Mechanism and regulation of calcium/calmodulin-dependent protein kinase II targeting to the NR2B subunit of the N-methyl-D-aspartate receptor
S Strack, RB McNeill, RJ Colbran - Journal of Biological Chemistry, 2000 - ASBMB
Calcium influx through the N-methyl-d-aspartate (NMDA)-type glutamate receptor and
activation of calcium/calmodulin-dependent kinase II (CaMKII) are critical events in certain
forms of synaptic plasticity. We have previously shown that autophosphorylation of CaMKII
induces high-affinity binding to the NR2B subunit of the NMDA receptor (Strack, S., and
Colbran, RJ (1998) J. Biol. Chem. 273, 20689–20692). Here, we show that residues 1290–
1309 in the cytosolic tail of NR2B are critical for CaMKII binding and identify by site-directed …
activation of calcium/calmodulin-dependent kinase II (CaMKII) are critical events in certain
forms of synaptic plasticity. We have previously shown that autophosphorylation of CaMKII
induces high-affinity binding to the NR2B subunit of the NMDA receptor (Strack, S., and
Colbran, RJ (1998) J. Biol. Chem. 273, 20689–20692). Here, we show that residues 1290–
1309 in the cytosolic tail of NR2B are critical for CaMKII binding and identify by site-directed …
