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 Concept Videos

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
Drug-Receptor Interactions01:29

Drug-Receptor Interactions

Drug-receptor interaction describes the binding of receptors by drugs, but not all drug-receptor interactions result in activation and tissue response. For instance, the binding of agonists activates the receptor to generate a cellular reaction, while antagonists bind to receptors without causing their activation.
Several parameters, such as the drug's affinity for its receptor and its efficacy, which is its ability to activate the receptor, determine the drug's effect on the tissue.
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:
Target Cell Response to Hormones01:22

Target Cell Response to Hormones

Hormones intricately bind to receptors on the surface or within target cells, initiating a cascade of cellular responses.
Notably, the cellular response can be regulated by altering the number of receptors expressed in the cell. For example, prolonged exposure to elevated hormone levels results in a gradual decline or down-regulation in the number of receptors for that specific hormone on the cell surface. Conversely, in response to low hormone levels, cells may use up-regulation, producing an...
Synthesis and Regulation of Thyroid Hormones01:20

Synthesis and Regulation of Thyroid Hormones

Low blood levels of the thyroid hormones — triiodothyronine (T3) and thyroxine (T4) — signal the hypothalamus to release the thyrotropin-releasing hormone (TRH). TRH then reaches the pituitary gland and stimulates the release of thyroid-stimulating hormone(TSH) into the bloodstream.
Upon reaching the thyroid gland, TSH stimulates the follicular cells' active uptake of iodide ions from the blood. The ions diffuse to the apical surface of the cells and are oxidized to iodine. The iodine is then...
Functions of Thyroid Hormones01:18

Functions of Thyroid Hormones

The thyroid hormone (TH) plays a pivotal role in the intricate orchestration of physiological processes, exerting profound effects on development, metabolism, and homeostasis throughout different life stages.
TH is indispensable for the normal development and maturation of the skeletal, muscular, and nervous systems during fetal and childhood growth. It facilitates bone mineral turnover and regulates protein synthesis in developing tissues, contributing significantly to overall growth and...

You might also read

Related Articles

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

Sort by
Same author

Exploring the mechanisms of biofield therapy through joint electrophysiological recordings in humans and mice.

IBRO neuroscience reports·2026
Same author

Structure-Based Discovery of Potent BCL-XL Inhibitors through Rescaffolding.

Journal of medicinal chemistry·2026
Same author

High rate of pulmonary exacerbations and neutrophilic airway inflammation in children with repaired esophageal atresia with or without tracheoesophageal fistula.

Pediatric research·2026
Same author

The Preclinical Effects and Mechanisms of Biofield Therapy on Pancreatic Cancer Cell Growth and Metastasis.

Cancer medicine·2026
Same author

Adapting Yoga Therapy to Meet the Needs of Inpatients Undergoing Hematopoietic Stem Cell Transplantation: Insights From an International, Multisite, Qualitative Study.

JCO global oncology·2026
Same author

Editorial: Understanding effective education: far transfer from a sociocultural and cognitive neural perspective.

Frontiers in psychology·2026
Same journal

Correction: Characterization of Mast2 kinase defines structural features, regulation, and substrates.

The Journal of biological chemistry·2026
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
See all related articles

Related Experiment Video

Updated: Jun 26, 2026

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
10:51

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists

Published on: November 16, 2013

Thyroxine-thyroid hormone receptor interactions.

Ben Sandler1, Paul Webb, James W Apriletti

  • 1Metabolic Research Unit and Diabetes Center, School of Medicine, University of California-San Francisco, 513 Parnassus Avenue, San Francisco, CA 94122-0540, USA.

The Journal of Biological Chemistry
|October 7, 2004
PubMed
Summary
This summary is machine-generated.

Thyroxine (T4) can activate thyroid hormone receptors (TRs), despite its 5' iodine group. Structural studies reveal TRbeta adapts to T4, suggesting T4

More Related Videos

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation
16:02

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation

Published on: February 10, 2023

In vivo Characterization of Endocrine Disrupting Chemical Effects via Thyroid Hormone Action Indicator Mouse
04:14

In vivo Characterization of Endocrine Disrupting Chemical Effects via Thyroid Hormone Action Indicator Mouse

Published on: October 6, 2023

Related Experiment Videos

Last Updated: Jun 26, 2026

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists
10:51

Reverse Yeast Two-hybrid System to Identify Mammalian Nuclear Receptor Residues that Interact with Ligands and/or Antagonists

Published on: November 16, 2013

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation
16:02

Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation

Published on: February 10, 2023

In vivo Characterization of Endocrine Disrupting Chemical Effects via Thyroid Hormone Action Indicator Mouse
04:14

In vivo Characterization of Endocrine Disrupting Chemical Effects via Thyroid Hormone Action Indicator Mouse

Published on: October 6, 2023

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Structural Biology

Background:

  • Thyroid hormone (TH) actions are mediated by nuclear receptors (TRs).
  • Triiodothyronine (T3) binds TRs with high affinity; thyroxine (T4) binds with lower affinity.
  • T4 has a bulky 5' iodine group absent in T3, potentially hindering binding.

Purpose of the Study:

  • To investigate how T4 affects TR activity and conformation.
  • To understand the structural basis for T4 interaction with TRs.
  • To assess T4's potential as a TR agonist.

Main Methods:

  • Ligand dissociation kinetics
  • Hydrophobic interaction chromatography
  • Non-denaturing gel electrophoresis
  • X-ray crystallography of TRbeta LBD-T3 and TRbeta LBD-T4 complexes

Main Results:

  • TR-T4 complexes adopt a different conformation than TR-T3 complexes in solution.
  • T4 acts as an agonist in vitro and in cells, independent of T3 conversion.
  • X-ray structures show TRbeta accommodates T4 via subtle structural adjustments, enabling coactivator binding.
  • TRbeta can adapt to T4's 5' iodine extension.

Conclusions:

  • Thyroxine (T4) can activate nuclear thyroid hormone receptors (TRs).
  • TRs possess structural adaptability to accommodate T4.
  • TR structural plasticity should be considered in the design of novel TR ligands.