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N-methyl-D-aspartate receptors (NMDARs) are heterotetramers mainly composed of two GluN1 subunits and two GluN2 or GluN3 subunits.Subunit composition of synaptic NMDARs is dynamically regulated and mediates critical roles in synaptic plasticity.It has been revealed that surface level of GluN2B-containing NMDARs can be regulated by phosphorylation at Y1472 residue in the GluN2BC-terminal domain (CTD) by Src family kinases.However,there are several other potential tyrosine sites in the GluN2B CTD and their function remains to be explored.