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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...

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...

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...

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...

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.

Action Potentials

Action Potentials

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Related Experiment Video

Updated: May 11, 2026

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

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

Published on: March 31, 2014

Dynamin isoforms decode action potential firing for synaptic vesicle recycling.

Shota Tanifuji¹, Megumi Funakoshi-Tago, Fumihito Ueda

¹Department of Physiology, Tokyo Medical University, Tokyo 160-8402, Japan.

The Journal of Biological Chemistry

|May 21, 2013

Summary

Three dynamin protein isoforms regulate synaptic vesicle recycling. Each dynamin isoform matches distinct neuronal firing patterns to specific vesicle reuse pathways, ensuring stable neurotransmission.

Keywords:

Action Potential Dynamin Electrophysiology Endocytosis Membrane Trafficking Neurobiology Sympathetic Neuron Synapses Synaptic Vesicle siRNA

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Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons

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Last Updated: May 11, 2026

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

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

Published on: March 31, 2014

FM Dye Cycling at the Synapse: Comparing High Potassium Depolarization, Electrical and Channelrhodopsin Stimulation

FM Dye Cycling at the Synapse: Comparing High Potassium Depolarization, Electrical and Channelrhodopsin Stimulation

Published on: May 24, 2018

Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons

Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons

Published on: September 4, 2017

Area of Science:

Neuroscience
Cell Biology
Molecular Biology

Background:

Presynaptic nerve terminals require stable neurotransmission through synaptic vesicle recycling.
Neuronal activity fluctuations necessitate adaptable vesicle trafficking mechanisms.
The molecular link between neuronal activity and vesicle recycling remains unclear.

Purpose of the Study:

To elucidate the molecular mechanism by which dynamin isoforms regulate synaptic vesicle recycling in response to varying neuronal activity.
To investigate how different dynamin isoforms match vesicle reuse pathways to specific action potential frequencies.

Main Methods:

Utilized genetic knockdown of dynamin isoforms in paired neurons.
Performed direct physiological measurements of synaptic transmission.
Analyzed vesicle trafficking kinetics and time constants.

Main Results:

Dynamin 3 exhibited slow kinetics, independent of action potential frequency, but acted rapidly (within 20 ms) post-AP.
Dynamin 1 regulated recycling to the readily releasable pool with fast kinetics in a slower time window (>50 ms) during high-frequency firing.
Dynamin 2 demonstrated intermediate kinetics, bridging the responses of dynamin 1 and 3.

Conclusions:

Dynamin isoforms differentially regulate synaptic vesicle recycling pathways.
Specific dynamin isoforms are tailored to distinct neuronal firing patterns, ensuring neurotransmission stability.
This isoform-specific regulation provides a molecular basis for adapting vesicle trafficking to neuronal activity.