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Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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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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Tail-anchoring of Proteins in the ER Membrane01:45

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
With the help of motor proteins such...
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Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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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.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Overview of Exosomes01:36

Overview of Exosomes

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Exosomes are stable, lipid bilayer-enclosed vesicles capable of crossing biological barriers. They can carry a wide range of molecules required for intercellular communication. Once exosomes are released from the cell where they originated, they enter a recipient cell through various pathways such as fusion, receptor-mediated endocytosis, macropinocytosis, and phagocytosis.
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Related Experiment Video

Updated: Jan 8, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
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Exosome Tethering Requires Tetherin Homodimerisation.

Yağmur Yıldızhan1, Adam M Bourke1, Hannah K Jackson1,2

  • 1Department of Pathology, University of Cambridge, Cambridge, UK.

Biology of the Cell
|December 18, 2025
PubMed
Summary
This summary is machine-generated.

Tetherin protein homodimers are crucial for retaining exosomes at the cell surface, controlling their release. This antiviral factor

Keywords:
exosomesextracellular vesiclesmembrane traffickingtethering

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Area of Science:

  • Cell Biology
  • Virology
  • Extracellular Vesicles

Background:

  • Exosomes are small extracellular vesicles involved in intercellular communication.
  • Tetherin is an antiviral restriction factor known to retain enveloped viruses and other particles at the cell surface.
  • The precise mechanism by which tetherin retains exosomes remains unclear.

Purpose of the Study:

  • To investigate the molecular mechanism by which tetherin retains exosomes at the cell surface.
  • To identify specific structural features of tetherin essential for exosome tethering.

Main Methods:

  • Biochemical assays
  • Live-cell imaging
  • Ultrastructural imaging
  • Mutational analysis of tetherin

Main Results:

  • Tetherin homodimer formation is essential for exosome retention at the cell surface.
  • Specific tetherin regions involved in trafficking to intraluminal vesicles (ILVs) have minimal impact on exosome tethering.
  • This suggests redundant mechanisms for tetherin trafficking to ILVs and exosomes.

Conclusions:

  • The formation of tetherin homodimers is a key molecular determinant for exosome tethering.
  • Tetherin's role in exosome retention is primarily mediated by its dimerization, not solely by its trafficking pathways to ILVs.
  • These findings offer the first molecular insights into the mechanisms governing exosome tethering and release control.