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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

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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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Overview of Secretory Vesicles01:33

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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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Vesicular Tubular Clusters01:45

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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.
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Pinching-off of Coated Vesicles01:32

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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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Intralumenal Vesicles and Multivesicular Bodies01:38

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Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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Related Experiment Video

Updated: Nov 21, 2025

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
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Membrane packing defects in synaptic vesicles recruit complexin and synuclein.

Jie Liu1, Bing Bu, Michael Crowe

  • 1Biomechanics and Biomaterials Laboratory, Department of Applied Mechanics, Beijing Institute of Technology, Beijing 100081, China.

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Complexin-1 and alpha-synuclein bind to curved membranes like synaptic vesicles. This interaction is driven by membrane packing defects, influenced by cholesterol, aiding neurotransmitter release.

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Last Updated: Nov 21, 2025

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Area of Science:

  • Neuroscience
  • Biophysics
  • Molecular Biology

Background:

  • Complexin-1 (Cpx) and alpha-synuclein (α-Syn) are key proteins in neurotransmitter release.
  • These proteins interact with synaptic vesicles (SVs), crucial for vesicle fusion.
  • Previous research indicates Cpx and α-Syn favor highly curved membranes, such as SVs.

Purpose of the Study:

  • To investigate the molecular mechanism behind the preferential association of Cpx and α-Syn with curved membranes.
  • To explain how these proteins interact with synaptic vesicles for efficient neurotransmitter release.

Main Methods:

  • In silico simulations were employed to model interactions.
  • Simulations probed the behavior of Cpx and α-Syn with membranes of varying curvature.
  • Membrane packing defects and their relationship with curvature were analyzed.

Main Results:

  • Preferential association of Cpx and α-Syn with smaller, curved membranes was observed.
  • This preference is linked to increased membrane packing defects in curved regions.
  • Hydrophobic acyl tails exposed by defects favorably interact with hydrophobic residues of Cpx and α-Syn.
  • Membrane defect concentration is proportional to curvature and cholesterol content.

Conclusions:

  • The study provides a biophysical explanation for Cpx and α-Syn's interaction with synaptic vesicles.
  • Membrane curvature and packing defects are critical factors in regulating these protein-membrane interactions.
  • Cholesterol plays a role in modulating membrane properties and potentially influencing protein association for neurotransmitter release.