[HTML][HTML] Protein kinase C activation modulates α-calmodulin kinase II binding to NR2A subunit of N-methyl-D-aspartate receptor complex
The N-methyl-d-aspartate (NMDA) receptor subunits NR2 possess extended intracellular C-
terminal domains by which they can directly interact with a large number of postsynaptic
density (PSD) proteins involved in synaptic clustering and signaling. We have previously
shown that PSD-associated α-calmodulin kinase II (αCaMKII) binds with high affinity to the C-
terminal domain of the NR2A subunit. Here, we show that residues 1412–1419 of the
cytosolic tail of NR2A are critical for αCaMKII binding, and we identify, by site directed …
terminal domains by which they can directly interact with a large number of postsynaptic
density (PSD) proteins involved in synaptic clustering and signaling. We have previously
shown that PSD-associated α-calmodulin kinase II (αCaMKII) binds with high affinity to the C-
terminal domain of the NR2A subunit. Here, we show that residues 1412–1419 of the
cytosolic tail of NR2A are critical for αCaMKII binding, and we identify, by site directed …