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Updated: Jun 28, 2026

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Luciferase Complementation Imaging Assay in Nicotiana benthamiana Leaves for Transiently Determining Protein-protein Interaction Dynamics

Published on: November 20, 2017

Imaging chemokine receptor dimerization with firefly luciferase complementation.

Kathryn E Luker¹, Mudit Gupta, Gary D Luker

¹Center for Molecular Imaging, Department of Radiology, University of Michigan Medical School, 109 Zina Pitcher Pl., A526 BSRB, Ann Arbor, MI 48109-2200, USA. gluker@umich.edu

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology

|November 13, 2008

Summary

This summary is machine-generated.

We developed a luciferase assay to study seven-transmembrane receptor dimerization. This method monitors chemokine receptor (CXCR4, CXCR7) homodimerization in cells and animals, aiding drug development.

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Area of Science:

Biochemistry
Molecular Biology
Pharmacology

Background:

Seven-transmembrane receptors are crucial drug targets involved in physiology and disease.
Receptor dimerization regulates ligand binding and signaling, presenting a therapeutic target.
Chemokine receptors CXCR4 and CXCR7 play key roles in development and cancer.

Purpose of the Study:

To develop a novel protein fragment complementation assay for monitoring seven-transmembrane receptor dimerization.
To investigate the dimerization of chemokine receptors CXCR4 and CXCR7 in vitro and in vivo.
To assess the impact of ligands and drugs on receptor dimerization.

Main Methods:

Developed a firefly luciferase-based protein fragment complementation assay.
Applied the assay to study homodimerization and heterodimerization of CXCR4 and CXCR7.
Utilized bioluminescence imaging in a breast cancer xenograft model.

Main Results:

The assay detected time- and dose-dependent changes in reporter signal upon ligand and drug treatment.
Chemokines modulated reporter signals for CXCR4 and CXCR7 homodimers but not heterodimers.
In vivo imaging demonstrated changes in receptor homodimerization in response to pharmacologic agents.

Conclusions:

The developed luciferase complementation assay is effective for monitoring seven-transmembrane receptor dimerization in cell-based assays and living animals.
This technology provides a valuable tool for analyzing receptor dimerization function and therapeutic modulation.
The findings highlight the potential of targeting receptor dimerization for therapeutic interventions.