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

Research output: Contribution to journalArticle

221 Citations (Scopus)

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-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.

Original languageEnglish
Pages (from-to)1765-1768
Number of pages4
JournalJournal of Neurochemistry
Volume73
Issue number4
DOIs
Publication statusPublished - 1999 Sep 28
Externally publishedYes

Keywords

  • GRIP
  • GluR2
  • Glutamate receptor-interacting protein
  • Phosphorylation
  • Protein kinase C
  • Receptor clustering
  • Synaptic plasticity

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

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