Abstract
The NMDA receptor activates a biochemical pathway that regulates long-term changes in synaptic strength. A combination of pharmacological and gene-knockout approaches shows that the postsynaptics signalling cascade initiated by the NMDA receptor involves Fyn tyrosine kinase. We found that Fyn phosphorylates the NMDA receptor and proteins associated with the receptor and proteins associated with the receptor. The interaction of the NMDA receptor with postsynaptic signalling proteins is likely to initiate changes in synaptic strength that contribute to learning and memory.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cell Adhesion Molecules / genetics
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Cell Adhesion Molecules / metabolism
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Cell Adhesion Molecules / physiology*
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Focal Adhesion Kinase 1
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Focal Adhesion Protein-Tyrosine Kinases
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Mice
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Mice, Knockout
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Neuronal Plasticity / physiology*
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Phosphorylation
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Phosphotyrosine / metabolism
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Protein-Tyrosine Kinases / genetics
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Protein-Tyrosine Kinases / metabolism
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Protein-Tyrosine Kinases / physiology*
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Proto-Oncogene Proteins / deficiency
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Proto-Oncogene Proteins / genetics
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Proto-Oncogene Proteins / physiology*
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Proto-Oncogene Proteins c-fyn
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Receptors, N-Methyl-D-Aspartate / physiology*
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Synapses / physiology*
Substances
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Cell Adhesion Molecules
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Proto-Oncogene Proteins
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Receptors, N-Methyl-D-Aspartate
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Phosphotyrosine
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Protein-Tyrosine Kinases
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Focal Adhesion Kinase 1
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Focal Adhesion Protein-Tyrosine Kinases
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Fyn protein, mouse
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Proto-Oncogene Proteins c-fyn
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Ptk2 protein, mouse