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

60.0K
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
60.0K
Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

2.7K
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:
2.7K
Internal Receptors01:31

Internal Receptors

74.8K
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.
74.8K
Types of Receptors: Internal Receptors01:07

Types of Receptors: Internal Receptors

32.8K
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...
32.8K
Signal Transduction: Overview01:26

Signal Transduction: Overview

11.9K
Cells respond to many types of information, often through receptor proteins positioned on the membrane. They respond to chemical signals, such as hormones, neurotransmitters, and other signaling molecules, initiating a series of molecular reactions to produce an appropriate response. This is called signal transduction. Cells also coordinate different responses elicited by the same signaling molecule via mediators, allowing molecular cross-talk.
Typically, signal transduction involves three...
11.9K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

3.4K
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...
3.4K

You might also read

Related Articles

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

Sort by
Same author

Metabotropic glutamate receptor subtype 7 has critical roles in regulation of the endocrine system and social behaviours.

Journal of neuroendocrinology·2018
Same author

The effect of kinship on spacing among female red-backed voles, Clethrionomys rufocanus bedfordiae.

Oecologia·2017
Same author

Ablation of neuropsin-neuregulin 1 signaling imbalances ErbB4 inhibitory networks and disrupts hippocampal gamma oscillation.

Translational psychiatry·2017
Same author

Genetic variation and local differences in Pacific cod Gadus macrocephalus around Japan.

Journal of fish biology·2016
Same author

Living scaffolds: surgical repair using scaffolds seeded with human adipose-derived stem cells.

Hernia : the journal of hernias and abdominal wall surgery·2015
Same author

Identification of hemiclonal reproduction in three species of Hexagrammos marine reef fishes.

Journal of fish biology·2014
Same journal

Nano-scale analyses of the chromatin decompaction induced by histone acetylation.

Archives of histology and cytology·2012
Same journal

Scale and tooth phenotypes in medaka with a mutated ectodysplasin-A receptor: implications for the evolutionary origin of oral and pharyngeal teeth.

Archives of histology and cytology·2012
Same journal

Recruited peripheral blood monocytes participate in the liver extramedullary hematopoietic milieu.

Archives of histology and cytology·2012
Same journal

Rapid three-dimensional analysis of renal biopsy sections by low vacuum scanning electron microscopy.

Archives of histology and cytology·2012
Same journal

A histomorphologic study of the normal healing response following digit amputation in C57bl/6 and MRL/MpJ mice.

Archives of histology and cytology·2011
Same journal

Neurocan contributes to the molecular heterogeneity of the perinodal ECM.

Archives of histology and cytology·2011
See all related articles

Related Experiment Video

Updated: Feb 18, 2026

High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy
15:13

High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy

Published on: July 25, 2014

11.9K

Subcellular steroid/nuclear receptor dynamics.

M Kawata1

  • 1Department of Anatomy and Neurobiology, Kyoto Prefectural University of Medicine, Japan. mkawata@basic.kpu-m.ac.jp

Archives of Histology and Cytology
|January 5, 2002
PubMed
Summary
This summary is machine-generated.

Steroid/nuclear receptors are ligand-dependent transcription factors. Their dynamic subcellular distribution and nuclear reorganization upon ligand binding can now be visualized in single cells using advanced imaging techniques.

More Related Videos

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

13.2K
Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
11:07

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

Published on: September 21, 2011

16.9K

Related Experiment Videos

Last Updated: Feb 18, 2026

High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy
15:13

High-resolution Spatiotemporal Analysis of Receptor Dynamics by Single-molecule Fluorescence Microscopy

Published on: July 25, 2014

11.9K
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

13.2K
Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
11:07

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

Published on: September 21, 2011

16.9K

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • Steroid/nuclear receptors, including those for steroid hormones, thyroid hormones, retinoic acids, and vitamin D, are crucial ligand-dependent transcription factors.
  • These receptors regulate gene transcription by binding to ligands and forming protein complexes with cofactors.

Purpose of the Study:

  • To investigate the dynamic subcellular localization and intranuclear reorganization of steroid/nuclear receptors.
  • To understand how ligand binding influences receptor distribution and transcriptional regulation.

Main Methods:

  • Utilized green fluorescent protein (GFP) and its variants for live-cell imaging.
  • Observed the subcellular distribution and intranuclear dynamics of steroid/nuclear receptors in response to ligand stimulation.

Main Results:

  • Steroid/nuclear receptors exhibit dynamic subcellular localization, with some shuttling between cytoplasm and nucleus.
  • Ligand binding induces rapid and complete nuclear translocation of receptors.
  • Intranuclear receptor distribution changes from homogeneous to heterogeneous, dot-like patterns upon hormonal stimulation.

Conclusions:

  • The subcellular distribution of steroid/nuclear receptors is highly dynamic and ligand-dependent.
  • Ligand-induced nuclear reorganization involves complex protein interactions and cofactor recruitment.
  • Advanced imaging allows for the visualization and localization of steroid/nuclear receptor activities within single cells.