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Related Concept Videos

Membrane Domains01:18

Membrane Domains

6.4K
The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the...
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Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
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Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

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Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
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Membrane Lipids01:32

Membrane Lipids

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Lipids are an essential component of all biological membranes. The average lipid content in mammalian membranes is 50%, though it can be as low as 20% in the inner mitochondrial membrane or as high as 80% in the myelin sheath present around the nerve cells.
Phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and sphingomyelin are the most common phospholipids present in mammalian membranes. At physiological pH, phosphatidylserine is negatively charged, while the other three...
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Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

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Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
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Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
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Related Experiment Video

Updated: Nov 2, 2025

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

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Ceramide structure dictates glycosphingolipid nanodomain assembly and function.

Senthil Arumugam1,2,3,4, Stefanie Schmieder5, Weria Pezeshkian6

  • 1Institut Curie, PSL Research University, U1143 INSERM, UMR3666 CNRS, Cellular and Chemical Biology unit, Paris, Cedex, France.

Nature Communications
|June 17, 2021
PubMed
Summary

GM1 gangliosides with saturated acyl chains actively form nanodomains in cell membranes, influencing cellular functions. Ligand binding, like cholera toxin, alters these domains, revealing the importance of ganglioside structure.

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Ganglioside Extraction, Purification and Profiling
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Mass Spectrometric Analysis of Glycosphingolipid Antigens
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Related Experiment Videos

Last Updated: Nov 2, 2025

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

13.6K
Ganglioside Extraction, Purification and Profiling
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Ganglioside Extraction, Purification and Profiling

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Mass Spectrometric Analysis of Glycosphingolipid Antigens
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Mass Spectrometric Analysis of Glycosphingolipid Antigens

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Area of Science:

  • Cell biology
  • Biophysics
  • Membrane biophysics

Background:

  • Gangliosides are crucial for cellular functions and pathogen interactions.
  • The dynamic organization and ligand response of gangliosides remain poorly understood.

Purpose of the Study:

  • To investigate how GM1 ganglioside structure affects its organization into membrane nanodomains.
  • To understand the impact of ligand binding on GM1 ganglioside nanodomains.

Main Methods:

  • Utilized fluorescence anisotropy imaging in living cells.
  • Incorporated synthetic, fluorescently labeled GM1 gangliosides with varying acyl chains.

Main Results:

  • GM1 with a saturated C16:0 acyl chain actively clustered into nanodomains, dependent on cholesterol, phosphatidylserine, and actin.
  • Cholera toxin B-subunit binding enlarged domains for both saturated and unsaturated GM1.
  • Co-clustering with CD59 was observed only for saturated GM1, not unsaturated.

Conclusions:

  • GM1 ganglioside ceramide acyl chain structure dictates nanodomain assembly and function.
  • These findings shed light on endogenous cellular processes involving ganglioside organization.