Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 534, Issue -, Pages 323-329Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2020.11.085
Keywords
NMDA receptor; GluN1 C-Terminus; CaM; RNA sequencing; Positive residues
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Funding
- NIH (USA)
- National Natural Science Foundation of China [81703535]
- Guangdong Nature Science Foundation [2019A1515011309]
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In this study, it was found that the positive charges of GluN1 C-terminus determine the translocation of CaM to the nucleus, regulating synaptic transmission and the gene expression of multiple cell surface receptors, consequently affecting NMDAR-mediated synaptic transduction.
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.
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