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• W2798840558 abstract "Regulated secretion is an essential process in alleukaryotic cells. The release of molecules containedinside exocytic granules and synaptic vesicles ismediated by the assembly of a SNARE complex formedby the coil-coiling of three proteins: SNAP-25, syntaxinand VAMP/synaptobrevin. It seems that SNAREcomplexes assemble together in rosette-shaped super-complexes but there is controversy on the actualnumber (N) of copies of SNARE complexes that arenecessary to mediate exocytosis. We discuss attemptsto determine the value of N and suggest that N varieswith the type of exocytic vesicles. In addition, wepropose that the N value in neuroexocytosis can beestimated by the comparative use of different types ofbotulinum neurotoxins.IntroductionNeuroexocytosis is the fundamental physiological processthat leads a nai¨ve cytosolic synaptic vesicle (SV) to bind toand fuse with the presynaptic membrane, therebydischarging its neurotransmitter contents into the syn-aptic cleft. Our interest in neuroexocytosis arose some20 years ago when we began to study the mechanism ofaction of the clostridial neurotoxins causing tetanus andbotulism. Meanwhile, an unprecedented wealth of infor-mation brought the field from the static, low-resolutionpicture provided by electron microscopy to the tantalizingmolecular and biophysical puzzle that is currentlyavailable. At present, many scientists are trying topinpoint the right place and time of action for the manymolecules that are suggested to be linked, in one way oranother, to neuroexocytosis.The three synaptic SNARE proteins SNAP-25, VAMP/synaptobrevin and syntaxin occupy a central position inthis process by forming a heterotrimeric complex, whichbinds N-ethylmaleimide sensitive fusion ATPase (NSF)and soluble NSF attachment protein [a-SNAP; hence theacronym SNARE (SNAP receptor)] [1]. The synapticSNARE proteins are the specific substrates of the eightclostridial neurotoxins (one tetanus neurotoxin, TeNT,and seven botulinum neurotoxins: BoNT/A–G) [2,3].These neurotoxins specifically bind to nerve terminalsand deliver their zinc-endopeptidase N-terminal domaininside the cytosol, where it specifically cleaves a SNAREprotein at a single site within its cytosolic portion. Suchspecific cleavage leads to a prolonged, but eventuallyreversible, inhibition of neuroexocytosis, which in vivoresults in the paralytic syndromes of botulism andtetanus. Despite the availability of several pieces ofexperimental evidence demonstrating the involvement ofSNAREproteinsinneuroexocytosis,andinthemajorityofmembrane traffic events within eukaryotic cells [4,5], thisremains the most impressive proof of their central role inneuroexocytosis; and a badly unwanted one, if oneconsiders the hundreds of thousands of newborn babiesthattheWHOreportstodieeachyearbytetanusneonatorum in the non tetanus-vaccinated areas of theworld [6].There is evidence that SNARE complexes assembletogether in rosette super-complexes around the site ofmembrane fusion. Additional proteins, including thecalcium sensor synaptotagmin I and the syntaxin-inter-acting protein Munc-18 [5,7,8], cooperate with SNAREs toaccomplish neuroexocytosis, although their completenumber and precise mode- and time-of-action has not yetbeen established [5,7,8]. In addition, the number of copiesof SNARE complexes, termed N, that are necessary tomediate exocytosis is not known. Different methodsprovide different estimates and we discuss here someattempts at determining the value of N and the possibilitythat N varies with the type of exocytosis event. We willconcludebyproposingtheuseofdifferenttypesofBoNTtoestimate the N value in neuroexocytosis.The neuronal SNARE complexDespitethelargerepertoireofSNAREsthatarepresentina typical mammalian cell (up to 26 have been identified inbudding yeast) [9], only a few of them are involved in therapid, highly controlled release of the neurotransmitter-containing vesicles, which follows nerve membranedepolarization. This event enables the influx of calciumthrough calcium channels located near the ‘active zones’,which are the preferred sites of neuroexocytosis [5,7].VAMP/synaptobrevin 1 and 2 (here abbreviated asVAMP) are 13 kDa integral membrane proteins of SVandof large dense-core granules. They consist of four parts" @default.
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• W2798840558 date "2005-01-01" @default.
• W2798840558 modified "2023-09-23" @default.
• W2798840558 title "SNAREcomplexesandneuroexocytosis: how many, how close?" @default.
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