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Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

11.1K
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...
11.1K
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...
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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...
2.5K
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

3.5K
Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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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.
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Related Experiment Video

Updated: Jun 26, 2025

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

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Serotonin Promotes Vesicular Association and Fusion by Modifying Lipid Bilayers.

Debsankar Saha Roy1, Ankur Gupta1, Vicky Vishvakarma1

  • 1Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai 400005, India.

The Journal of Physical Chemistry. B
|May 14, 2024
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Summary

Monoamine neurotransmitters like serotonin can enhance vesicle fusion by interacting with lipid bilayers. This finding reveals a new mechanism for controlling neurotransmission.

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

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Related Experiment Videos

Last Updated: Jun 26, 2025

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
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An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins
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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

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Membrane Biophysics

Background:

  • Chemical neurotransmission relies on vesicle fusion and cargo release.
  • Amphiphilic neurotransmitters interact with lipid bilayers, potentially influencing fusion.

Purpose of the Study:

  • To investigate if serotonin enhances artificial lipid vesicle association and fusion in vitro.
  • To explore the mechanism behind serotonin's effect on membrane properties.

Main Methods:

  • Fluorescence correlation spectroscopy
  • Total internal reflection fluorescence microscopy
  • Molecular dynamics simulations
  • Fluorescence spectroscopy

Main Results:

  • Serotonin dose-dependently enhanced vesicle-bilayer association, increasing spontaneous fusion rates.
  • Serotonin insertion increased bilayer water content, suggesting a drying transition drives association.
  • Dopamine and norepinephrine showed similar effects, but tryptophan did not.

Conclusions:

  • Monoamines can modulate vesicle fusion through lipid bilayer interactions.
  • This lipid bilayer-mediated mechanism offers a new perspective on neurotransmission regulation.