Evidence map›Paper›PMID 22431337›Full record

ReviewThe Journal of physiology2012

Neto1 and Neto2: auxiliary subunits that determine key properties of native kainate receptors.

Susumu Tomita, Pablo E Castillo

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

57 citing papers in PubMed, 76 citations in OpenAlex.

  1. Trial
  2. Article
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  4. Review
  5. Article
  6. Article
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  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structure and gating of kainate receptors.Frontiers in pharmacology · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Neto proteins differentially modulate the gating properties ofbioRxiv : the preprint server for biology · 2024
    Article
  18. Article
  19. Article
  20. 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

2 authors at 2 institutions in 1 country.

Susumu TomitaProgram in Cellular Neuroscience, Neurodegeneration and Repair (CNNR), Department of Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, CT 06510, USA. susumu.tomita@yale.edu
Pablo E Castillo
Albert Einstein College of Medicine · USYale University · US

Funding

Activity-dependent synaptic plasticity expressed by NMDARsR01MH081935 · NIMH · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI CASTILLO, PABLO E · 2008 to 2018
$4.0M
Mechanism for Regulating Kainate-Type Glutamate Receptor ActivityR01MH085080 · NIMH · YALE UNIVERSITY · PI TOMITA, SUSUMU · 2010 to 2014
$2.0M
NIMH NIH HHS R01 MH081935NIMH NIH HHS R01 MH085080
6 · The paper itself

Abstract

Kainate receptors (KARs) are a subfamily of ionotropic glutamate receptors (iGluRs) that mediate excitatory synaptic transmission, regulate neurotransmitter release, and show a remarkably selective distribution in the brain. Compared to other iGluRs, the precise contribution of KARs to brain function is less understood. Unlike recombinant KARs, native KARs exhibit characteristically slow channel kinetics. The underlying explanation for this dissimilar kinetics has remained elusive until recently. New research has identified Neto1 and Neto2 as KAR auxiliary subunits that determine unique properties of synaptic KARs, including their slow kinetics and high affinity for agonist. Whether these auxiliary subunits regulate KAR trafficking and targeting at the synapse is less clear. By regulating channel gating, Neto1 and Neto2 can increase the diversity of KAR functional properties. These auxiliary subunits may represent a starting point for a better understanding of the role played by neuronal KARs under normal and pathological conditions, but also, they may provide an alternative target for the development of new drugs regulating KARs and brain function.

Indexed as

AnimalsKainic Acid ReceptorsLDL-Receptor Related ProteinsLipoproteins, LDLMembrane ProteinsProtein SubunitsReceptors, N-Methyl-D-AspartateSynapsesKainic Acid ReceptorsLDL-Receptor Related ProteinsLipoproteins, LDLMembrane ProteinsNeto1 protein, mouseNETO2 protein, mouseProtein SubunitsReceptors, N-Methyl-D-Aspartate

Identifiers

PMID22431337
PMCPMC3424747
OpenAlexW2149366664

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.