Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit

Katherine W. Roche, Richard J. O'Brien, Andrew L. Mammen, Jeffrey Bernhardt, Richard L. Huganir

Research output: Contribution to journalArticlepeer-review

Abstract

We have characterized the phosphorylation of the glutamate receptor subunit GluR1, using biochemical and electrophysiological techniques. GluR1 is phosphorylated on multiple sites that are all located on the C-terminus of the protein. Cyclic AMP-dependent protein kinase specifically phosphorylates SER-845 of GluR1 in transfected HEK cells and in neurons in culture. Phosphorylation of this residue results in a 40% potentiation of the peak current through GluR1 homomeric channels. In addition, protein kinase C specifically phosphorylates Ser-831 of GluR1 in HEK-293 cells and in cultured neurons. These results are consistent with the recently proposed transmembrane topology models of glutamate receptors, in which the C-terminus is intracellular. In addition, the modulation of GluR1 by PKA phosphorylation of Ser-845 suggests that phosphorylation of this residue may underlie the PKA-induced potentiation of AMPA receptors in neurons.

Original languageEnglish (US)
Pages (from-to)1179-1188
Number of pages10
JournalNeuron
Volume16
Issue number6
DOIs
StatePublished - Jun 1996

ASJC Scopus subject areas

  • Neuroscience(all)

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