Physiological and Pathological Roles of CaMKII-PP1 Signaling in the Brain
AbstractCa2+/calmodulin (CaM)-dependent protein kinase II (CaMKII), a multifunctional serine (Ser)/threonine (Thr) protein kinase, regulates diverse activities related to Ca2+-mediated neuronal plasticity in the brain, including synaptic activity and gene expression. Among its regulators, protein phosphatase-1 (PP1), a Ser/Thr phosphatase, appears to be critical in controlling CaMKII-dependent neuronal signaling. In postsynaptic densities (PSDs), CaMKII is required for hippocampal long-term potentiation (LTP), a cellular process correlated with learning and memory. In response to Ca2+ elevation during hippocampal LTP induction, CaMKIIα, an isoform that translocates from the cytosol to PSDs, is activated through autophosphorylation at Thr286, generating autonomous kinase activity and a prolonged Ca2+/CaM-bound state. Moreover, PP1 inhibition enhances Thr286 autophosphorylation of CaMKIIα during LTP induction. By contrast, CaMKII nuclear import is regulated by Ser332 phosphorylation state. CaMKIIδ3, a nuclear isoform, is dephosphorylated at Ser332 by PP1, promoting its nuclear translocation, where it regulates transcription. In this review, we summarize physio-pathological roles of CaMKII/PP1 signaling in neurons. CaMKII and PP1 crosstalk and regulation of gene expression is important for neuronal plasticity as well as survival and/or differentiation. View Full-Text
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Shioda, N.; Fukunaga, K. Physiological and Pathological Roles of CaMKII-PP1 Signaling in the Brain. Int. J. Mol. Sci. 2018, 19, 20.
Shioda N, Fukunaga K. Physiological and Pathological Roles of CaMKII-PP1 Signaling in the Brain. International Journal of Molecular Sciences. 2018; 19(1):20.Chicago/Turabian Style
Shioda, Norifumi; Fukunaga, Kohji. 2018. "Physiological and Pathological Roles of CaMKII-PP1 Signaling in the Brain." Int. J. Mol. Sci. 19, no. 1: 20.
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