In the striatum, dopamine D1R (D1 receptor) activation potentiates NMDA (N-methyl-D-aspartate) transmission and is required for NMDA-mediated long-term potentiation at corticostriatal synapses. By using a combination of co-immunoprecipitation, pull-out with glutathione S-transferase-fusion proteins and bioluminescence resonance energy transfer, we have reported that the D1R forms a heteromeric complex with the NMDAR (NMDA receptor) and that this mechanism is crucial to recruit the D1R to the postsynaptic density. By using confocal and radioligand-binding assay, we also demonstrated that the interaction with NMDAR abolishes agonist-mediated D1R sequestration, indicating that oligomerization with NMDAR could represent a novel regulatory mechanism modulating D1R cellular trafficking and desensitization.

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