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. 2018 Aug 8;19(8):2319. doi: 10.3390/ijms19082319

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© 2018 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Pin1 regulation of NMDAR complex and synaptic plasticity. Synaptic activation of NMDAR stimulates Ca2⁺/Calmodulin-dependent protein Kinase II (CaMKII) and casein kinase II (CK2) activity. CK2 phosphorylates the PDZ (postsynaptic density-95(PSD-95)/Discs large/zona occludens-1) ligand of NR2B. Pin1 binds and stabilizes probably the conformational change of NR2B phosphorylated disrupting the interaction between NMDAR on the cell surface and the PDZ domains of PSD-95. This leads to destabilization and internalization of surface NMDAR that influences, in turn, synaptic transmission and spine morphology. NR2A; NR2B; AMPA; F-Actin; Contarctin; CaMKII, Ca2⁺-Calmodulin dependent protein Kinase II; CK2, casein Kinase 2; PSD-95 presents three PDZ domains, SH3 (Sarc homology 3 domain) and GK (guanylate kinase-like domain) domains; Pin1; GKAP, Guanylate kinase associate protein; Shank, shank protein.