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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/32618
Title: SNAP-25 Is a Target of Protein Kinase C Phosphorylation Critical to NMDA Receptor Trafficking
Authors: Lau, C. Geoffrey; Takayasu, Yukihiro; Rodenas-Ruano, Alma; Paternain, Ana V.; Lerma Gómez, Juan; Bennett, Michael V. L.; Zukin, R. Suzanne
Issue Date: 6-Jan-2010
Publisher: Society for Neuroscience
Citation: Journal of Neuroscience 3081): 242-254 (2010)
Abstract: Protein kinase C (PKC) enhances NMDA receptor (NMDAR)-mediated currents and promotes NMDAR delivery to the cell surface via SNARE-dependent exocytosis. Although the mechanisms of PKC potentiation are established, the molecular target of PKC is unclear. Here we show that synaptosomal-associated protein of 25 kDa (SNAP-25), a SNARE protein, is functionally relevant to PKC-dependent NMDAR insertion, and identify serine residue-187 as the molecular target of PKC phosphorylation. Constitutively active PKC delivered via the patch pipette potentiated NMDA (but not AMPA) whole-cell currents in hippocampal neurons. Expression of RNAi targeting SNAP-25 or mutant SNAP-25(S187A) and/or acute disruption of the SNARE complex by treatment with BoNT A, BoNT B or SNAP-25 C-terminal blocking peptide abolished NMDAR potentiation. A SNAP-25 peptide and function-blocking antibody suppressed PKC potentiation of NMDA EPSCs at mossy fiber-CA3 synapses. These findings identify SNAP-25 as the target of PKC phosphorylation critical to PKC-dependent incorporation of synaptic NMDARs and document a postsynaptic action of this major SNARE protein relevant to synaptic plasticity.
Description: 18 páginas, 8 figuras, 4 figuras suplementarias.
Publisher version (URL): http://dx.doi.org/10.1523/JNEUROSCI.4933-08.2010
URI: http://hdl.handle.net/10261/32618
ISSN: 0270-6474
DOI: 10.1523/JNEUROSCI.4933-08.2010
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