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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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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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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...
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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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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
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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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Related Experiment Video

Updated: Feb 25, 2026

Preparation of Synaptic Plasma Membrane and Postsynaptic Density Proteins Using a Discontinuous Sucrose Gradient
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Unc13 Aligns SNAREs and Superprimes Synaptic Vesicles.

Mark T Palfreyman1, Erik M Jorgensen1

  • 1Department of Biology, Howard Hughes Medical Institute, University of Utah, Salt Lake City, UT 84112, USA.

Neuron
|August 4, 2017
PubMed
Summary
This summary is machine-generated.

Unc13 proteins are crucial for exocytosis. New research shows Unc13 ensures SNARE complex assembly and identifies an autoinhibited state, advancing our understanding of vesicle trafficking.

Keywords:
C. elegansMunc13SNAREsUNC-13biochemistrydockingprimingsuperprimingsynaptic transmissionsynaptic vesicle

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Area of Science:

  • Cellular Biology
  • Neuroscience
  • Molecular Biology

Background:

  • Unc13 proteins are essential regulators of vesicle docking and priming in the process of exocytosis.
  • Proper functioning of Unc13 is critical for neurotransmitter release and synaptic transmission.

Purpose of the Study:

  • To elucidate the role of Unc13 in the assembly of SNARE complexes.
  • To identify and characterize novel regulatory states of Unc13 function.

Main Methods:

  • Investigated the interaction between Unc13 and SNARE proteins.
  • Utilized biochemical and biophysical techniques to study Unc13 structure and regulation.

Main Results:

  • Demonstrated that Unc13 facilitates the formation of functional SNARE subcomplexes.
  • Identified a previously unrecognized autoinhibited state of Unc13, regulated by its C1 and C2 domains.

Conclusions:

  • Unc13 plays a key role in ensuring the correct assembly of SNAREs for efficient exocytosis.
  • The discovery of an autoinhibited state provides new insights into the regulation of Unc13 activity and vesicle release.