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A neuronal role for SNAP-23 in postsynaptic glutamate receptor trafficking.

Regulated exocytosis is essential for many biological processes and many components of the protein trafficking machinery are ubiquitous. However, there are also exceptions, such as SNAP-25, a neuron-specific SNARE protein that is essential for synaptic vesicle release from presynaptic nerve terminals. In contrast, SNAP-23 is a ubiquitously expressed SNAP-25 homolog that is critical for regulated exocytosis in non-neuronal cells. However, the role of SNAP-23 in neurons has not been elucidated. We found that SNAP-23 was enriched in dendritic spines and colocalized with constituents of the postsynaptic density, whereas SNAP-25 was restricted to axons. In addition, loss of SNAP-23 using genetically altered mice or shRNA targeted to SNAP-23 led to a marked decrease in NMDA receptor surface expression and NMDA receptor currents, whereas loss of SNAP-25 did not. SNAP-23 is therefore important for the functional regulation of postsynaptic glutamate receptors.

Pubmed ID: 20118925


  • Suh YH
  • Terashima A
  • Petralia RS
  • Wenthold RJ
  • Isaac JT
  • Roche KW
  • Roche PA


Nature neuroscience

Publication Data

March 23, 2010

Associated Grants

  • Agency: Intramural NIH HHS, Id: NIH0012309351
  • Agency: Intramural NIH HHS, Id: ZIA BC009404-08
  • Agency: Intramural NIH HHS, Id: ZIA BC011035-02
  • Agency: Intramural NIH HHS, Id: ZIA NS002994-08

Mesh Terms

  • Animals
  • Axons
  • Cell Line
  • Cell Membrane
  • Dendrites
  • Dendritic Spines
  • Hippocampus
  • Humans
  • In Vitro Techniques
  • Membrane Potentials
  • Mice
  • Mice, Transgenic
  • Neurons
  • Qb-SNARE Proteins
  • Qc-SNARE Proteins
  • Rats
  • Rats, Sprague-Dawley
  • Receptors, Glutamate
  • Receptors, N-Methyl-D-Aspartate
  • Synapses
  • Synaptosomal-Associated Protein 25
  • Vesicular Transport Proteins