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Vol. 59, Issue 5, 960-964, May 2001
Laboratory of Integrative Neuroscience (G.-Y.L., D.A.W., M.H.H.,
J.P.L.) and Laboratory for Molecular Biology (D.A.W., J.P.L.),
Department of Biological Sciences, University of Illinois at Chicago,
Chicago, Illinois
Protein kinase-C (PKC) activation differentially affects currents from
N-methyl-D-aspartate (NMDA) type glutamate
receptors depending upon their subunit composition. Experiments using
chimeras initially indicated that the cytoplasmic C-terminal tails of
NR2B (responsive to PKC) and NR2C (unresponsive to PKC) subunits
contain the amino acid residues responsible for the observed disparity of PKC effects. However, truncation and point mutation experiments have
suggested that PKC action on NMDA receptors may be entirely indirect,
working via the phosphorylation of associated proteins. Here we suggest
that PKC does, in fact, affect NR2B/NR1-011 NMDA currents by direct
phosphorylation of the NR2B tail at residues S1303 and S1323.
Replacement of either of these residues with Ala severely reduces PKC
potentiation. To verify that S1303 and S1323 are sites of direct
phosphorylation by PKC, synthetic peptides from the regions surrounding
these sites were used as substrates for in vitro assays with purified
rat brain PKC. These results indicate that PKC can directly
phosphorylate S1303 and S1323 in the NR2B C terminus, leading to
enhanced currents through NMDA receptor channels. The direct action of
PKC on certain NMDA receptor subtypes may be important in any
physiological or pathological process where PKC and NR2B/NR1 receptors interact.
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