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Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

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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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SNAREs and Membrane Fusion01:43

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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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Pinching-off of Coated Vesicles01:32

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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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Overview of Secretory Vesicles01:33

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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.
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Tail-anchoring of Proteins in the ER Membrane01:45

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Related Experiment Video

Updated: Jun 29, 2025

In Vivo Single-Molecule Tracking at the Drosophila Presynaptic Motor Nerve Terminal
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Synaptotagmin 7 docks synaptic vesicles to support facilitation and Doc2α-triggered asynchronous release.

Zhenyong Wu1,2, Grant F Kusick3,4, Manon M M Berns5

  • 1Department of Neuroscience, University of Wisconsin-Madison, Madison, United States.

Elife
|March 27, 2024
PubMed
Summary
This summary is machine-generated.

Doc2α is the primary calcium sensor for asynchronous neurotransmitter release, while synaptotagmin 7 (syt7) aids in synaptic vesicle docking. This clarifies the molecular mechanisms of asynchronous release at excitatory synapses.

Keywords:
asynchronous releasecell biologyiGluSnFRmouseneuroscienceshort-term plasticitysynaptic vesicle dockingsynaptotagminzap-and-freeze

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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
  • Molecular Biology
  • Cell Biology

Background:

  • The molecular mechanisms underlying asynchronous neurotransmitter release are not fully understood.
  • Synaptotagmin (syt) 7 and Doc2 have been implicated as calcium sensors for this process, but their specific roles are debated.

Purpose of the Study:

  • To elucidate the distinct roles of Doc2α and syt7 in asynchronous neurotransmitter release at excitatory mouse hippocampal synapses.
  • To resolve the controversy surrounding the calcium sensors responsible for asynchronous exocytosis.

Main Methods:

  • Utilized genetic deletion (knockout) of Doc2α and syt7 in mouse hippocampal neurons.
  • Assessed neurotransmitter release kinetics, including synchronous and asynchronous release, using electrophysiological recordings.
  • Investigated synaptic vesicle docking and replenishment dynamics.

Main Results:

  • Doc2α is the major Ca2+ sensor for asynchronous release; its absence significantly reduces release after single action potentials.
  • Syt7 is crucial for activity-dependent docking of synaptic vesicles, ensuring replenishment for sustained release during repetitive activity.
  • Disruption of both Doc2α and syt7 showed non-additive effects, supporting their distinct roles.

Conclusions:

  • Doc2α acts as the primary Ca2+ sensor for asynchronous neurotransmitter release.
  • Syt7 facilitates asynchronous release by promoting activity-dependent synaptic vesicle docking.
  • A new model proposes syt7 drives docking, supplying vesicles for both synchronous (syt1-mediated) and asynchronous (Doc2α and other sensors) release.