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of transcription factors and translation factor, respectively. Phosphorylated proteins change
their activity and regulate signaling pathways, and then new synapses are formed, resulting in
a change of synaptic activity (Fig. 2).
The functional significance of the regulated change of many other substrates of CaMII
needs to be investigated at the molecular level in the neural system. Furthermore, some
neuronal diseases may be related to the disruption of synaptic activity
via
the impaired
functioning of CaMKII. Many of CaMKII's targets are also phosphorylated by various
protein kinases, including PKA, PKC, MAP kinase, and Src family tyrosine kinases,
indicating that cross-talk of CaMKII signaling with other signaling systems is important to
the synaptic plasticity. Taken together, CaMKII is one of the best candidates for a molecular
component of the memory apparatus, and the PSD is a good candidate for the body of their
apparatus.
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