Evidence map›Paper›PMID 15190111›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2004

Regulation of synaptic strength and AMPA receptor subunit composition by PICK1.

Akira Terashima, Lucy Cotton, Kumlesh K Dev, Guido Meyer, Shahid Zaman, Fabrice Duprat, Jeremy M Henley, Graham L Collingridge, John T R Isaac

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
6.2field-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

100 citing papers in PubMed, 184 citations in OpenAlex.

  1. Review
  2. Review
  3. Protein interacting with C-kinase 1 (PICK1) regulates synaptic function and reversal learning in a mouse model for schizophrenia.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2025
    Article
  4. Article
  5. Article
  6. Molecular Mechanisms of AMPA Receptor Trafficking in the Nervous System.International journal of molecular sciences · 2023
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Phosphorylation-Dependent Regulation of CaFrontiers in synaptic neuroscience · 2020
    Article
  14. Review
  15. Review
  16. Preferential generation of CaThe Journal of biological chemistry · 2019
    Article
  17. Article
  18. Article
  19. Mechanisms of AMPA Receptor Endosomal Sorting.Frontiers in molecular neuroscience · 2018
    Review
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Akira TerashimaMedical Research Council Centre for Synaptic Plasticity, Department of Anatomy, University of Bristol, Bristol BS8 1TD, United Kingdom.
Lucy Cotton
Kumlesh K Dev
Guido Meyer
Shahid Zaman
Fabrice Duprat
Jeremy M Henley
Graham L Collingridge
John T R Isaac
Medical Research Council · GB

Funding

Mechanisms of Synaptic Plasticity and Development of Circuit FunctionZIANS003011 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI ISAAC, JOHN · 2009 to 2010
$3.7M
Synaptic Plasticity in Developing Cortical NetworksZ01NS003011 · NINDS · NEUROLOGICAL DISORDERS AND STROKE · PI ISAAC, JOHN · 2005 to 2008
$2.4M
Medical Research Council G9629038Medical Research Council G9629038(61600)Wellcome Trust
6 · The paper itself

Abstract

PICK1 (protein interacting with C kinase-1) regulates the surface expression of the AMPA receptor (AMPAR) GluR2 subunit, however, the functional consequences of this interaction are not well understood. Previous work has suggested that PICK1 promotes the internalization of AMPARs. However, we found that when PICK1 is virally expressed in the CA1 region of hippocampal slices, it causes an increase in AMPAR-mediated EPSC amplitude. This effect is associated with increased AMPAR rectification and sensitivity to polyamine toxin. These effects are blocked by PKC or calcium/calmodulin-dependent protein kinase II inhibitors, indicating that the virally expressed PICK1 signals through an endogenous kinase cascade. In contrast, blockade of interactions with GluR2 at the N-ethylmaleimide-sensitive factor site did not cause a change in subunit composition, suggesting that the effects of PICK1 are not simply a nonspecific consequence of removing AMPARs from the surface. Immunocytochemical and biochemical analyses in dissociated cultured hippocampal neurons show that PICK1 causes a decrease in endogenous GluR2 surface expression but no change in GluR1 surface levels. To address the physiological role of PICK1, we virally expressed C-terminal GluR2 peptides. Blockade of endogenous PICK1 PDZ (postsynaptic density-95/Discs large/zona occludens-1) domain interactions produced opposite effects on synaptic strength and AMPAR rectification to those observed with PICK1 expression. This demonstrates that AMPAR subunit composition is physiologically regulated through a mechanism involving PICK1 PDZ domain interactions. These findings suggest that PICK1 acts to downregulate the GluR2 content of AMPARs at hippocampal CA1 synapses, thereby increasing synaptic strength at resting membrane potentials.

Indexed as

Nuclear ProteinsAnimalsCarrier ProteinsCytoskeletal ProteinsElectrophysiologyEmbryo, MammalianHippocampusImmunohistochemistryPolymerase Chain ReactionRatsRats, Sprague-DawleyReceptors, AMPARecombinant Fusion ProteinsSynapsesCarrier ProteinsCytoskeletal Proteinsglutamate receptor ionotropic, AMPA 2Nuclear ProteinsPICK1 protein, ratReceptors, AMPARecombinant Fusion Proteins

Identifiers

PMID15190111
PMCPMC3310907
OpenAlexW2142255838

What OpenQuestion holds

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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.