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The Journal of Neuroscience, January 1, 2000, 20(1):89-102

Control of GluR1 AMPA Receptor Function by cAMP-Dependent Protein Kinase

T. G. Banke1, 2, D. Bowie1, H.-K. Lee3, R. L. Huganir3, A. Schousboe2, and S. F. Traynelis1

1 Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia 30322, 2 Department of Pharmacology, Royal Danish School of Pharmacy, Copenhagen, Denmark DK-2100, and 3 Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Modulation of postsynaptic AMPA receptors in the brain by phosphorylation may play a role in the expression of synaptic plasticity at central excitatory synapses. It is known from biochemical studies that GluR1 AMPA receptor subunits can be phosphorylated within their C terminal by cAMP-dependent protein kinase A (PKA), which is colocalized with the phosphatase calcineurin (i.e., phosphatase 2B). We have examined the effect of PKA and calcineurin on the time course, peak open probability (PO,PEAK), and single-channel properties of glutamateevoked responses for neuronal AMPA receptors and homomeric GluR1(flip) receptors recorded in outside-out patches. Inclusion of purified catalytic subunit Calpha -PKA in the pipette solution increased neuronal AMPA receptor PO,PEAK (0.92) compared with recordings made with calcineurin included in the pipette (PO,PEAK 0.39). Similarly, Calpha -PKA increased PO,PEAK for recombinant GluR1 receptors (0.78) compared with patches excised from cells cotransfected with a cDNA encoding the PKA peptide inhibitor PKI (PO,PEAK 0.50) or patches with calcineurin included in the pipette (PO,PEAK 0.42). Neither PKA nor calcineurin altered the amplitude of single-channel subconductance levels, weighted mean unitary current, mean channel open period, burst length, or macroscopic response waveform for recombinant GluR1 receptors. Substitution of an amino acid at the PKA phosphorylation site (S845A) on GluR1 eliminated the PKA-induced increase in PO,PEAK, whereas the mutation of a Ca2+,calmodulin-dependent kinase II and PKC phosphorylation site (S831A) was without effect. These results suggest that AMPA receptor peak response open probability can be increased by PKA through phosphorylation of GluR1 Ser845.

Key words: AMPA receptors; glutamate; LTD; PKA; calcineurin; open probability; GluR1

Copyright © 2000 Society for Neuroscience  0270-6474/0/20189-14$05.00/0


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