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Transducer Mechanism: Nuclear Receptors

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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:

Protein Import into the Peroxisomes

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Regulation of Nuclear Protein Sorting

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The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:

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Related Experiment Video

Updated: Jun 15, 2026

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

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

Published on: November 15, 2013

Oxysterol-binding proteins.

Neale D Ridgway¹

¹Department of Pediatrics, Dalhousie University, Halifax, Nova Scotia, B3H 4H7, Canada. nridgway@dal.ca

Sub-Cellular Biochemistry

|March 10, 2010

Summary

This summary is machine-generated.

Cholesterol distribution is vital for eukaryotic cell function, maintained by proteins like oxysterol-binding proteins (OSBPs). These proteins facilitate sterol transport between organelles, crucial for cellular homeostasis.

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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

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Last Updated: Jun 15, 2026

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

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

Published on: November 15, 2013

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Eukaryotic cells maintain distinct cholesterol levels across organelles, with plasma membranes rich and endoplasmic reticulum poor.
This cholesterol gradient is essential for cellular functions like signaling and transport, and for rapid responses to sterol fluctuations.
Vesicular transport and sterol-binding/transport proteins are key to maintaining this intracellular cholesterol distribution.

Purpose of the Study:

To discuss the functional and structural characteristics of the mammalian oxysterol-binding protein (OSBP) and OSBP-related protein (ORP) family.
To explore the role of the OSBP/ORP family in sterol transport and homeostasis.
To present evidence supporting a 'dual-targeting' model for sterol transport mediated by OSBP/ORPs.

Main Methods:

Review of existing literature on OSBP/ORP family members.
Analysis of structural and functional data related to OSBP/ORPs.
Discussion of experimental evidence implicating OSBPs in sterol transport.

Main Results:

The OSBP/ORP gene family comprises 12 members, each with a conserved sterol-binding domain.
OSBPs/ORPs possess additional domains enabling targeting to multiple organelle membranes.
Evidence suggests OSBPs facilitate rapid, energy-independent sterol transport between organelles.

Conclusions:

The OSBP/ORP family plays a critical role in regulating intracellular cholesterol distribution.
A 'dual-targeting' model explains how OSBPs/ORPs transport sterols between different cellular membranes.
Understanding OSBP/ORP function is key to comprehending cholesterol homeostasis and cellular signaling.