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 RIS Download
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