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
Excited to see the lab’s first original research publication in print and congrats to Jon Wong for his first scientific publication! It was even a featured article. PDF can be found here.
Gray JA, Zito K, and Hell JW (2016). Non-ionotropic signaling by the NMDA receptor: controversy and opportunity. F1000Research, 5(F1000 Faculty Rev): 1010. In collaboration with Karen Zito and Johannes Hell, I recently reviewed the emerging literature on possible non-ionotropic signaling
Was excited to be able to contribute to an elegant study from the Zito Lab showing that NMDA receptor-mediated spine shrinkage requires glutamate binding but not ion flux through the channel, supporting recent studies showing that the NMDA receptor can