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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...
13.1K
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...
3.3K
Rab Proteins01:14

Rab Proteins

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
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Related Experiment Video

Updated: Oct 4, 2025

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy

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SNARE proteins: zip codes in vesicle targeting?

Seiichi Koike1,2, Reinhard Jahn2

  • 1Department of Life Sciences and Bioengineering, Graduate School of Science and Engineering, University of Toyama, Toyama, Japan.

The Biochemical Journal
|February 4, 2022
PubMed
Summary

Soluble NSF Attachment Protein Receptors (SNAREs) may act as targeting signals, not just fusion mediators, in eukaryotic cell vesicle traffic. This review explores evidence for SNAREs regulating targeting specificity in membrane transport.

Keywords:
membrane fusionsnare proteinstrafficking

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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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Related Experiment Videos

Last Updated: Oct 4, 2025

Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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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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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Eukaryotic membrane traffic relies on transport vesicles for intracellular delivery.
  • Vesicle targeting involves Rab GTPases and phosphoinositides recognized by tethering factors.
  • Soluble NSF Attachment Protein Receptors (SNAREs) mediate the final fusion step.

Purpose of the Study:

  • To review evidence on the role of SNARE proteins in vesicle targeting.
  • To discuss recent data supporting SNAREs as targeting signals.
  • To explore SNARE participation in regulating targeting specificity.

Main Methods:

  • Literature review of existing research.
  • Analysis of recent experimental data.
  • Discussion of mechanistic models.

Main Results:

  • SNARE proteins interact with targeting signals and tethering factors.
  • Evidence suggests SNAREs may influence targeting specificity.
  • SNAREs might function beyond mediating membrane fusion.

Conclusions:

  • SNARE proteins have a potential dual role in vesicle traffic.
  • SNAREs may regulate targeting specificity in addition to fusion.
  • Further research is needed to fully elucidate SNARE function in targeting.