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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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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
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Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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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...
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Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

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The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
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Related Experiment Video

Updated: Oct 17, 2025

Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
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Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay

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Room for Two: The Synaptophysin/Synaptobrevin Complex.

Dustin N White1, Michael H B Stowell1

  • 1MCD Biology, University of Colorado Boulder, Boulder, CO, United States.

Frontiers in Synaptic Neuroscience
|October 7, 2021
PubMed
Summary
This summary is machine-generated.

Synaptophysin (SYP) and synaptobrevin (VAMP2) form a vital complex that anchors the SNARE machinery. This anchoring is crucial for regulating synaptic vesicle release and maintaining neuronal communication.

Keywords:
fusion machinerysupercomplexsynaptic fusionsynaptobrevinsynaptophysin (SYP)

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Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
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Vibrodissociation of Neurons from Rodent Brain Slices to Study Synaptic Transmission and Image Presynaptic Terminals
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Last Updated: Oct 17, 2025

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Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
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Vibrodissociation of Neurons from Rodent Brain Slices to Study Synaptic Transmission and Image Presynaptic Terminals
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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Synaptic vesicle release involves over 30 proteins, with disruptions causing neurological disorders like epilepsy and neurodegeneration.
  • Synaptophysin (SYP) is a mysterious presynaptic protein with proposed roles as a calcium sensor, cholesterol binder, or ion channel.
  • SYP's interaction with synaptobrevin (VAMP2) is physiologically significant, as VAMP2 is a key component of the neuronal SNARE complex.

Purpose of the Study:

  • To elucidate the functional role of the synaptophysin/synaptobrevin (SYP/VAMP2) complex in neuronal exocytosis.
  • To investigate how the SYP/VAMP2 complex contributes to the regulation of synaptic vesicle trafficking and fusion.

Main Methods:

  • The study focuses on the structural and functional implications of the SYP/VAMP2 interaction within the presynaptic terminal.
  • Analysis of the role of SYP and VAMP2 in the formation and anchoring of the SNARE complex.

Main Results:

  • The SYP/VAMP2 complex is implicated in the trafficking and regulation of the SNARE complex.
  • Structural observations suggest the SYP/VAMP2 complex anchors the SNARE assembly at the presynaptic membrane before vesicle fusion.

Conclusions:

  • The SYP/VAMP2 complex is essential for the proper structure and function of the neuronal exocytotic machinery.
  • Understanding the SYP/VAMP2 complex's role is critical for comprehending neuronal communication and associated disorders.