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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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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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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.
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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.
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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.
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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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Related Experiment Video

Updated: May 2, 2026

Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons
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Synaptotagmin 7 functions as a Ca2+-sensor for synaptic vesicle replenishment.

Huisheng Liu1, Hua Bai, Enfu Hui

  • 1Department of Neuroscience, Howard Hughes Medical Institute, University of Wisconsin-Madison, Madison, United States.

Elife
|February 27, 2014
PubMed
Summary

Synaptotagmin 7 (syt 7) is crucial for calcium-dependent synaptic vesicle replenishment in neurons. This protein interacts with calmodulin (CaM) to regulate vesicle recycling at nerve terminals.

Keywords:
neurotranmissionsynaptic vesiclesynaptotagmin

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An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins
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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Synaptotagmin (syt) 7 is one of three ubiquitously expressed syt isoforms in metazoans.
  • The precise function of syt 7 in neuronal synaptic vesicle (SV) replenishment remains largely unknown.

Purpose of the Study:

  • To elucidate the role of syt 7 in Ca(2+)-dependent and Ca(2+)-independent SV replenishment pathways.
  • To investigate the interaction between syt 7 and calmodulin (CaM) in regulating SV dynamics.

Main Methods:

  • Investigated SV replenishment pathways using genetic mutations disrupting Ca(2+)-binding sites in syt 7.
  • Utilized a calmodulin antagonist to assess its effect on SV replenishment.
  • Examined the Ca(2+)-dependent binding interaction between syt 7 and CaM.

Main Results:

  • Syt 7 selectively and critically regulates the Ca(2+)-dependent SV replenishment pathway.
  • Disruption of Ca(2+)-binding to syt 7 abolished its function, indicating syt 7 acts as a Ca(2+)-sensor.
  • Loss of syt 7 function was mimicked by a CaM antagonist.
  • Syt 7 binds specifically and Ca(2+)-dependently to CaM, requiring intact Ca(2+)-binding sites on syt 7.

Conclusions:

  • A complex of syt 7 and CaM acts as a key regulator of SV replenishment in presynaptic nerve terminals.
  • This conserved complex plays a critical role in maintaining neurotransmission through efficient vesicle recycling.