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Título: | LTP requires a unique postsynaptic SNARE fusion machinery |
Autor: | Jurado, Sandra CSIC ORCID; Goswami, Debanjan; Zhang, Yingsha; Miñano Molina, Alfredo J.; Südhof, Thomas C.; Malenka, Robert C. | Fecha de publicación: | 2013 | Editor: | Elsevier | Citación: | Neuron 77(3): 542-558 (2013) | Resumen: | Membrane fusion during exocytosis is mediated by assemblies of SNARE (soluble NSF-attachment protein receptor) and SM (Sec1/Munc18-like) proteins. The SNARE/SM proteins involved in vesicle fusion during neurotransmitter release are well understood, whereas little is known about the protein machinery that mediates activity-dependent AMPA receptor (AMPAR) exocytosis during long-term potentiation (LTP). Using direct measurements of LTP in acute hippocampal slices and an in vitro LTP model of stimulated AMPAR exocytosis, we demonstrate that the Q-SNARE proteins syntaxin-3 and SNAP-47 are required for regulated AMPAR exocytosis during LTP but not for constitutive basal AMPAR exocytosis. In contrast, the R-SNARE protein synaptobrevin-2/VAMP2 contributes to both regulated and constitutive AMPAR exocytosis. Both the central complexin-binding and the N-terminal Munc18-binding sites of syntaxin-3 are essential for its postsynaptic role in LTP. Thus, postsynaptic exocytosis of AMPARs during LTP is mediated by a unique fusion machinery that is distinct from that used during presynaptic neurotransmitter release. | Versión del editor: | https://doi.org/10.1016/j.neuron.2012.11.029 | URI: | http://hdl.handle.net/10261/308994 | DOI: | 10.1016/j.neuron.2012.11.029 | ISSN: | 0896-6273 |
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