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Related Concept Videos

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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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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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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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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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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The Early Endosome: Endocytosis of Transferrin01:28

The Early Endosome: Endocytosis of Transferrin

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Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
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Related Experiment Video

Updated: Jun 4, 2025

Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers
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Expression, Purification, and Liposome Binding of Budding Yeast SNX-BAR Heterodimers

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Endosomal sorting protein SNX4 limits synaptic vesicle docking and release.

Josse Poppinga1, Nolan J Barrett1, L Niels Cornelisse1,2

  • 1Department of Functional Genomics, Center for Neurogenomics and Cognitive Research (CNCR), VU University, Amsterdam, Netherlands.

Elife
|December 19, 2024
PubMed
Summary
This summary is machine-generated.

Sorting nexin 4 (SNX4) organizes membrane recycling in neurons. SNX4 depletion enhances neurotransmission by increasing synaptic vesicle density at the active zone, suggesting SNX4 negatively regulates vesicle release.

Keywords:
cell biologyhippocampal neuronmouseneuroscienceneurotranmissionplasticityrecycling endosomevesicle recruitment

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Sorting nexin 4 (SNX4) is crucial for membrane recycling and found in neuronal synapses.
  • The precise role of SNX4 in synapse function and neurotransmission is not well understood.

Purpose of the Study:

  • To investigate the function of SNX4 in regulating synaptic transmission and structure.
  • To determine how SNX4 impacts neurotransmitter release and vesicle dynamics at the synapse.

Main Methods:

  • Generation of a conditional SNX4 knock-out (cKO) mouse model.
  • Electrophysiological recordings to assess neurotransmission and synaptic function.
  • Analysis of synapse ultrastructure and synaptic vesicle localization via electron microscopy.

Main Results:

  • SNX4 cKO synapses exhibited enhanced neurotransmission during high-frequency stimulation, with normal basal neurotransmission.
  • Synapse ultrastructure analysis revealed an increased number of docked synaptic vesicles at the active zone and a decreased active zone length.
  • SNX4 depletion did not alter overall vesicle number, recycling, or levels of key proteins like VAMP2.

Conclusions:

  • SNX4 acts as a negative regulator of synaptic vesicle docking and neurotransmitter release.
  • SNX4 plays a significant role in regulating synaptic vesicle recruitment and density at the active zone.
  • These findings highlight SNX4's importance in synaptic plasticity and function.