Biochemical and Biophysical Research Communications, Vol.534, 323-329, 2021
The NMDAR GluN1-1a C-terminus binds to CaM and regulates synaptic function
The binding of calmodulin (CaM) to NMDAR (N-methyl-D-aspartate receptor) GluN1 C-terminus is required for cacium (Ca2+)/calmodulin (CaM)-dependent inactivation of NMDAR. Previously, we found that GluN1 C-terminus translocated to nucleus, and regulated synaptic transmission. However, whether GluN1 C-terminus containing the nuclear localization signaling regulates the cellular distribution of CaM, and the CaM binding are not clear. In this study, we found that the 10 positive residues of GluN1 C-terminus determined the translocation of CaM to the nucleus. RNA sequencing data showed that CaM could regulate the genes expression of multiple cell surface membrane receptors. This was confirmed by electrophysiology data that the 10A mutation of GluN1 C-terminus increased the NMDAR/AMAPR-mediated synaptic transduction. (C) 2020 Elsevier Inc. All rights reserved.