The primary role of SNARE proteins is to mediate vesicle fusion – the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can mediate the fusion of vesicles with membrane-bound compartments .
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The primary role of SNARE proteins is to mediate vesicle fusion – the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can mediate the fusion of vesicles with membrane-bound compartments .
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Several SNARE proteins are located on both vesicles and target membranes, therefore, a more recent classification scheme takes into account structural features of SNAREs, dividing them into R-SNAREs and Q-SNAREs.
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One particular R-SNARE proteins is synaptobrevin, which is located in the synaptic vesicles.
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SNAREs are small, abundant, sometimes tail-anchored proteins which are often post-translationally inserted into membranes via a C-terminal transmembrane domain.
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SNARE proteins must assemble into trans-SNARE complexes to provide the force that is necessary for vesicle fusion.
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The SNARE proteins domains proceed in forming a coiled-coil motif in the direction of the C-termini of their respective domains.
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The unstable configuration of the TM domains eventually causes the two membranes to fuse and the SNARE proteins come together within the same membrane, which is referred to as a "cis"-SNARE complex.
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Energy input that is required for SNARE proteins-mediated fusion to take place comes from SNARE proteins-complex disassembly.
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The ATP hydrolysis-coupled dissociation of SNARE proteins complexes is an energy investment that can be compared to "cocking the gun" so that, once vesicle fusion is triggered, the process takes place spontaneously and at optimum velocity.
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Availability of SNAP-25 in the SNARE proteins complex is theorized to possibly be spatially regulated via localization of lipid microdomains in the target membrane.
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Conversely, the Habc domain can again disassociate with the SNARE proteins domain leaving syntaxin free to associate with both SNAP-25 and synaptobrevin.
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The light chain of BoNT acts as a metalloprotease on SNARE proteins that is dependent on Zn ions, cleaving them and eliminating their function in exocytosis.
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In each of these cases, Botulinum Neurotoxin causes functional damage to SNARE proteins, which has significant physiological and medical implications.
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Complexins stabilize the primed SNARE proteins-complex rendering the vesicles ready for rapid exocytosis.
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