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SAP102 Mediates Synaptic Clearance of NMDA Receptors
Journal article   Open access   Peer reviewed

SAP102 Mediates Synaptic Clearance of NMDA Receptors

Bo-Shiun Chen, John A. Gray, Antonio Sanz-Clemente, Zhe Wei, Eleanor V. Thomas, Roger A. Nicoll and Katherine W. Roche
Cell reports (Cambridge), v 2(5), pp 1120-1128
01 Nov 2012
PMID: 23103165
url
http://www.cell.com/article/S2211124712003282/pdfView
Published, Version of Record (VoR) Open
url
https://doi.org/10.1016/j.celrep.2012.09.024View
Published, Version of Record (VoR) Open

Abstract

Cell Biology Life Sciences & Biomedicine Science & Technology
Membrane-associated guanylate kinases (MAGUKs) are the major family of scaffolding proteins at the postsynaptic density. The PSD-MAGUK subfamily, which includes PSD-95, PSD-93, SAP97, and SAP102, is well accepted to be primarily involved in the synaptic anchoring of numerous proteins, including N-methyl-D-aspartate receptors (NMDARs). Notably, the synaptic targeting of NMDARs depends on the binding of the PDZ ligand on the GluN2B subunit to MAGUK PDZ domains, as disruption of this interaction dramatically decreases NMDAR surface and synaptic expression. We recently reported a secondary interaction between SAP102 and GluN2B, in addition to the PDZ interaction. Here, we identify two critical residues on GluN2B responsible for the non-PDZ binding to SAP102. Strikingly, either mutation of these critical residues or knockdown of endogenous SAP102 can rescue the defective surface expression and synaptic localization of PDZ binding-deficient GluN2B. These data reveal an unexpected, nonscaffolding role for SAP102 in the synaptic clearance of GluN2B-containing NMDARs.

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Cell Biology
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