Extensive phosphorylation of AMPA receptors in neurons

Graham H. Diering, Seok Heo, Natasha K. Hussain, Bian Liu, Richard L. Huganir

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


Regulation of AMPA receptor (AMPAR) function is a fundamental mechanism controlling synaptic strength during long-term potentiation/depression and homeostatic scaling. AMPAR function and membrane trafficking is controlled by protein-protein interactions, as well as by posttranslational modifications. Phosphorylation of the GluA1 AMPAR subunit at S845 and S831 play especially important roles during synaptic plasticity. Recent controversy has emerged regarding the extent to which GluA1 phosphorylation may contribute to synaptic plasticity. Here we used a variety of methods to measure the population of phosphorylated GluA1-containing AMPARs in cultured primary neurons and mouse forebrain. Phosphorylated GluA1 represents large fractions from 12% to 50% of the total population under basal and stimulated conditions in vitro and in vivo. Furthermore, a large fraction of synapses are positive for phospho-GluA1-containing AMPARs. Our results support the large body of research indicating a prominent role of GluA1 phosphorylation in synaptic plasticity.

Original languageEnglish (US)
Pages (from-to)E4920-E4927
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number33
StatePublished - Aug 16 2016


  • AMPA receptor
  • Excitatory synapse
  • Protein kinase A
  • Protein kinase C
  • Synaptic plasticity

ASJC Scopus subject areas

  • General


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