V-snare
V-snare - Related Videos
09:19
Analysis of SNARE-mediated Membrane Fusion Using an Enzymatic Cell Fusion Assay
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2012
We have developed a cell fusion assay that quantifies SNARE-mediated membrane fusion events by activated expression of β-galactosidase.
01:43
SNAREs and Membrane Fusion
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2023
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...
10:58
SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy
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Cited by 8 •
2016
Here, we present a protocol to detect single, SNARE-mediated fusion events between liposomes and supported bilayers in microfluidic channels using polarized TIRFM, with single molecule sensitivity and ~15 msec time resolution. Lipid and soluble cargo release can be detected simultaneously. Liposome size, lipid diffusivity, and fusion pore properties are measured.
08:55
Visualizing Intracellular SNARE Trafficking by Fluorescence Lifetime Imaging Microscopy
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Cited by 5 •
2017
This protocol describes a new method allowing for the quantitative visualization of complex formation of SNARE proteins, based on Förster resonance energy transfer, and fluorescence lifetime imaging microscopy.
08:51
The Microscopy-Based Assay to Study and Analyze the Recycling Endosomes using SNARE Trafficking
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2022
Recycling endosomes are part of the endosomal tubular network. Here we present a method to quantify the dynamics of recycling endosomes using GFP-STX13 as an organelle marker.
FAQs
Fusion depends on the V-SNARE recognizing complementary T-SNAREs on the target membrane. Their coiled-coil domains assemble into a stable four-helix bundle, which brings the two lipid bilayers into close proximity. This molecular rearrangement supplies the central mechanical step that allows the vesicle membrane and target membrane to merge rather than merely contact one another.
Complementarity helps direct a transport vesicle toward the correct destination instead of allowing fusion with an arbitrary membrane. Because the V-SNARE pairs with target-membrane T-SNAREs, the resulting fusion event occurs at a defined compartment. This selectivity supports intracellular organization and helps preserve the distinct identities of cellular organelles.
Coiled-coil domains provide the structural interface through which V-SNAREs and T-SNAREs assemble into a four-helix bundle. As this bundle forms, it draws the vesicle and target membranes together. Their role is therefore more than recognition: the domains convert SNARE pairing into the close membrane apposition required for fusion.
The vesicle first approaches its target membrane, where its V-SNARE encounters complementary T-SNAREs. The SNARE proteins then assemble their coiled-coil domains into a tight four-helix bundle. Membrane proximity increases until fusion occurs, allowing the vesicle contents to enter the target compartment or, in secretory pathways, the extracellular space.
V-SNARE-mediated transport contributes to neurotransmitter release, hormone secretion, membrane recycling, and protein transport. In each case, the fusion step determines how vesicle cargo reaches a destination or exits the cell. These examples connect the molecular pairing mechanism to communication between cells, secretion, membrane maintenance, and movement of proteins within the cell.
V-SNARE activity links cargo delivery to membrane specificity. Pairing with complementary T-SNAREs restricts fusion to the appropriate target membrane, so vesicle contents are delivered to the intended compartment. This selective trafficking helps preserve differences among organelles while supporting broader membrane dynamics, including recycling and the movement of proteins through intracellular pathways.