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SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

10.9K
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.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
10.9K
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

11.0K
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...
11.0K
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

2.5K
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...
2.5K
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

8.5K
Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
8.5K
Rab Cascades01:25

Rab Cascades

2.6K
Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
2.6K
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

3.1K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
3.1K

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Related Experiment Video

Updated: Jun 21, 2025

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
09:19

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

Published on: October 19, 2012

14.0K

A role for synapsin tetramerization in synaptic vesicle clustering.

Sang-Ho Song1, George J Augustine1,2

  • 1Temasek Life sciences Laboratory, Singapore.

The Journal of Physiology
|July 9, 2024
PubMed
Summary

Synapsins regulate synaptic vesicle (SV) clustering. Tetramerization of synapsins, forming larger structures, optimally bridges SVs, overcoming repulsive forces and creating a reserve pool of SVs in presynaptic terminals.

Keywords:
synapsinssynaptic vesicle clusteringsynaptic vesicle traffickingtetramerization

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An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins
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Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture
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Last Updated: Jun 21, 2025

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Synapsins are implicated in regulating synaptic vesicle (SV) clustering.
  • The precise mechanism of synapsin action in SV clustering remains debated.

Purpose of the Study:

  • To review synapsins and their interactions.
  • To highlight the hypothesis of synapsin tetramerization as a mechanism for SV clustering.

Main Methods:

  • Literature review of synapsin function and interactions.
  • Analysis of experimental data supporting the tetramerization hypothesis.

Main Results:

  • Synapsin tetramers are larger than dimers.
  • Tetramers can form optimal bridges between SVs.
  • This bridging overcomes repulsive forces between negatively charged SV membranes.

Conclusions:

  • Synapsin tetramerization provides a plausible mechanism for SV clustering.
  • This mechanism explains the formation of a reserve pool of SVs in presynaptic terminals.