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Abstract Synaptic NMDA-type glutamate receptors (NMDARs) are central components of all neural computations. NMDAR levels critically vary between synapses but how the synaptic localization of NMDARs is controlled remains unclear. Here we show that SIK3, a serine–threonine protein kinase, localizes to synapses where it phosphorylates the obligatory NMDAR subunit GluN1 at a single site. This single phosphorylation event controls NMDAR recruitment to synapses.
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