Phosphorylation of Serine-880 in GluR2 by Protein Kinase C Prevents Its C Terminus from Binding with Glutamate Receptor-Interacting Protein |
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Authors: | Shinji Matsuda,Sumiko Mikawa,& Hirokazu Hirai |
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Affiliation: | Laboratory for Memory and Learning, RIKEN Brain Science Institute, Saitama, Japan. |
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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. |
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Keywords: | GluR2 Glutamate receptor-interacting protein GRIP Phosphorylation Protein kinase C Synaptic plasticity Receptor clustering |
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