Abstract
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.
Publication types
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Research Support, N.I.H., Intramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Axons / physiology
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Cell Line
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Cell Membrane / metabolism
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Dendrites / physiology
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Dendritic Spines / physiology
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Hippocampus / physiology
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Humans
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In Vitro Techniques
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Membrane Potentials / physiology
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Mice
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Mice, Transgenic
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Neurons / physiology*
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Qb-SNARE Proteins / genetics
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Qb-SNARE Proteins / metabolism*
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Qc-SNARE Proteins / genetics
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Qc-SNARE Proteins / metabolism*
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Rats
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Rats, Sprague-Dawley
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Receptors, Glutamate / metabolism*
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Receptors, N-Methyl-D-Aspartate / metabolism
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Synapses / physiology*
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Synaptosomal-Associated Protein 25 / genetics
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Synaptosomal-Associated Protein 25 / metabolism
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Vesicular Transport Proteins / genetics
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Vesicular Transport Proteins / metabolism*
Substances
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Qb-SNARE Proteins
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Qc-SNARE Proteins
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Receptors, Glutamate
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Receptors, N-Methyl-D-Aspartate
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Snap23 protein, mouse
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Snap23 protein, rat
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Snap25 protein, mouse
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Snap25 protein, rat
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Synaptosomal-Associated Protein 25
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Vesicular Transport Proteins