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J Biol Chem, Vol. 273, Issue 33, 20689-20692, August 14, 1998
From the Department of Molecular Physiology and Biophysics and
Center for Molecular Neuroscience, Vanderbilt University Medical
Center, Nashville, Tennessee 37232-0615
Activation and Thr286
autophosphorylation of calcium/calmodulindependent kinase II
(CaMKII) following Ca2+ influx via
N-methyl-D-aspartate (NMDA)-type glutamate
receptors is essential for hippocampal long term potentiation (LTP), a
widely investigated cellular model of learning and memory. Here, we
show that NR2B, but not NR2A or NR1, subunits of NMDA receptors are responsible for autophosphorylation-dependent targeting of
CaMKII. CaMKII and NMDA receptors colocalize in neuronal dendritic
spines, and a CaMKII·NMDA receptor complex can be isolated from brain extracts. Autophosphorylation induces direct high-affinity binding of
CaMKII to a 50 amino acid domain in the NR2B cytoplasmic tail; little
or no binding is observed to NR2A and NR1 cytoplasmic tails. Specific
colocalization of CaMKII with NR2B-containing NMDA receptors in
transfected cells depends on receptor activation, Ca2+
influx, and Thr286 autophosphorylation. Translocation of
CaMKII because of interaction with the NMDA receptor Ca2+
channel may potentiate kinase activity and provide exquisite spatial
and temporal control of postsynaptic substrate phosphorylation.
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