Identification and characterization of a novel phosphorylation site on the GluR1 subunit of AMPA receptors

Hey Kyoung Lee, Kogo Takamiya, Kimihiko Kameyama, Kaiwen He, Sandy Yu, Luciano Rossetti, David Wilen, Richard L. Huganir

Research output: Contribution to journalArticlepeer-review

Abstract

Phosphorylation of various AMPA receptor subunits can alter synaptic transmission and plasticity at excitatory glutamatergic synapses in the central nervous system. Here, we identified threonine-840 (T840) on the GluR1 subunit of AMPA receptors as a novel phosphorylation site. T840 is phosphorylated by protein kinase C (PKC) in vitro and is a highly turned-over phosphorylation site in the hippocampus. Interestingly, the high basal phosphorylation of T840 in the hippocampus is maintained by a persistent activity of a protein kinase, which is counter-balanced by a basal protein phosphatase activity. To study the function of T840, we generated a line of mutant mice lacking this phosphorylation site using a gene knock-in technique. The mice generated lack T840, in addition to two previously identified phosphorylation sites S831 and S845. Using this mouse, we demonstrate that T840 may regulate synaptic plasticity in an age-dependent manner.

Original languageEnglish (US)
Pages (from-to)86-94
Number of pages9
JournalMolecular and Cellular Neuroscience
Volume36
Issue number1
DOIs
StatePublished - Sep 2007

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience
  • Cell Biology

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