Profiling of Estrogen-regulated MicroRNAs in Breast Cancer Cells

Published on: February 21, 2014

Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer

Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer

Published on: March 17, 2016

Area of Science:

Molecular Biology
Oncology
Genetics

Background:

Estrogen receptor alpha (ERα) drives proliferation in ERα-positive breast cancer, a common subtype.
Endocrine therapies targeting ERα signaling improve patient prognosis but face resistance.
Overcoming endocrine resistance necessitates a deep understanding of ERα regulatory mechanisms.

Approach:

This review synthesizes current knowledge on ERα regulation.
It examines ERα expression through copy number variation, epigenetic, and transcriptional control.
Post-translational modifications and their impact on ERα function are also discussed.

Key Points:

ERα expression is tightly controlled at multiple levels.
Epigenetic modifications and transcriptional regulation significantly impact ERα activity.
Post-translational modifications fine-tune ERα function and cellular responses.

Conclusions:

Comprehensive understanding of ERα regulation is vital for developing strategies against endocrine resistance.
Targeting ERα regulatory pathways offers potential therapeutic avenues for breast cancer treatment.