In this ongoing collaboration with Antonio Sanz-Clemente at Northwestern University, we define an additional mechanism regulating the synaptic expression of the GluN2B subunit of NMDA receptors.  Following synaptic activity, the GluN2B subunit is phosphorylated on the C-terminal PDZ ligand at S1480 but casein kinase 2 (CK2) resulting in the removal of GluN2B from the synapse. We now show that these extrasynaptic GluN2B subunits are dephosphorylated by PP1 in an activity-dependent manner resulting in the re-entry into the synapse.

See our paper at Cell Reports:

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PP1 dephosphorylates GluN2B in the PDZ ligand to regulate synaptic NMDA receptor content