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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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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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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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Chemical Synapses01:26

Chemical Synapses

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Chemical synapses are specialized sites between two neurons or between a neuron and a non-neuronal cell like a muscle, glandular or sensory cell.
Because chemical synapses depend on the release of neurotransmitter molecules from synaptic vesicles to pass on their signal, there is an approximately one millisecond delay between when the axon potential reaches the presynaptic terminal and when the neurotransmitter leads to opening of postsynaptic ion channels. Additionally, this signaling is...
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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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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Related Experiment Video

Updated: Jul 12, 2025

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

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Synapsin condensation controls synaptic vesicle sequestering and dynamics.

Christian Hoffmann1, Jakob Rentsch2, Taka A Tsunoyama3

  • 1Laboratory of Molecular Neuroscience, German Center for Neurodegenerative Diseases (DZNE), 10117, Berlin, Germany.

Nature Communications
|October 23, 2023
PubMed
Summary
This summary is machine-generated.

Synaptic vesicles (SVs) are confined and motile at synapses due to the liquid-like condensates formed by SVs and synapsin 1. This interaction ensures reliable SV behavior for neuronal transmission.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biophysics

Background:

  • Neuronal transmission depends on regulated neurotransmitter release from synaptic vesicles (SVs).
  • SV confinement and mobility at synaptic boutons are crucial for rapid neurotransmitter release but poorly understood.
  • Synapsin 1 is a highly abundant synaptic protein involved in SV regulation.

Purpose of the Study:

  • To elucidate the mechanism underlying synaptic vesicle confinement and motility.
  • To investigate the role of synapsin 1 in organizing synaptic vesicles within boutons.

Main Methods:

  • Ultrafast single-molecule tracking (SMT) in reconstituted SV systems and living neurons.
  • Two-color SMT and super-resolution imaging in living axons.
  • Experiments using synapsin triple knock-out animals.

Main Results:

  • Synaptic vesicles and synapsin 1 form liquid-like condensates.
  • Synapsin 1 slows its own movement within these condensates, indicating increased packing.
  • Synapsin 1 drives SV accumulation in boutons and restores native SV motility patterns, even with a short fragment.

Conclusions:

  • Synapsin 1 condensation is sufficient to ensure both confinement and motility of synaptic vesicles.
  • This process enables the formation of mesoscale domains of SVs at synapses in vivo.
  • Synapsin 1 plays a critical role in organizing SVs for efficient neuronal signaling.