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- W5032022 abstract "Secretion in all eukaryotic cells involves a family of proteins known as SNAREs (soluble Nethylmaleimide‐sensitive factor attachment protein receptors). In the nervous system, theseproteins are the main molecular constituents of the synaptic vesicle fusion machinery. The release of molecules contained inside exocytic granules and synaptic vesicles is mediated bythe assembly of a four helix bundle complex: the SNARE complex. It is formed by the coilcoiling of three proteins: the v‐SNARE VAMP/Synaptobrevin and the t‐SNAREs, Syntaxin andSNAP‐25 (synaptosome‐associated protein of 25 kDa). A cooperative interaction between SNARE complexes has been suggested to be necessary for the fusion of a synaptic vesiclewith the presynaptic membrane to occur. Previous experiments, made with botulinum neurotoxins type A and E on mouse neuromuscular junction, led to predict a central role of the SNAP‐25 C‐terminus in protein‐protein contacts between SNARE complexes. Previously conducted sequence comparisons and molecular dynamics simulations, led to the finding that this central role in such interactions could be played by a key Arginine residue at the SNAP‐25 C‐terminus. In particular, the SNAP‐25 Arg206 residue possibly forms an ionic bond with a negative charge amino acid of Syntaxin from an adjacent SNARE complex. A computational model, based on such interactions, proposes that the formation of the vesicle/presynaptic membrane fusion pore is catalyzed by a SNARE supercomplex consisting in a ten petal rosette. This prediction was tested in Drosophila melanogaster by altering the putative key amino acids, thought to be involved in rosette formation, by site‐directed mutagenesis. Two transgenic lines (harboring the mutation bearing constructs in a SNAP‐25 wild‐type background) were thus generated: UAS‐SNAP‐25WT (control) and UAS‐SNAP‐25R206A. Using the UAS/GAL4 system the expression of these constructs was directed specifically in the nervous system. The mRNA expression profiles, the locomotor behaviour and the morphology of the neuromuscular junction of these mutants were characterized in third instar larvae. Electrophysiological recordings performed at the larval neuromuscular junction showed that the ElavALl4/UAS‐SNAP‐25R206A mutants present a decrease in the probability of vesicle fusion as compared to ElavGAL4/UAS‐SNAP‐25WT, our control, in both spontaneous and evoked exocytosis. These findings highlight the key role of Arg206 and support the model entailing the involvement of a rosette of SNARE complexes in the process of neuroexocytosis." @default.
- W5032022 created "2016-06-24" @default.
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- W5032022 date "2011-01-26" @default.
- W5032022 modified "2023-09-27" @default.
- W5032022 title "SNARE complexes associate in a rosette-like structure at the Drosophila neuromuscular junction" @default.
- W5032022 hasPublicationYear "2011" @default.
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