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Journal of Neuroscience, Vol 14, 1123-1129, Copyright © 1994 by Society for Neuroscience
Phosphorylation of AMPA-type glutamate receptors by calcium/calmodulin- dependent protein kinase II and protein kinase C in cultured hippocampal neurons
SE Tan, RJ Wenthold and TR Soderling
Vollum Institute, Oregon Health Sciences University, Portland 97201.
Phosphorylation of glutamate receptors (GluRs) is emerging as an important
regulatory mechanism. In this study 32P labeling of non-NMDA GluRs was
investigated in cultured hippocampal neurons stimulated 2-15 min with
agonists that selectively stimulate either Ca2+/calmodulin- dependent
protein kinase II (CaM-kinase II), Ca2+/phospholipid- dependent protein
kinase C (PKC), or cAMP-dependent protein kinase A (PKA). Treatment of
hippocampal neurons with glutamate/glycine (Glu/Gly), ionomycin, or
12-O-tetradecanoylphorbol 13-acetate (TPA) increased 32P labeling of
immunoprecipitated alpha-amino-3-hydroxy-5- methyl-4-isoxazoleproprionate
(AMPA)-type GluRs by 145%, 180%, and 227%, respectively, of control values.
This increased phosphorylation of GluRs was predominantly 32P-Ser with
little 32P-Thr and no detectable 32P-Tyr. Glu/Gly and ionomycin, but not
TPA, also increased 32P labeling of CaM-kinase II by 175% and 195%,
respectively, of control values. Of these three agonists, only TPA
stimulated phosphorylation of MARCKS (225% of control), a specific
substrate of PKC. Forskolin treatment gave a three- to fourfold increase in
the active catalytic subunit of PKA but did not result in the 32P labeling
of AMPA-type GluRs, CaM-kinase II, or MARCKS. Phosphorylation of GluRs in
response to Glu/Gly was blocked by a specific NMDA receptor/ion channel
antagonist (DL-2-amino-5-phosphonovaleric acid) or by a cell- permeable
inhibitor of CaM-kinase II (1-[N,O-bis(1,5-
isoquinolinesulfonyl)-N-methyl-L-tyrosyl]-4- phenylpiperazine, KN-62).
These results are consistent with the hypothesis that Ca2+ influx through
the NMDA-type ion channel can activate CaM-kinase II, which in turn can
phosphorylate and regulate AMPA-type GluR ion channels (McGlade-McCulloh et
al., 1993).(ABSTRACT TRUNCATED AT 250 WORDS)
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