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Positive Surface Charge Of Glun1 N-Terminus Mediates The Direct Interaction With Ephb2 And Nmdar Mobility., Halley R. Washburn, Nan L. Xia, Wei Zhou, Yu-Ting Mao, Matthew B. Dalva

Department of Neuroscience Faculty Papers

Localization of the N-methyl-D-aspartate type glutamate receptor (NMDAR) to dendritic spines is essential for excitatory synaptic transmission and plasticity. Rather than remaining trapped at synaptic sites, NMDA receptors undergo constant cycling into and out of the postsynaptic density. Receptor movement is constrained by protein-protein interactions with both the intracellular and extracellular domains of the NMDAR. The role of extracellular interactions on the mobility of the NMDAR is poorly understood. Here we demonstrate that the positive surface charge of the hinge region of the N-terminal domain in the GluN1 subunit of the NMDAR is required to maintain NMDARs at dendritic spine …