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Protein Diffusion in the Membrane

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

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Related Experiment Video

Updated: Oct 22, 2025

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Detection of Toxin Translocation into the Host Cytosol by Surface Plasmon Resonance

Published on: January 3, 2012

Cholera Toxin as a Probe for Membrane Biology.

Anne K Kenworthy¹, Stefanie S Schmieder^2,3,4, Krishnan Raghunathan⁵

¹Center for Membrane and Cell Physiology and Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22903, USA.

|August 26, 2021

Summary

Cholera toxin B-subunit (CTxB) is a key tool for studying cell membrane dynamics. Its interaction with GM1 glycosphingolipids enables research into membrane structure, trafficking, and nanodomain assembly.

Keywords:

GL-Lect hypothesis GM1 cholera toxin B-subunit endocytosis glycolipids membrane curvature membrane nanodomains membrane rafts retrograde trafficking

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Area of Science:

Membrane biology and biophysics
Cellular and molecular biology

Background:

Cholera toxin B-subunit (CTxB) is a widely used research tool.
CTxB is a stable homopentameric protein.
CTxB binds to GM1 glycosphingolipids on cell membranes.

Purpose of the Study:

To review advances in membrane biology and biophysics.
To highlight the utility of CTxB and GM1 in studying membrane dynamics.
To explore vesicular trafficking and nanodomain assembly models.

Main Methods:

Review of existing literature on CTxB and GM1.
Analysis of studies utilizing CTxB for membrane research.
Focus on membrane structure, dynamics, and lipid interactions.

Main Results:

CTxB provides a robust model for membrane studies.
CTxB facilitates exploration of membrane dynamics.
Advances in understanding vesicular trafficking and nanodomain assembly are discussed.

Conclusions:

CTxB is an invaluable tool in membrane research.
The CTxB-GM1 interaction is crucial for understanding membrane organization.
Further research utilizing CTxB will continue to advance membrane biology.