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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...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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...
Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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

Tail-anchoring of Proteins in the ER Membrane

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...
Chemical Synapses01:26

Chemical Synapses

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...
Chemical Synapses01:26

Chemical Synapses

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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Related Experiment Video

Updated: Jun 1, 2026

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
08:06

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient

Published on: September 3, 2014

SV31 is a Zn2+-binding synaptic vesicle protein.

Joern Barth1, Herbert Zimmermann, Walter Volknandt

  • 1Institute of Cell Biology and Neuroscience, Biocenter, Goethe-University, Frankfurt am Main, Germany. j.barth@em.uni-frankfurt.de

Journal of Neurochemistry
|June 15, 2011
PubMed
Summary

Researchers discovered a new synaptic vesicle protein, SV31, that binds zinc ions. This protein is located in endosomes and synaptic-like vesicles in neuronal cells, suggesting a role in zinc transport.

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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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Last Updated: Jun 1, 2026

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
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Published on: September 3, 2014

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An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins
09:33

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

Published on: June 26, 2018

Area of Science:

  • Neurobiology
  • Proteomics
  • Molecular Biology

Background:

  • A novel 31 kDa synaptic vesicle membrane protein (SV31) was identified.
  • SV31's function remained unknown, but its topology and phylogeny suggested a role as a vesicular transporter.

Purpose of the Study:

  • To investigate the function of the novel synaptic vesicle protein SV31.
  • To determine SV31's metal ion-binding properties and cellular localization.

Main Methods:

  • Recombinant SV31 protein expression and metal ion-binding assays.
  • Heterologous expression of SV31-RFP in PC12 cells and zinc-binding verification using FluoZin-3.
  • Sucrose density gradient fractionation and immunocytochemical analysis.

Main Results:

  • Recombinant SV31 binds Zn(2+) and Ni(2+), and to a lesser extent Cu(2+).
  • SV31-RFP co-localizes partially with synaptic vesicle markers and rab5 in transfected PC12 cells.
  • Immunocytochemistry shows SV31 localization in the soma, neurites, and near the plasma membrane, co-localizing with SNAP-25 and syntaxin1A.

Conclusions:

  • SV31 is a novel Zn(2+)-binding protein.
  • In PC12 cells, SV31 is targeted to endosomes and synaptic-like microvesicles.
  • SV31 may play a role in intracellular zinc transport within neuronal compartments.