Characterization of multiple phosphorylation sites on the AMPA receptor GluR1 subunit.
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.
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- Receptors, AMPA
- Phosphorylation
- Neurology & Neurosurgery
- Molecular Sequence Data
- Membrane Potentials
- Humans
- Gene Expression
- Cells, Cultured
- Amino Acid Sequence
- 5202 Biological psychology
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Receptors, AMPA
- Phosphorylation
- Neurology & Neurosurgery
- Molecular Sequence Data
- Membrane Potentials
- Humans
- Gene Expression
- Cells, Cultured
- Amino Acid Sequence
- 5202 Biological psychology