Abstract
The possibility that membrane fusion events in the postsynaptic cell may be required for the change in synaptic strength resulting from long-term potentiation (LTP) was examined. Introducing substances into the postsynaptic cell that block membrane fusion at a number of different steps reduced LTP. Introducing SNAP, a protein that promotes membrane fusion, into cells enhanced synaptic transmission, and this enhancement was significantly less when generated in synapses that expressed LTP. Thus, postsynaptic fusion events, which could be involved either in retrograde signaling or in regulating postsynaptic receptor function or both, contribute to LTP.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Botulinum Toxins / pharmacology
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Carrier Proteins / metabolism
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Carrier Proteins / pharmacology
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Ethylmaleimide / pharmacology
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Excitatory Postsynaptic Potentials
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Exocytosis
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Guinea Pigs
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Hippocampus / drug effects
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Hippocampus / physiology*
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In Vitro Techniques
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Long-Term Potentiation* / drug effects
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Membrane Fusion*
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Membrane Proteins / metabolism
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Membrane Proteins / pharmacology
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Molecular Sequence Data
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N-Ethylmaleimide-Sensitive Proteins
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Patch-Clamp Techniques
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Peptides / pharmacology
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Pyramidal Cells / physiology
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Receptors, N-Methyl-D-Aspartate / physiology
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Recombinant Proteins / pharmacology
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Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Synaptic Membranes / physiology*
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Synaptic Transmission
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Vesicular Transport Proteins*
Substances
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Carrier Proteins
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Membrane Proteins
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Peptides
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Receptors, N-Methyl-D-Aspartate
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Recombinant Proteins
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Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Vesicular Transport Proteins
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Botulinum Toxins
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N-Ethylmaleimide-Sensitive Proteins
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Ethylmaleimide