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Related Concept Videos

Membrane Domains01:18

Membrane Domains

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 anterior...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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 cytoskeletal...
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Membrane Fluidity01:23

Membrane Fluidity

Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
Fluid Mosaic Model01:19

Fluid Mosaic Model

Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich with the analogy of...

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Related Experiment Video

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Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients
08:15

Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients

Published on: July 16, 2018

Creating and modulating microdomains in pore-spanning membranes.

Alexander Orth1, Ludger Johannes, Winfried Römer

  • 1Institut für Organische und Biomolekulare Chemie, Georg-August-Universität Göttingen, Tammannstr. 2, 37077 Göttingen, Germany.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry
|December 3, 2011
PubMed
Summary

The pore size of the substrate significantly influences lipid membrane phase separation. This study demonstrates substrate control over lipid domain size in pore-spanning bilayers, impacting membrane organization.

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Last Updated: May 27, 2026

Membrane Remodeling of Giant Vesicles in Response to Localized Calcium Ion Gradients
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Published on: March 5, 2017

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics
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A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

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Area of Science:

  • Biophysics
  • Materials Science
  • Cell Biology

Background:

  • Plasma membrane structure is dictated by lipid and protein composition, and cytoskeleton interactions.
  • Microscopic phase separation in lipid bilayers is crucial for membrane function.
  • Substrate topography can influence membrane organization.

Purpose of the Study:

  • To investigate how underlying porous substrates affect lipid membrane phase separation.
  • To explore the control of lipid domain size in pore-spanning bilayers.
  • To examine the impact of Shiga toxin binding on membrane phase behavior.

Main Methods:

  • Preparation of pore-spanning lipid bilayers (DOPC/sphingomyelin/cholesterol/Gb(3)) on ordered silicon pore arrays.
  • Functionalization of silicon substrate with hydrophobic layers for membrane formation.
  • Confocal laser scanning fluorescence microscopy to visualize lipid domain coexistence (liquid-ordered and liquid-disordered).

Main Results:

  • Microscopic phase separation of lipid mixtures in pore-spanning bilayers is strongly influenced by the substrate's pore size.
  • The size of liquid-ordered (l(o)) phase domains was controlled by pore diameter, temperature, and cholesterol content.
  • Shiga toxin B-pentamer binding induced and increased l(o)-phase domains, even in non-phase separating membranes.

Conclusions:

  • Highly ordered porous substrates can dictate lipid membrane phase separation and domain organization.
  • Substrate engineering offers a method to control lipid membrane nanostructure.
  • Specific molecular interactions, like toxin binding, can significantly alter membrane phase behavior.