Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

SNAREs and Membrane Fusion

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.
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...

Fusion of Secretory Vesicles with the Plasma Membrane

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.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...

Vesicular Tubular Clusters

Vesicular Tubular Clusters

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...

Overview of Secretory Vesicles

Overview of Secretory Vesicles

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...

Rab Cascades

Rab Cascades

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.

Pinching-off of Coated Vesicles

Pinching-off of Coated Vesicles

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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Serotonergic Input into the Cerebellar Cortex Modulates Anxiety-Like Behavior.

The Journal of neuroscience : the official journal of the Society for Neuroscience·2025

Same author

Synapsin 2a tetramerisation selectively controls the presynaptic nanoscale organisation of reserve synaptic vesicles.

Nature communications·2024

Same author

Social memory deficit caused by dysregulation of the cerebellar vermis.

Nature communications·2023

Same author

A functional logic for neurotransmitter corelease in the cholinergic forebrain pathway.

Proceedings of the National Academy of Sciences of the United States of America·2023

Same author

Feedback inhibition underlies new computational functions of cerebellar interneurons.

eLife·2022

Same author

A neural circuit for excessive feeding driven by environmental context in mice.

Nature neuroscience·2021

Search research articles

Related Experiment Video

Updated: Jun 21, 2025

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

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

Published on: October 19, 2012

A role for synapsin tetramerization in synaptic vesicle clustering.

Sang-Ho Song¹, George J Augustine^1,2

¹Temasek Life sciences Laboratory, Singapore.

The Journal of Physiology

|July 9, 2024

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:

synapsins synaptic vesicle clustering synaptic vesicle trafficking tetramerization

More Related Videos

An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins

An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins

Published on: June 26, 2018

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Published on: August 2, 2019

Related Experiment Videos

Last Updated: Jun 21, 2025

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

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

Published on: October 19, 2012

An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins

An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins

Published on: June 26, 2018

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Presynapse Formation Assay Using Presynapse Organizer Beads and “Neuron Ball” Culture

Published on: August 2, 2019

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.