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

In vivo composition of NMDA receptor signaling complexes differs between membrane subdomains and is modulated by PSD-95 and PSD-93.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 16 Jun 2010

Delint-Ramirez Ilse, Fernández Esperanza, Bayés Alex, Kicsi Emese, Komiyama Noboru H, Grant Seth G N

Abstract excerpt

Lipid rafts are dynamic membrane microdomains enriched in cholesterol and sphingolipids involved in the compartmentalization of signaling pathways, trafficking and sorting of proteins. At synapses, the glutamatergic NMDA receptor and its cytoplasmic scaffold protein PSD-95 move between postsynaptic density (PSD) and rafts following learning or ischemia. However it is not known whether the signaling complexes...

Read the complete abstract on PubMed

Topics

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

Share to Cholera Toxin
Share to Disks Large Homolog 4 Protein

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

Share to Gangliosidosis, GM1

Share to Guanylate Kinases

Share to Membrane Microdomains

Share to PDZ Domains

Share to Receptors, N-Methyl-D-Aspartate

Share to Valine

Source

Open in PubMed Open full text

Identifiers

PMID: 20554866
DOI: 10.1523/JNEUROSCI.1792-10.2010
PMCID: PMC2912510

Genes

PSD

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

In vivo composition of NMDA receptor signaling complexes differs between membrane subdomains and is modulated by PSD-95 and PSD-93.PMID 20554866Read ↗

Distinct domains within PSD-95 mediate synaptic incorporation, stabilization, and activity-dependent trafficking.Semantic proximity Read ↗

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

Postsynaptic density 95 (PSD-95) serine 561 phosphorylation regulates a conformational switch and bidirectional dendritic spine structural plasticity.Semantic proximity Read ↗

Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs.Semantic proximity Read ↗

alpha-Isoform of calcium-calmodulin-dependent protein kinase II and postsynaptic density protein 95 differentially regulate synaptic expression of NR2A- and NR2B-containing N-methyl-d-aspartate receptors in hippocampus.Semantic proximity Read ↗

Cell-type specific visualization and biochemical isolation of endogenous synaptic proteins in miceSemantic proximity Read ↗

Differential control of postsynaptic density scaffolds via actin-dependent and -independent mechanisms.Semantic proximity Read ↗

NMDA receptors are selectively partitioned into complexes and supercomplexes during synapse maturation.Semantic proximity Read ↗

Synaptic accumulation of PSD-95 and synaptic function regulated by phosphorylation of serine-295 of PSD-95.Semantic proximity Read ↗

The Protein Biochemistry of the Postsynaptic Density in Glutamatergic Synapses Mediates Learning in Neural Networks.Semantic proximity Read ↗

PSD-95 regulates NMDA receptors in developing cerebellar granule neurons of the rat.Semantic proximity Read ↗

Differential expression of two NMDA receptor interacting proteins, PSD-95 and SynGAP during mouse development.Semantic proximity Read ↗

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