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

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking.

Neuron - 29 Oct 2009

Hayashi Takashi, Thomas Gareth M, Huganir Richard L

Abstract excerpt

Modification of NMDA receptor function and trafficking contributes to the regulation of synaptic transmission and is important for several forms of synaptic plasticity. Here, we report that NMDA receptor subunits NR2A and NR2B have two distinct clusters of palmitoylation sites in their C-terminal region. Palmitoylation within the first cluster on a membrane-proximal region increases tyrosine phosphorylation of...

Read the complete abstract on PubMed

Topics

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

Share to Anesthetics, Local
Share to Golgi Apparatus
Share to Immunoprecipitation

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

Share to Lipoylation

Share to Palmitates

Share to Receptors, N-Methyl-D-Aspartate

Share to Tetrodotoxin

Share to Tritium

Source

Open in PubMed Open full text

Identifiers

PMID: 19874789
DOI: 10.1016/j.neuron.2009.08.017
PMCID: PMC2788208

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

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking.PMID 19874789Read ↗

Palmitoylation at two cysteine clusters on the C-terminus of GluN2A and GluN2B differentially control synaptic targeting of NMDA receptors.Semantic proximity Read ↗

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

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

Palmitoylation regulates glutamate receptor distributions in postsynaptic densities through control of PSD95 conformation and orientation.Semantic proximity Read ↗

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

NMDA Receptor Dysregulation by Defective Depalmitoylation in the Infantile Neuronal Ceroid Lipofuscinosis Mouse ModelSemantic proximity Read ↗

Palmitoylation of estrogen receptors is essential for neuronal membrane signaling.Semantic proximity Read ↗

Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation.Semantic proximity Read ↗

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

Palmitoylation of KChIP splicing variants is required for efficient cell surface expression of Kv4.3 channels.Semantic proximity Read ↗

Membrane targeting of L-type calcium channels. Role of palmitoylation in the subcellular localization of the beta2a subunit.Semantic proximity Read ↗

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

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