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Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

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...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased ATP...
Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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...
Pinching-off of Coated Vesicles01:32

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...
Exocytosis00:50

Exocytosis

Exocytosis is a process that releases molecules outside the cell. Like other bulk transport mechanisms, exocytosis requires energy.
Exocytosis is the opposite of endocytosis, which brings molecules inside the cell. Sometimes, the released materials are signaling molecules. For example, neurons typically use exocytosis to release neurotransmitters. Cells also use exocytosis to insert proteins such as ion channels into their cell membranes, secrete proteins for use in the extracellular matrix, or...

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Live Imaging of Synaptic Vesicle Recycling in the Neuromuscular Junction of Dissected Larval Zebrafish
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The synapsin cycle: a view from the synaptic endocytic zone.

E Evergren1, F Benfenati, O Shupliakov

  • 1Department of Neuroscience, Karolinska Institutet, Stockholm, Sweden. emma.evergreen@ki.se

Journal of Neuroscience Research
|April 25, 2007
PubMed
Summary

Synapsin phosphoproteins are crucial for neurotransmitter release and nerve terminal function. New research reveals their role in synaptic vesicle recycling, expanding our understanding of these key proteins.

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Last Updated: Jul 15, 2026

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Published on: May 24, 2018

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Synapsin phosphoproteins, known for over 30 years, are implicated in neurotransmitter release and synaptogenesis.
  • These proteins are vital for clustering synaptic vesicles (SVs) at active zones and modulating synaptic strength.
  • Existing knowledge lacks a complete understanding of synapsin functions within the nerve terminal.

Purpose of the Study:

  • To elucidate the complete functional roles of synapsins within the nerve terminal.
  • To investigate the involvement of synapsins in synaptic vesicle (SV) recycling.
  • To explore novel functions of synapsins beyond their known roles.

Main Methods:

  • The study likely involved advanced microscopy techniques to observe synapsin localization during neurotransmitter release.
  • Biochemical assays may have been used to analyze protein interactions and SV dynamics.
  • Genetic manipulation or pharmacological interventions could have been employed to study synapsin function.

Main Results:

  • Synapsins play a critical role in the clustering of synaptic vesicles (SVs) at active zones.
  • These proteins modulate synaptic strength by acting at pre- and postdocking levels.
  • Recent findings show synapsins migrate to the endocytic zone during neurotransmitter release.

Conclusions:

  • Synapsins are essential for synaptic vesicle clustering and synaptic strength modulation.
  • Synapsin migration to the endocytic zone suggests a significant role in synaptic vesicle recycling.
  • Further research is needed to fully comprehend the multifaceted functions of synapsins in neuronal communication.