Evidence map›Paper›PMID 25834043›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2015

A proteomic analysis reveals the interaction of GluK1 ionotropic kainate receptor subunits with Go proteins.

Izabela Rutkowska-Wlodarczyk, M Isabel Aller, Sergio Valbuena, Jean-Charles Bologna, Laurent Prézeau, Juan Lerma

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
  2. GluDs are ionotropic dopamine receptors tuned by G-proteins.bioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Kainate Receptors Inhibit Glutamate Release Via Mobilization of Endocannabinoids in Striatal Direct Pathway Spiny Projection Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  11. Review
  12. Article
  13. Article
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

6 authors at 2 institutions in 2 countries.

Izabela Rutkowska-WlodarczykInstituto de Neurociencias, Consejo Superior de Investigaciones Científicas, Universidad Miguel Hernández, 03550 San Juan de Alicante, Spain, and.ORCID http://orcid.org/0000-0003-0799-3327
M Isabel AllerInstituto de Neurociencias, Consejo Superior de Investigaciones Científicas, Universidad Miguel Hernández, 03550 San Juan de Alicante, Spain, and.
Sergio ValbuenaInstituto de Neurociencias, Consejo Superior de Investigaciones Científicas, Universidad Miguel Hernández, 03550 San Juan de Alicante, Spain, and.
Jean-Charles BolognaInstitut de Génomique Fonctionnelle, Centre National de la Recherche Scientifique, Institut National de la Santé et de la Recherche Médicale, 34094 Montpellier cedex 5, France.
Laurent PrézeauInstitut de Génomique Fonctionnelle, Centre National de la Recherche Scientifique, Institut National de la Santé et de la Recherche Médicale, 34094 Montpellier cedex 5, France.
Juan LermaInstituto de Neurociencias, Consejo Superior de Investigaciones Científicas, Universidad Miguel Hernández, 03550 San Juan de Alicante, Spain, and jlerma@umh.es.
Universitat de Miguel Hernández d'Elx · ESInstitut de Génomique Fonctionnelle · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kainate receptors (KARs) are found ubiquitously in the CNS and are present presynaptically and postsynaptically regulating synaptic transmission and excitability. Functional studies have proven that KARs act as ion channels as well as potentially activating G-proteins, thus indicating the existance of a dual signaling system for KARs. Nevertheless, it is not clear how these ion channels activate G-proteins and which of the KAR subunits is involved. Here we performed a proteomic analysis to define proteins that interact with the C-terminal domain of GluK1 and we identified a variety of proteins with many different functions, including a Go α subunit. These interactions were verified through distinct in vitro and in vivo assays, and the activation of the Go protein by GluK1 was validated in bioluminescence resonance energy transfer experiments, while the specificity of this association was confirmed in GluK1-deficient mice. These data reveal components of the KAR interactome, and they show that GluK1 and Go proteins are natural partners, accounting for the metabotropic effects of KARs.

Indexed as

ProteomicsAnimalsBrainFemaleGanglia, SpinalGTP-Binding Protein alpha Subunits, Gi-GoHEK293 CellsHumansKainic AcidKainic Acid ReceptorsMaleMiceMice, KnockoutProtein BindingProtein Interaction Domains and MotifsProtein SubunitsGTP-Binding Protein alpha Subunits, Gi-GoKainic AcidKainic Acid ReceptorsProtein SubunitsGluK1Go proteinkainate receptorsmetabotropicnoncanonicalproteomics

Identifiers

PMID25834043
PMCPMC6705410
OpenAlexW2006461475

What OpenQuestion holds

Textmetadata
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.