The NMDA (N-methyl D-aspartate) receptors in the brain play a critical role in synaptic plasticity, synaptogenesis and excitotoxicity. NMDA R1 and combination of one or more NMDAR2 subunits forms NMDA receptor glutamate-gated ion channels. In this hetromer complex, NMDA R1 binds to co-agonist glycine and NMDA R2 binds to neurotransmitter glutamate (1). Several studies have suggested that protein phosphorylation of NMDA receptors may affect channel function, and additionally regulate these receptors’ synaptic trafficking and surface expression. Once activated thru phospholyation, these channels allow movement of Ca2+ and Na+ into the cell and K+ out of the cell. Serine 1303 on NMDAR2B has been identified as a major phospholyation site for CaM kinase II and PKC, regulating kinase-mediated NMNDAR2B/R1 current (2,3). NMDAR has been linked to various neurodegenerative disorders such as schizophrenia, epilepsy, and Alzheimer's disease (4).
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