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Positive surface charge of GluN1 N-terminus mediates the direct interaction with EphB2 and NMDAR mobility

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  • Halley R. Washburn

    (Thomas Jefferson University)

  • Nan L. Xia

    (Thomas Jefferson University
    University of Chicago)

  • Wei Zhou

    (Thomas Jefferson University)

  • Yu-Ting Mao

    (Thomas Jefferson University)

  • Matthew B. Dalva

    (Thomas Jefferson University)

Abstract

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 synapses and mediates the direct extracellular interaction with a negatively charged phospho-tyrosine on the receptor tyrosine kinase EphB2. Loss of the EphB-NMDAR interaction by either mutating GluN1 or knocking down endogenous EphB2 increases NMDAR mobility. These findings begin to define a mechanism for extracellular interactions mediated by charged domains.

Suggested Citation

  • Halley R. Washburn & Nan L. Xia & Wei Zhou & Yu-Ting Mao & Matthew B. Dalva, 2020. "Positive surface charge of GluN1 N-terminus mediates the direct interaction with EphB2 and NMDAR mobility," Nature Communications, Nature, vol. 11(1), pages 1-16, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14345-6
    DOI: 10.1038/s41467-020-14345-6
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    Cited by:

    1. Martin Hruska & Rachel E. Cain & Matthew B. Dalva, 2022. "Nanoscale rules governing the organization of glutamate receptors in spine synapses are subunit specific," Nature Communications, Nature, vol. 13(1), pages 1-19, December.

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