Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Roche, KW; O'Brien, RJ; Mammen, AL; Bernhardt, J; Huganir, RL

Published Date

  • June 1996

Published In

Volume / Issue

  • 16 / 6

Start / End Page

  • 1179 - 1188

PubMed ID

  • 8663994

Pubmed Central ID

  • 8663994

International Standard Serial Number (ISSN)

  • 0896-6273

Language

  • eng

Conference Location

  • United States