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Related Experiment Video

Updated: Jan 24, 2026

Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis

Oligomerization Dynamics of Cell Surface Receptors in Living Cells by Total Internal Reflection Fluorescence Microscopy Combined with Number and Brightness Analysis

Published on: November 6, 2019

A general method to quantify ligand-driven oligomerization from fluorescence-based images.

Michael R Stoneman¹, Gabriel Biener¹, Richard J Ward²

¹Physics Department, University of Wisconsin-Milwaukee, Milwaukee, WI, USA.

|May 22, 2019

Summary

This summary is machine-generated.

We developed fluorescence intensity fluctuation spectrometry to identify, quantify, and assess the stability of protein oligomers. This technique can screen drugs targeting protein-protein interactions for high-throughput applications.

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Last Updated: Jan 24, 2026

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Area of Science:

Biophysics
Biochemistry
Molecular Biology

Background:

Protein oligomerization is crucial for cellular function.
Understanding protein oligomeric states is vital for drug discovery.
Existing methods for analyzing protein oligomers can be time-consuming or limited in scope.

Purpose of the Study:

Introduce fluorescence intensity fluctuation spectrometry (FIFS) for protein oligomer analysis.
Determine the identity, abundance, and stability of protein oligomers.
Investigate the oligomeric states of specific receptors in response to ligands.

Main Methods:

Developed and validated fluorescence intensity fluctuation spectrometry (FIFS).
Tested the method on monomers and oligomers of known sizes.
Applied FIFS to study epidermal growth factor receptor and secretin receptor oligomerization.

Main Results:

FIFS accurately determines protein oligomer identity, abundance, and stability.
Revealed oligomeric states of epidermal growth factor receptor and secretin receptor.
Demonstrated the method's applicability in the presence and absence of agonist ligands.

Conclusions:

Fluorescence intensity fluctuation spectrometry is a powerful tool for protein oligomer research.
This method enables rapid, high-throughput screening of drugs targeting protein-protein interactions.
FIFS offers a scalable solution for studying dynamic protein interactions.