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Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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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...
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Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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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...
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Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

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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...
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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...
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SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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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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Related Experiment Video

Updated: Nov 4, 2025

Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons
07:30

Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons

Published on: September 4, 2017

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Calcium-dependent docking of synaptic vesicles.

Melissa Silva1, Van Tran1, Alain Marty1

  • 1UniversitĂ© de Paris, SPPIN-Saints Pères Paris Institute for the Neurosciences, CNRS, F-75006 Paris, France.

Trends in Neurosciences
|May 29, 2021
PubMed
Summary
This summary is machine-generated.

Calcium ions regulate neurotransmitter release by controlling vesicle docking and maturation at presynaptic terminals. These calcium-dependent processes are crucial for synaptic strength and plasticity, impacting phenomena like synaptic facilitation.

Keywords:
SNARE proteinsactive zoneshort-term synaptic plasticitysynaptic vesiclessynaptotagminvesicle docking

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

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Calcium ion concentration in presynaptic terminals is critical for regulating neurotransmitter release.
  • The precise mechanisms underlying calcium's role in transmitter release have been largely unclear.

Purpose of the Study:

  • To review recent studies elucidating the mechanisms of calcium ion regulation of transmitter release.
  • To highlight the role of calcium in vesicle dynamics and synaptic strength modulation.

Main Methods:

  • Fast-freezing electron microscopy to visualize vesicle movements.
  • Total internal reflection fluorescence microscopy to study calcium-dependent vesicle dynamics.
  • Electrophysiological recordings from simple synapses.
  • Molecular studies identifying calcium-sensitive protein domains.

Main Results:

  • Calcium ions trigger exocytosis and modulate synaptic strength by controlling a final vesicle maturation step.
  • Complex calcium-dependent vesicle movements, including docking, occur on millisecond timescales.
  • Calcium-sensitive domains on Munc13 and synaptotagmin-1 facilitate membrane proximity for release.

Conclusions:

  • Calcium-dependent vesicle docking occurs across various timescales and is vital for synaptic facilitation, post-tetanic potentiation, and neuromodulator effects.
  • Understanding calcium's role in vesicle dynamics provides insights into synaptic plasticity and function.