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The Journal of Neuroscience, March 1, 2001, 21(5):1501-1509
Hippocampal Synaptic Plasticity Involves Competition between
Ca2+/Calmodulin-Dependent Protein Kinase II and
Postsynaptic Density 95 for Binding to the NR2A Subunit of the NMDA
Receptor
F.
Gardoni1,
L. H.
Schrama2,
A.
Kamal2,
W. H.
Gispen2,
F.
Cattabeni1, and
M.
Di
Luca1
1 Institute of Pharmacological Sciences, University of
Milan, 20133 Milan, Italy, and 2 Medical Pharmacology,
Rudolf Magnus Institute of Neuroscience, University of
Utrecht, 3584 CG Utrecht, The Netherlands
NMDA receptor, Ca2+/calmodulin-dependent
protein kinase II ( CaMKII), and postsynaptic density 95 (PSD-95) are
three major components of the PSD fraction. Both CaMKII and PSD-95
have been shown previously to bind NR2 subunits of the NMDA receptor
complex. The nature and mechanisms of targeting to the NMDA receptor
subunits are, however, not completely understood. Here we report that
the C-terminal NR2A(S1389-V1464) sequence was sufficient to guarantee
the association of both native and recombinant CaMKII and PSD-95.
PSD-95(54-256) was able to compete with the binding of both native and
recombinant CaMKII to the NR2A C-tail. Accordingly,
CaMKII(1-325) competes with both the native PSD-95 and the native
kinase itself for the binding to NR2A. In addition, Ser/Ala1289 and
Ser/Asp1289 point mutations on the unique CaMKII phosphosite of NR2A
did not significantly influence the binding of native CaMKII and
PSD-95 to the NR2A C-tail. Finally, the association-dissociation of
CaMKII and PSD-95 to and from the NR2A C-tail was significantly
modulated by activation of NMDA receptor achieved by either
pharmacological tools or long-term potentiation induction, underlining
the importance of dynamic and reciprocal interactions of NMDA receptor,
CaMKII, and PSD-95 in hippocampal synaptic plasticity.
Key words:
CaMKII; LTP; NMDA; postsynaptic density; PSD-95; synaptic plasticity
Copyright © 2001 Society for Neuroscience 0270-6474/01/2151501-09$05.00/0
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