αCaMKII binding to the C‐terminal tail of NMDA receptor subunit NR2A and its modulation by autophosphorylation
- 11 August 1999
- journal article
- Published by Wiley in FEBS Letters
- Vol. 456 (3) , 394-398
- https://doi.org/10.1016/s0014-5793(99)00985-0
Abstract
Ca2+/calmodulin-dependent protein kinase II (CaMKII), a multifunctional, widely distributed enzyme, is enriched in post-synaptic densities (PSDs). Here, we demonstrate that CaMKII binds to a discrete C-terminal region of the NR2A subunit of NMDA receptors and promotes the phosphorylation of a Ser residue of this NMDA receptor subunit. Glutathione S-transferase (GST)-NR2A(1349-1464) binds native CaMKII from solubilised hippocampal PSDs in ‘pull-out’ and overlay experiments and this binding is competed by recombinant αCaMKII(1-315). The longer GST-NR2A(1244-1464), although containing the CaMKII phosphosite Ser-1289, binds the kinase with a lower efficacy. CaMKII association to NR2A(1349-1464) is positively modulated by kinase autophosphorylation in the presence of Ca2+/calmodulin. These data provide direct evidence for a mechanism modulating the synaptic strengthKeywords
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