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Regulation of NMDA Receptor Transport: A KIF17–Cargo Binding/Releasing Underlies Synaptic Plasticity and Memory In Vivo

Regulation of NMDA receptor trafficking is crucial to modulate neuronal communication. Ca2+/calmodulin-dependent protein kinase phosphorylates the tail domain of KIF17, a member of the kinesin superfamily, to control NMDA receptor subunit 2B (GluN2B) transport by changing the KIF17–cargo interaction in vitro. However, the mechanisms of regulation of GluN2B transport in vivo and its physiological significance are unknown. We generated transgenic mice carrying wild-type KIF17 (TgS), or KIF17 with S1029A (TgA) or S1029D (TgD) phosphomimic mutations in kif17−/− background. TgA/kif17−/− and TgD/kif17−/− mice exhibited reductions in synaptic NMDA receptors because of their inability to load/unload GluN2B onto/from KIF17, leading to impaired neuronal plasticity, CREB activation, and spatial memory. Expression of GFP-KIF17 in TgS/kif17−/− mouse neurons rescued the synaptic and behavioral defects of kif17−/− mice. These results suggest that phosphorylation-based regulation of NMDA receptor transport is critical for learning and memory in vivo.