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CaM kinase II, in a calcium and calmodulin dependent manner, phosphorylates many different brain substrates including synapsin I, tryptophan hydroxylase, tyrosine hydroxylase and nitric oxide synthase thereby performing regulatory functions associated with increases in intracellular free calcium. CaM kinase II is particularly abundant in the hippocampus and forebrain where it comprises ~1% of total protein. Within the neuron, CaM kinase II is a major component of the postsynaptic density fraction accounting for as much as 30% of total protein in the post synaptic density (PSD) region.
Autophosphorylation of threonine-286 occurs after calcium/calmodulin activation and can enable CaM kinase II to remain active independent of free calcium. Autophosphorylation of CaM kinase II in hippocampal neurons, which results in relatively high levels of kinase activity even at basal calcium concentrations, may allow for both upward and downward regulation as opposed to simply on/off regulation.
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