Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein

Shinji Matsuda, Sumiko Mikawa, Hirokazu Hirai

研究成果: Article査読

224 被引用数 (Scopus)

抄録

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-methyhsoxazole-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.

本文言語English
ページ(範囲)1765-1768
ページ数4
ジャーナルJournal of Neurochemistry
73
4
DOI
出版ステータスPublished - 1999 9 28
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 細胞および分子神経科学

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