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Phosphorylation on the Brain

N-Methyl-D-aspartate (NMDA) receptors are gated ion channels that respond to glutamate, the major excitatory neurotransmitter of the mammalian central nervous system. In addition to mediating synaptic transmission, they play important roles in synapse formation, synaptic plasticity, and learning and memory. Their function and trafficking is often regulated by phosphorylation. The receptors consist of two NR1 subunits combined with additional NR2 and NR3 subunits. The NR2 subunits display unique spatiotemporal expression patterns and confer distinct pharmacological and functional properties on NMDA receptors.

Mutation of Ser1244 affects NMDA receptor channel kinetics.

In this Paper of the Week, Chen and colleagues provide compelling data identifying a novel phosphorylation site on the NMDA receptor subunit NR2C, a subunit with very restricted expression in the cerebellum whose regulation has received very little attention. In a series of rigorous biochemical and functional experiments Chen et al. define the serine 1244 of NR2C as a cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) phosphorylation site and go on to show that phosphorylation at this site has a selective effect on NMDA channel kinetics. These findings provide a significant step in our understanding of NMDA receptor regulation in the cerebellum.

FOOTNOTES

See referenced article, J. Biol. Chem. 2006, 281, 16583–16590

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