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Related Concept Videos

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...
The Early Endosome: Endocytosis of Transferrin01:28

The Early Endosome: Endocytosis of Transferrin

Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
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Maturation of Endosomes01:28

Maturation of Endosomes

The early endosome containing internalized molecules matures through transformations in its location, morphology, intraluminal pH, and membrane protein composition. Together, these changes result in a more acidic late endosome that contains multiple intraluminal vesicles; therefore, the late endosome is also called a multivesicular body (MVB).
Changes in location
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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.
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Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
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Brain Membrane Fractionation: An Ex Vivo Approach to Assess Subsynaptic Protein Localization
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Synaptic membrane proteins form stable microdomains in early endosomes.

Ulf Geumann1, Christina Schäfer, Dietmar Riedel

  • 1Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen 37077, Germany.

Microscopy Research and Technique
|November 26, 2009
PubMed
Summary

Synaptic membrane proteins form stable, dynamic clusters within endosomes, persisting through membrane recycling. Cholesterol depletion disrupts these microdomains, highlighting their importance in endosomal organization.

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Area of Science:

  • Cell Biology
  • Membrane Biology
  • Neuroscience

Background:

  • Membrane proteins organize into microdomains in the plasma membrane, stabilized by protein interactions and cholesterol.
  • The persistence of these microdomains during endocytotic membrane trafficking remains largely unknown.

Purpose of the Study:

  • To investigate the existence and stability of protein-organized microdomains within endosomes.
  • To determine the role of cholesterol and other proteins in maintaining endosomal microdomain structure.

Main Methods:

  • Stimulated emission-depletion (STED) microscopy was employed to visualize and analyze endosomal microdomains.
  • A novel semiautomatic method was developed and validated by immunoelectron microscopy for domain counting.
  • Liposome fusion was used to acutely alter endosomal lipid composition and study its effects.

Main Results:

  • Synaptophysin and SNARE proteins were found to be organized in microdomains within endosomes derived from neuroendocrine PC12 cells.
  • Cholesterol depletion using methyl-beta-cyclodextrin led to the disintegration of most observed microdomains.
  • Endosomal microdomain frequency was unaffected by fusion with protein-free liposomes, regardless of lipid composition, and by Rab protein depletion.
  • Exogenous proteins introduced via liposome fusion equilibrated within existing microdomains.

Conclusions:

  • Synaptic membrane proteins form stable yet dynamic clusters within endosomes.
  • These microdomains are cholesterol-dependent and likely persist during membrane recycling processes.