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. 2014 Dec 22;8:407. doi: 10.3389/fncel.2014.00407

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Copyright © 2014 Jurado.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution and reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Postsynaptic SNARE complex involved in AMPARs insertion during LTP. Top panel represents dendritic SNARE proteins involved in constitutive trafficking of NMDARs and AMPARs. SNAP-25 is depicted as membrane-bound regulating constitutive NMDARs exocytosis whereas the vesicle SNARE synaptobrevin-2 (Syb-2) may be an integral component of both AMPARs and NMDARs-containing endosomes. Bottom panel illustrates the formation of a specific postsynaptic SNARE complex involved in AMPARs exocytosis upon NMDAR activation. SNAP-47 is shown in close proximity to syntaxin-3 which is anchored to the plasma membrane in an open conformation by its interaction with an unknown postsynaptic SM protein. In a similar fashion to SNAP-25, Syb-2 is depicted regulating constitutive recycling of AMPARs. Plasma membrane-bound Syntaxin-3 molecules may constitute micro-domains or hot spots for exocytosis of AMPARs-containing endosomes during LTP. Calcium influx into the postsynaptic terminal promotes the assembly of a SNARE complex constituted by Stx-3, SNAP-47 and Syb-2, as well as complexin (not shown) and a postsynaptic synaptotagmin isoform (Syt-X) still to be identified.