Trans-snare Complex
Trans-snare Complex - 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.
03:21
Trans-Spinal Direct Current Stimulation of a Rat's Spinal Motoneuron
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2025
This video describes the in vivo intracellular recording of rat motoneurons under trans-spinal direct current stimulation. The protocol describes how to measure membrane properties and record the rhythmic firing of motoneurons before, during, and after anodal or cathodal polarization of the spinal cord.
11:49
Trans-vivo Delayed Type Hypersensitivity Assay for Antigen Specific Regulation
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Cited by 19 •
2013
We describe a valuable diagnostic assay that could potentially be used to decide the withdrawal of immunosuppression after transplant without elevated risk of graft rejection. The assay uses the principles of Delayed Type Hypersensitivity and provides accurate assessment of both donor specific effector and regulatory immune responses mounted by recipients.
FAQs
The parallel four-helix bundle formed by v-SNAREs and t-SNAREs draws the opposing bilayers progressively closer. This mechanical zippering reduces the membrane gap and promotes bending of the bilayers. As the membranes deform, they can proceed through hemifusion, in which the outer leaflets connect, toward formation of a fusion pore that permits cargo delivery.
Trans-SNARE assembly is linked to a sequence of membrane remodeling events rather than an immediate opening. The closely apposed bilayers first undergo bending, followed by hemifusion and then fusion-pore formation. These transitions change the membranes from separate compartments into a continuous membrane connection, allowing vesicle contents to pass into the target compartment.
The trans arrangement places complementary v-SNAREs and t-SNAREs on opposing membranes, allowing their interaction to exert force across the membrane gap. A bundle assembled in this configuration can pull the two bilayers together directly. This spatial organization explains how molecular binding is coupled to membrane apposition, bending, and eventual continuity.
Vesicle docking brings a vesicle into a productive relationship with its target membrane, whereas fusion requires the bilayers to bend, pass through hemifusion, and open a pore. The trans-SNARE complex helps connect these stages by mechanically drawing the membranes together. Studying it therefore clarifies how docking can progress toward cargo release and membrane continuity.
A useful conceptual sequence begins with complementary v-SNARE and t-SNARE binding across the membrane gap. Researchers can then relate four-helix-bundle formation to membrane apposition and zippering, followed by bilayer bending, hemifusion, and fusion-pore opening. Tracking these linked stages helps connect protein assembly with the physical outcomes of vesicle fusion.
This complex is relevant wherever vesicles deliver cargo by fusing with target membranes. The source specifically connects it with intracellular trafficking, secretion, neurotransmitter release, and hormone secretion. Its study can therefore link molecular membrane mechanics to rapid cellular communication, regulated cargo delivery, and the membrane-trafficking defects that disrupt these processes.