Abstract
Phosphorylation of the glutamate receptor is an important mechanism of synaptic plasticity. Here, we show that the C terminus of GluR2 of the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptor is phosphorylated by protein kinase C and that serine-880 is the major phosphorylation site. This phosphorylation also occurs in human embryonic kidney (HEK) cells by addition of 12-O-tetradecanoylphorbol 13-acetate. Our immunoprecipitation experiment revealed that the phosphorylation of serine-880 in GluR2 drastically reduced the affinity for glutamate receptor-interacting protein (GRIP), a synaptic PDZ domain-containing protein, in vitro and in HEK cells. This result suggests that modulation of serine-880 phosphorylation in GluR2 controls the clustering of AMPA receptors at excitatory synapses and consequently contributes to synaptic plasticity.
MeSH terms
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Amino Acid Sequence
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Antibodies
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Binding Sites
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism*
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Cell Line
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Humans
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Immunoblotting
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry
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Nerve Tissue Proteins / metabolism*
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Peptide Fragments / chemistry
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Peptide Fragments / immunology
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Phosphorylation
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Phosphoserine / metabolism
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Protein Kinase C / metabolism*
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Receptors, AMPA / metabolism
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Receptors, Metabotropic Glutamate / chemistry
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Receptors, Metabotropic Glutamate / genetics
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Receptors, Metabotropic Glutamate / metabolism*
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Serine*
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Synapses / physiology
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Transfection
Substances
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Antibodies
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Carrier Proteins
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GRIP1 protein, human
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Nerve Tissue Proteins
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Peptide Fragments
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Receptors, AMPA
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Receptors, Metabotropic Glutamate
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Recombinant Proteins
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metabotropic glutamate receptor 2
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Phosphoserine
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Serine
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Protein Kinase C