Dynamic Control of CaMKII Translocation and Localization in Hippocampal Neurons by NMDA Receptor Stimulation

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Science  02 Apr 1999:
Vol. 284, Issue 5411, pp. 162-167
DOI: 10.1126/science.284.5411.162

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Calcium-calmodulin–dependent protein kinase II (CaMKII) is thought to increase synaptic strength by phosphorylating postsynaptic density (PSD) ion channels and signaling proteins. It is shown that N-methyl-D-aspartate (NMDA) receptor stimulation reversibly translocates green fluorescent protein–tagged CaMKII from an F-actin–bound to a PSD-bound state. The translocation time was controlled by the ratio of expressed β-CaMKII to α-CaMKII isoforms. Although F-actin dissociation into the cytosol required autophosphorylation of or calcium-calmodulin binding to β-CaMKII, PSD translocation required binding of calcium-calmodulin to either the α- or β-CaMKII subunits. Autophosphorylation of CaMKII indirectly prolongs its PSD localization by increasing the calmodulin-binding affinity.

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