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Related Concept Videos

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.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
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.
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...
Vesicular Tubular Clusters01:45

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...
Synaptic Signaling01:09

Synaptic Signaling

Neurons communicate at synapses, or junctions, to excite or inhibit the activity of other neurons or target cells, such as muscles. Synapses may be chemical or electrical.
Most synapses are chemical, meaning an electrical impulse or action potential spurs the release of chemical messengers called neurotransmitters. The neuron sending the signal is called the presynaptic neuron, and the neuron receiving the signal is the postsynaptic neuron.
The presynaptic neuron fires an action potential that...
Synaptic Signaling01:12

Synaptic Signaling

Neurons communicate at synapses, or junctions, to excite or inhibit the activity of other neurons or target cells, such as muscles. Synapses may be chemical or electrical.
Exocytosis00:50

Exocytosis

Exocytosis is a process that releases molecules outside the cell. Like other bulk transport mechanisms, exocytosis requires energy.
Exocytosis is the opposite of endocytosis, which brings molecules inside the cell. Sometimes, the released materials are signaling molecules. For example, neurons typically use exocytosis to release neurotransmitters. Cells also use exocytosis to insert proteins such as ion channels into their cell membranes, secrete proteins for use in the extracellular matrix, or...

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Related Experiment Video

Updated: Jul 3, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Synaptic vesicle fusion.

Josep Rizo1, Christian Rosenmund

  • 1Department of Biochemistry, University of Texas Southwestern Medical Center, 6000 Harry Hines Boulevard, Dallas, Texas 75390, USA. jose@arnie.swmed.edu

Nature Structural & Molecular Biology
|July 12, 2008
PubMed
Summary
This summary is machine-generated.

Neurotransmitter release relies on SNARE complexes and Munc18-1 for membrane fusion. Understanding the complex interplay of proteins like Munc13s, RIMs, synaptotagmin-1, and complexins is crucial for elucidating this release mechanism.

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

Published on: October 19, 2012

Examination of Synaptic Vesicle Recycling Using FM Dyes During Evoked, Spontaneous, and Miniature Synaptic Activities
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Examination of Synaptic Vesicle Recycling Using FM Dyes During Evoked, Spontaneous, and Miniature Synaptic Activities

Published on: March 31, 2014

Related Experiment Videos

Last Updated: Jul 3, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
10:58

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

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

Examination of Synaptic Vesicle Recycling Using FM Dyes During Evoked, Spontaneous, and Miniature Synaptic Activities
08:10

Examination of Synaptic Vesicle Recycling Using FM Dyes During Evoked, Spontaneous, and Miniature Synaptic Activities

Published on: March 31, 2014

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • The release of neurotransmitters is a fundamental process in neuronal communication.
  • SNARE complexes are central to the fusion of synaptic vesicles with the plasma membrane.
  • Proteins such as Munc18-1, Munc13s, RIMs, synaptotagmin-1, and complexins play critical roles in regulating this machinery.

Purpose of the Study:

  • To elucidate the intricate molecular mechanisms governing neurotransmitter release.
  • To understand the roles of key proteins, including SNAREs, Munc18-1, Munc13s, RIMs, synaptotagmin-1, and complexins, in synaptic vesicle fusion.
  • To highlight the importance of protein-protein and protein-membrane interactions in presynaptic function.

Main Methods:

  • The study is primarily based on a review and synthesis of existing literature on the molecular machinery of neurotransmitter release.
  • It involves analyzing the known functions and interactions of proteins involved in synaptic vesicle exocytosis.
  • Focus is on understanding the functional roles of SNARE complexes, Munc18-1, Munc13s, RIMs, synaptotagmin-1, and complexins.

Main Results:

  • SNARE complexes mediate the close apposition and fusion of vesicle and plasma membranes.
  • Munc18-1 is essential for controlling SNARE complex formation and potentially directly participates in fusion.
  • Munc13s and RIMs orchestrate SNARE assembly, impacting vesicle priming and presynaptic plasticity.
  • Synaptotagmin-1, triggered by Ca2+, initiates release via interactions with SNAREs, membranes, and complexins.

Conclusions:

  • A comprehensive understanding of neurotransmitter release requires detailed knowledge of the interaction network among all involved proteins and membranes.
  • The interplay between SNAREs, Munc18-1, Munc13s, RIMs, synaptotagmin-1, and complexins is critical for regulated exocytosis.
  • Further research into these molecular interactions will advance our understanding of synaptic function and plasticity.