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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 C -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, C-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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H.-X. Chen and S. N. Roper
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S. F. Oliveria, L. L. Gomez, and M. L. Dell'Acqua
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