K. Shen et al., CAMKII-BETA FUNCTIONS AS AN F-ACTIN TARGETING MODULE THAT LOCALIZES CAMKII-ALPHA BETA HETEROOLIGOMERS TO DENDRITIC SPINES/, Neuron (Cambridge, Mass.), 21(3), 1998, pp. 593-606
Ca2+/calmodulin-dependent protein kinase II (CaMKII) is a serine/threo
nine protein kinase that regulates long-term potentiation and other fo
rms of neuronal plasticity. Functional differences between the neurona
l CaMKII alpha and CaMKII beta isoforms are not yet known. Here, we us
e green fluorescent protein-tagged (GFP-tagged) CaMKII isoforms and sh
ow that CaMKII beta is bound to F-actin in dendritic spines and cell c
ortex while CaMKII alpha is largely a cytosolic enzyme. When expressed
together, the two isoforms form large heterooligomers, and a small fr
action of CaMKII beta is sufficient to dock the predominant CaMKII alp
ha to the actin cytoskeleton. Thus, CaMKII beta functions as a targeti
ng module that localizes a much larger number of CaMKII alpha isozymes
to synaptic and cytoskeletal sites of action.