Phosphorylation of Serine‐880 in GluR2 by Protein Kinase C Prevents Its C Terminus from Binding with Glutamate Receptor‐Interacting Protein

@article{Matsuda1999PhosphorylationOS,
  title={Phosphorylation of Serine‐880 in GluR2 by Protein Kinase C Prevents Its C Terminus from Binding with Glutamate Receptor‐Interacting Protein},
  author={Shinji Matsuda and Sumiko Mikawa and Hirokazu Hirai},
  journal={Journal of Neurochemistry},
  year={1999},
  volume={73}
}
Abstract : Phosphorylation of the glutamate receptor is an important mechanism of synaptic plasticity. Here, we show that the C terminus of GluR2 of the α‐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… 
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