Evidence map›Paper›PMID 19874789›Full record

ArticleNeuron2009

Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking.

Takashi Hayashi, Gareth M Thomas, Richard L Huganir

Open access · bronzeAbstract read
In one paragraph

Article in Neuron, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed, 1 pooled it
6.1field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

140 citing papers in PubMed, 1 synthesis or guideline pooled it, 218 citations in OpenAlex.

  1. Guideline
  2. Review
  3. Article
  4. Article
  5. Review
  6. Distinct Regulation of Early Trafficking of the NMDA Receptors by the Ligand-Binding Domains of the GluN1 and GluN2A Subunits.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  7. Review
  8. Article
  9. Article
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  11. Article
  12. Review
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  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. NMDA Receptor and Its Emerging Role in Cancer.International journal of molecular sciences · 2023
    Review

80 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Takashi HayashiHoward Hughes Medical Institute, Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Gareth M Thomas
Richard L Huganir
Johns Hopkins University · USHoward Hughes Medical Institute · US

Funding

Regulation of the NMDA Receptor Signaling ComplexR01MH064856 · NIMH · JOHNS HOPKINS UNIVERSITY · PI HUGANIR, RICHARD L · 2002 to 2011
$3.6M
Howard Hughes Medical InstituteNIMH NIH HHS R01 MH064856
6 · The paper itself

Abstract

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 tyrosine-based internalization motifs by Src family protein tyrosine kinases, leading to enhanced stable surface expression of NMDA receptors. In addition, palmitoylation of these sites regulates constitutive internalization of the NMDA receptor in developing neurons. In marked contrast, palmitoylation of the second cluster in the middle of C terminus by distinct palmitoyl transferases causes receptors to accumulate in the Golgi apparatus and reduces receptor surface expression. These data suggest that regulated palmitoylation of NR2 subunits differentially modulates receptor trafficking and might be important for NMDA-receptor-dependent synaptic plasticity.

Indexed as

Anesthetics, LocalAnimalsCells, CulturedCerebral CortexCysteineGolgi ApparatusGreen Fluorescent ProteinsHumansImmunoprecipitationLipoylationMembrane ProteinsMiceMutationNeuronsPalmitatesProtein TransportAnesthetics, LocalCysteineGODZ protein, mouseGreen Fluorescent ProteinsMembrane ProteinsNR2A NMDA receptorNR2B NMDA receptorPalmitatesProtein-Tyrosine KinasesReceptors, N-Methyl-D-AspartateTetrodotoxinTritiumTyrosine

Identifiers

PMID19874789
PMCPMC2788208
OpenAlexW2001679254

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.