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(Received for publication, August 8, 1996, and in revised form, November 25, 1996)
From the Modulation of
N-methyl-D-aspartate receptors in the brain by
protein phosphorylation may play a central role in the regulation of
synaptic plasticity. To examine the phosphorylation of the NR1 subunit
of N-methyl-D-aspartate receptors in
situ, we have generated several polyclonal antibodies that
recognize the NR1 subunit only when specific serine residues are
phosphorylated. Using these antibodies, we demonstrate that protein
kinase C (PKC) phosphorylates serine residues 890 and 896 and
cAMP-dependent protein kinase (PKA) phosphorylates serine
residue 897 of the NR1 subunit. Activation of PKC and PKA together lead
to the simultaneous phosphorylation of neighboring serine residues 896 and 897. Phosphorylation of serine 890 by PKC results in the dispersion
of surface-associated clusters of the NR1 subunit expressed in
fibroblasts, while phosphorylation of serine 896 and 897 has no effect
on the subcellular distribution of NR1. The PKC-induced redistribution
of the NR1 subunit in cells occurs within minutes of serine 890 phosphorylation and reverses upon dephosphorylation. These results
demonstrate that PKA and PKC phosphorylate distinct residues within a
small region of the NR1 subunit and differentially affect the
subcellular distribution of the NR1 subunit.
Volume 272, Number 8,
Issue of February 21, 1997
pp. 5157-5166
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
Department of Neuroscience,
¶ Biopolymers Laboratory, Howard Hughes Medical Institute, The
Johns Hopkins University School of Medicine,
Baltimore, Maryland 21205
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