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Protein Dynamics in Living Cells

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Updated: Mar 3, 2026

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves

Protein-protein Interactions Visualized by Bimolecular Fluorescence Complementation in Tobacco Protoplasts and Leaves

Published on: March 9, 2014

Studying Protein-Protein Interactions In Planta Using Advanced Fluorescence Microscopy.

Marc Somssich^1,2, Rüdiger Simon³

¹Institute for Developmental Genetics, Heinrich Heine University, Universitätsstr. 1, 40225, Düsseldorf, Germany.

Methods in Molecular Biology (Clifton, N.J.)

|April 26, 2017

Summary

This study details Förster resonance energy transfer (FRET) methods for analyzing protein interactions in plants. It provides a guide for acceptor photobleaching (APB) and fluorescence lifetime imaging microscopy (FLIM) in Nicotiana benthamiana.

Keywords:

APB Acceptor photobleaching Confocal fluorescence microscopy FLIM FRET Fluorescence lifetime Live cell imaging Nicotiana benthamiana Protein–protein interaction

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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

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Last Updated: Mar 3, 2026

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Published on: March 9, 2014

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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

Area of Science:

Molecular Biology
Cell Biology
Biophysics

Background:

Protein-protein interactions are fundamental to biological processes.
Understanding these interactions requires robust analytical techniques.
Förster resonance energy transfer (FRET) is a powerful method for studying molecular interactions in vivo.

Purpose of the Study:

To provide a comprehensive guide for performing FRET measurements in plants.
To detail acceptor photobleaching (APB) and fluorescence lifetime imaging microscopy (FLIM) protocols.
To enable in vivo analysis of protein interactions within specific cellular compartments in planta.

Main Methods:

Confocal fluorescence microscopy.
Acceptor photobleaching (APB) FRET.
Fluorescence lifetime imaging microscopy (FLIM).
Plant expression system: Nicotiana benthamiana.

Main Results:

Established step-by-step protocols for APB-FRET and FLIM-FRET.
Demonstrated the feasibility of these techniques in Nicotiana benthamiana.
Enabled visualization and quantification of protein interactions in living plant cells.

Conclusions:

APB-FRET and FLIM-FRET are effective methods for studying protein interactions in planta.
These techniques are crucial for understanding plant biological processes at the molecular level.
The provided guide facilitates the application of advanced FRET imaging in plant science.