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Updated: Oct 18, 2025

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Published on: August 15, 2013

A bimolecular fluorescence complementation flow cytometry screen for membrane protein interactions.

Florian Schmitz¹, Jessica Glas¹, Richard Neutze¹

¹Department of Chemistry and Molecular Biology, Gothenburg University, Box 462, 405 30, Göteborg, Sweden.

Scientific Reports

|September 29, 2021

Summary

This summary is machine-generated.

We developed a novel screening method using bimolecular fluorescence complementation (BiFC) and flow cytometry to study membrane protein interactions in yeast. This approach efficiently identifies protein:protein interactions (PPIs) in vivo.

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Last Updated: Oct 18, 2025

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Flow Cytometric Analysis of Bimolecular Fluorescence Complementation: A High Throughput Quantitative Method to Study Protein-protein Interaction

Published on: August 15, 2013

Bimolecular Fluorescence Complementation

Bimolecular Fluorescence Complementation

Published on: April 15, 2011

A Fluorescence Fluctuation Spectroscopy Assay of Protein-Protein Interactions at Cell-Cell Contacts

A Fluorescence Fluctuation Spectroscopy Assay of Protein-Protein Interactions at Cell-Cell Contacts

Published on: December 1, 2018

Area of Science:

Cellular biology
Biochemistry
Molecular biology

Background:

Membrane protein interactions are vital for cellular functions.
Existing methods for detecting protein:protein interactions (PPIs) often target soluble proteins.
Visualizing membrane protein complexes in vivo is challenging.

Purpose of the Study:

To develop a robust screening approach for analyzing membrane protein interactions.
To adapt bimolecular fluorescence complementation (BiFC) assays for membrane proteins.
To utilize flow cytometry for high-throughput screening of in vivo PPIs.

Main Methods:

Utilized bimolecular fluorescence complementation (BiFC) in Saccharomyces cerevisiae.
Employed flow cytometry to analyze membrane protein complex formation.
Developed a method to distinguish specific PPIs from random interactions.

Main Results:

Successfully screened for membrane protein interaction partners in yeast.
Demonstrated the ability to discriminate specific complexes from random interactions with statistical confidence.
Established an efficient in vivo screening setup for PPIs.

Conclusions:

The developed BiFC-based flow cytometry approach is effective for studying membrane protein interactions.
This method facilitates high-throughput screening of in vivo PPIs.
The approach enhances our understanding of molecular mechanisms in cellular environments.