synaptobrevin , VAMP (skrót)

Complexin binds to the groove between the synaptobrevin and syntaxin helices.

Proteins such as synaptotagmin and synaptobrevin interact to fuse the vesicle into the membrane.

Complexin promotes interaction of the transmembrane regions of syntaxin and synaptobrevin.

The Tetanus toxin follows a similar pathway, but instead attacks the protein synaptobrevin on the synaptic vesicle.

Synaptobrevin is degraded by tetanospasmin, a protein derived from the bacterium Clostridium tetani, which causes tetanus.

A related bacterium, Clostridium botulinum, produces botulinum toxin that also hydrolyzes synaptobrevin.

EGR-1 has also been found to regulate the expression of synaptobrevin II (a protein important for synaptic exocytosis).

Vesicle-associated membrane protein 5 also known as VAMP5 is a human gene which encodes a member of the synaptobrevin protein family.

One particular R-SNARE is synaptobrevin, which is located in the synaptic vesicles.

Tetanospasmin appears to prevent the release of neurotransmitters by selectively cleaving a component of synaptic vesicles called synaptobrevin II.

Synaphin promotes neuronal exocytosis by promoting interaction between the complementary syntaxin and synaptobrevin transmembrane regions that reside in opposing membranes prior to fusion.

Synaptobrevin and syntaxin contribute one -helix each, while SNAP-25 participates with two -helices (abbreviated as Sn1 and Sn2).

By exploiting the rapid change in pH upon synaptic vesicle fusion, pHluorins tagged to synaptobrevin have been used to visualize synaptic activity in neurons.

Synaptobrevin is one of the SNARE proteins involved in formation of the SNARE complexes.

The action of the A-chain stops the affected neurons from releasing the inhibitory neurotransmitters GABA (gamma-aminobutyric acid) and glycine by degrading the protein synaptobrevin.

The toxin appears to act by selective cleavage of a protein component of synaptic vesicles, synaptobrevin II, and this prevents the release of neurotransmitters by the cells.

The VAMP5 gene is a member of the vesicle-associated membrane protein (VAMP)/synaptobrevin family and the SNARE superfamily.

SNAP-25 is a Q-SNARE protein contributing two α-helices in the formation of the exocytotic fusion complex in neurons where it assembles with syntaxin-1 and synaptobrevin.

The SNARE (H3) domain binds to both synaptobrevin and SNAP-25 forming the core SNARE complex.

Südhof was also responsible for elucidating the action of tetanus and botulinum toxins, which selectively cleave synaptobrevin and SNAP-25, respectively, inhibiting vesicle fusion with the presynaptic membrane.

Out of four α-helices of the core SNARE complex one is contributed by synaptobrevin, one by syntaxin, and two by SNAP-25 (in neurons).

In neuronal exocytosis, syntaxin and synaptobrevin are anchored in respective membranes by their C-terminal domains, whereas SNAP-25 is tethered to the plasma membrane via several cysteine-linked palmitoyl chains.

The exact function of the protein is unknown: it interacts with the essential synaptic vesicle protein synaptobrevin, but when the synaptophysin gene is experimentally inactivated in animals, they still develop and function normally.

This light chain is an enzyme (a protease) that attacks one of the fusion proteins (SNAP-25, syntaxin or synaptobrevin) at a neuromuscular junction, preventing vesicles from anchoring to the membrane to release acetylcholine.

Formation of the "trans"-SNARE complex proceeds through an intermediate complex composed of SNAP-25 and syntaxin-1, which later accommodates synaptobrevin-2 (the quoted syntaxin and synaptobrevin isotypes participate in neuronal neuromediator release).