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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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Related Experiment Video

Updated: Jan 17, 2026

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy

Published on: September 11, 2015

Building a dynamic model for EGFR-family dimerization using quantitative, live-cell fluorescence methods.

Eric A Burns¹, Brent Matyas², Diane S Lidke¹

¹Department of Pathology and Comprehensive Cancer Center, University of New Mexico Health Sciences Center, Albuquerque, New Mexico.

Biophysical Journal

|September 17, 2025

Summary

This summary is machine-generated.

Advanced fluorescence techniques reveal how epidermal growth factor receptor (EGFR) family signaling, including EGFR and HER2, drives cancer. These methods uncover receptor dynamics and inform targeted therapy development for improved cancer treatment outcomes.

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

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Published on: November 6, 2019

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

Related Experiment Videos

Last Updated: Jan 17, 2026

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy

Published on: September 11, 2015

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

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Deciphering the Structural Effects of Activating EGFR Somatic Mutations with Molecular Dynamics Simulation

Published on: May 20, 2020

Area of Science:

Cellular signaling and molecular biology
Biophysics and structural biology
Cancer research and therapeutics

Background:

The epidermal growth factor receptor (EGFR) family is crucial for cell growth and survival.
Aberrant EGFR signaling, driven by mutations or overexpression, promotes cancer progression.
Current treatments targeting EGFR family members show limited clinical success.

Purpose of the Study:

To review structural insights into EGFR-family receptor oligomerization.
To highlight the application of advanced fluorescence techniques in studying EGFR dynamics.
To explore how receptor oligomerization influences cancer development and therapeutic responses.

Main Methods:

Analysis of high-resolution structural data (cryo-EM, crystallography).
Application of live-cell quantitative fluorescence techniques (FRET, SPT, super-resolution microscopy, FFS).
Examination of oncogenic mutations affecting EGFR-family receptor structure and function.

Main Results:

Ligand-induced dimerization and activation mechanisms are partially understood through static structures.
Fluorescence methods reveal dynamic, transient, and higher-order oligomerization states of EGFR family receptors.
Oncogenic mutations stabilize receptor oligomerization, leading to constitutive signaling and therapeutic resistance.

Conclusions:

Fluorescence-based methods bridge the gap between structural data and in situ receptor function.
Understanding EGFR-family oligomerization dynamics is critical for cancer biology.
Advanced fluorescence techniques aid in designing more effective targeted therapies against EGFR-driven cancers.