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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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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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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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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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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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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...
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COP Coated Vesicles00:59

COP Coated Vesicles

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Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of...
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Related Experiment Video

Updated: Jun 6, 2025

Subcellular Fractionation for the Isolation of Synaptic Components from the Murine Brain
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Subcellular Fractionation for the Isolation of Synaptic Components from the Murine Brain

Published on: September 14, 2022

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Molecular architecture of synaptic vesicles.

Uljana Kravčenko1,2, Max Ruwolt3, Jana Kroll4,5,6

  • 1In situ Structural Biology, Max Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Berlin 13125, Germany.

Proceedings of the National Academy of Sciences of the United States of America
|November 27, 2024
PubMed
Summary

This study reveals the structural diversity and molecular architecture of individual synaptic vesicles (SVs) using cryoelectron tomography. It details protein organization within SVs and their interaction with clathrin coats, advancing understanding of SV recycling.

Keywords:
V-ATPaseclathrincryo-ETsynaptic vesicles

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Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons
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Related Experiment Videos

Last Updated: Jun 6, 2025

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Examination of Synaptic Vesicle Recycling Using FM Dyes During Evoked, Spontaneous, and Miniature Synaptic Activities
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Examination of Synaptic Vesicle Recycling Using FM Dyes During Evoked, Spontaneous, and Miniature Synaptic Activities

Published on: March 31, 2014

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Structural Biology

Background:

  • Synaptic vesicles (SVs) are crucial for neurotransmission, maintaining molecular composition through recycling.
  • Previous models of SVs are based on averages, lacking detail on individual vesicle heterogeneity.
  • The structural and molecular architecture of individual SVs remains poorly understood.

Purpose of the Study:

  • To visualize the molecular details and structural heterogeneity of individual synaptic vesicles.
  • To describe the protein organization within SVs and their interaction with clathrin machinery.
  • To advance the understanding of synaptic vesicle diversity and molecular architecture.

Main Methods:

  • Cryoelectron tomography was used to visualize SVs isolated from mouse brains and cultured neurons.
  • Subtomogram averaging was employed to determine the structure of V-ATPases.
  • Bioluminescence assays were utilized to investigate protein interactions.

Main Results:

  • Identified diverse small proteins on SV surfaces and internal protein densities.
  • Determined the structure of V-ATPases and their complex with synaptophysin (Syp).
  • Observed random V-ATPase distribution and identified partially assembled clathrin coats on a subpopulation of vesicles.

Conclusions:

  • Synaptic vesicles exhibit significant structural heterogeneity and complex molecular architecture.
  • V-ATPases interact with Syp and are randomly distributed on SVs.
  • Clathrin-coated vesicles and baskets are located near the cell membrane, suggesting roles in SV recycling.