The C-terminus of NMDAR GluN1-1a Subunit Translocates to Nucleus and Regulates Synaptic Function.

ABSTRACT: NMDARs, the Ca²⁺ permeable channels, play central roles in synaptic plasticity, brain development, learning, and memory. NMDAR binding partners and associated signaling has been extensively studied in synapse-to-nucleus communications. However, whether NMDARs could directly regulate synapse-to-nucleus communications is largely unknown. Here, we analyze the four alternative splicing of the C-terminus isoforms of GluN1 (1a, 2a, 3a, and 4a), and find that C1 domain of GluN1 is necessary for nuclear localization. Besides, we find that the 10 basic amino acids in C1 domain determine the nuclear localization of GluN1 C-terminus. Further investigating the expression patterns of the full length of GluN1 four isoforms shows that only GluN-1a exhibits the cytoplasmic and nucleus distribut

SUBMITTER: Zhou L 

PROVIDER: S-EPMC6176477 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature