| First Author | Jurado S | Year | 2013 |
| Journal | Neuron | Volume | 77 |
| Issue | 3 | Pages | 542-58 |
| PubMed ID | 23395379 | Mgi Jnum | J:197846 |
| Mgi Id | MGI:5494785 | Doi | 10.1016/j.neuron.2012.11.029 |
| Citation | Jurado S, et al. (2013) LTP requires a unique postsynaptic SNARE fusion machinery. Neuron 77(3):542-58 |
| abstractText | 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. |
