Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The synaptic localization of NR2B-containing NMDA receptors is controlled by interactions with PDZ proteins and AP-2.

Neuron - 15 Sept 2005

Prybylowski Kate, Chang Kai, Sans Nathalie, Kan Lilly, Vicini Stefano, Wenthold Robert J

Abstract excerpt

The NMDA receptor (NMDAR) is a component of excitatory synapses and a key participant in synaptic plasticity. We investigated the role of two domains in the C terminus of the NR2B subunit--the PDZ binding domain and the clathrin adaptor protein (AP-2) binding motif--in the synaptic localization of NMDA receptors. NR2B subunits lacking functional PDZ binding are excluded from the synapse. Mutations in the AP-2...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cerebellum
Share to DNA Probes
Share to Excitatory Postsynaptic Potentials

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Immunoprecipitation

Share to Models, Neurological

Share to Receptors, N-Methyl-D-Aspartate

Share to Synapses

Share to Two-Hybrid System Techniques

Source

Open in PubMed Open full text

Identifiers

PMID: 16157279
DOI: 10.1016/j.neuron.2005.08.016
PMCID: PMC1350965

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The synaptic localization of NR2B-containing NMDA receptors is controlled by interactions with PDZ proteins and AP-2.PMID 16157279Read ↗

Role of the fourth membrane domain of the NR2B subunit in the assembly of the NMDA receptor.Semantic proximity Read ↗

Tyrosine phosphorylation regulates the endocytosis and surface expression of GluN3A-containing NMDA receptors.Semantic proximity Read ↗

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking.Semantic proximity Read ↗

Endocytosis and synaptic removal of NR3A-containing NMDA receptors by PACSIN1/syndapin1.Semantic proximity Read ↗

Subunit-specific NMDA receptor trafficking to synapses.Semantic proximity Read ↗

SAP102 mediates synaptic clearance of NMDA receptors.Semantic proximity Read ↗

PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-D-aspartate receptor subunit NR2A.Semantic proximity Read ↗

Independent regulation of early trafficking of NMDA receptors by ligand-binding domains of the GluN1 and GluN2A subunitsSemantic proximity Read ↗

Glutamate binding to the GluN2B subunit controls surface trafficking of N-methyl-D-aspartate (NMDA) receptors.Semantic proximity Read ↗

A new motif necessary and sufficient for stable localization of the delta2 glutamate receptors at postsynaptic spines.Semantic proximity Read ↗

Loss of postsynaptic NMDARs drives nanoscale reorganization of Munc13-1 and PSD-95Semantic proximity Read ↗

Non-ionotropic signaling through the NMDA receptor GluN2B carboxy terminal domain drives morphological plasticity of dendritic spines and reverses fragile X phenotypes in mouse hippocampusSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.