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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
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...
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:
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...

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Related Experiment Video

Updated: Jul 13, 2026

Heterokaryon Technique for Analysis of Cell Type-specific Localization
09:31

Heterokaryon Technique for Analysis of Cell Type-specific Localization

Published on: March 11, 2011

How specific are nuclear "receptors" for thyroid hormones?

J R Tata

    Nature
    |September 4, 1975
    PubMed
    Summary

    Thyroid hormone receptors are not solely in the nucleus, challenging previous models. Further research is needed to understand the physiological role of extranuclear thyroid hormone binding.

    Area of Science:

    • Endocrinology
    • Molecular Biology
    • Cell Biology

    Background:

    • Thyroid hormones play crucial roles in metabolism and development.
    • Nuclear receptors have been the primary focus for understanding thyroid hormone action.
    • Extranuclear binding sites for thyroid hormones have been reported but their significance is debated.

    Purpose of the Study:

    • To critically assess the physiological relevance of current in vitro methods for studying thyroid hormone binding.
    • To re-evaluate the analogy between thyroid hormone receptors and steroid hormone receptors based on binding site distribution.

    Main Methods:

    • Investigated the presence and characteristics of high-affinity, saturable binding sites for thyroid hormones.
    • Examined binding sites in isolated nuclei and major extranuclear cellular components.

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

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    In vivo Characterization of Endocrine Disrupting Chemical Effects via Thyroid Hormone Action Indicator Mouse
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    Last Updated: Jul 13, 2026

    Heterokaryon Technique for Analysis of Cell Type-specific Localization
    09:31

    Heterokaryon Technique for Analysis of Cell Type-specific Localization

    Published on: March 11, 2011

    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 15, 2013

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

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  • Assessed the ability of cytosol to promote nuclear binding of thyroid hormones.

    • Main Results:

    • Identified "high-affinity-saturable" binding sites for thyroid hormones in major extranuclear cellular components, not just isolated nuclei.
    • Observed similar characteristics of these binding sites across different cellular locations.
    • Demonstrated that cytosol does not promote nuclear binding of thyroid hormones.

    Conclusions:

    • The widespread distribution of thyroid hormone binding sites challenges the exclusive nuclear localization model.
    • The analogy with steroid hormone receptors, which primarily act via nuclear receptors, is invalidated.
    • A critical reassessment of the physiological relevance of in vitro nuclear binding assays for thyroid hormones is necessary.