Evidence map›Paper›PMID 28871958›Full record

ArticleeLife2017

Control of AMPA receptor activity by the extracellular loops of auxiliary proteins.

Irene Riva, Clarissa Eibl, Rudolf Volkmer, Anna L Carbone, Andrew Jr Plested

Abstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Article
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  12. Structural insights into function of ionotropic glutamate receptors.Biochemistry (Moscow) Supplement. Series A, Membrane and cell biology · 2022
    Article
  13. Article
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  17. Review
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  19. Nonselective cation permeation in an AMPA-type glutamate receptor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. Review
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

5 authors.

Irene Riva *Institute of Biology, Cellular Biophysics, Humboldt Universität zu Berlin, Berlin, Germany.
Clarissa Eibl *Institute of Biology, Cellular Biophysics, Humboldt Universität zu Berlin, Berlin, Germany.
Rudolf VolkmerChemical Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.
Anna L CarboneInstitute of Biology, Cellular Biophysics, Humboldt Universität zu Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0001-9746-2778
Andrew Jr PlestedInstitute of Biology, Cellular Biophysics, Humboldt Universität zu Berlin, Berlin, Germany.ORCID http://orcid.org/0000-0001-6062-0832

Funding

Austrian Science Fund FWF J 3682
6 · The paper itself

Abstract

At synapses throughout the mammalian brain, AMPA receptors form complexes with auxiliary proteins, including TARPs. However, how TARPs modulate AMPA receptor gating remains poorly understood. We built structural models of TARP-AMPA receptor complexes for TARPs γ2 and γ8, combining recent structural studies and de novo structure predictions. These models, combined with peptide binding assays, provide evidence for multiple interactions between GluA2 and variable extracellular loops of TARPs. Substitutions and deletions of these loops had surprisingly rich effects on the kinetics of glutamate-activated currents, without any effect on assembly. Critically, by altering the two interacting loops of γ2 and γ8, we could entirely remove all allosteric modulation of GluA2, without affecting formation of AMPA receptor-TARP complexes. Likewise, substitutions in the linker domains of GluA2 completely removed any effect of γ2 on receptor kinetics, indicating a dominant role for this previously overlooked site proximal to the AMPA receptor channel gate.

Indexed as

Allosteric RegulationAmino Acid SubstitutionAnimalsCalcium ChannelsDNA Mutational AnalysisMiceModels, BiologicalModels, MolecularProtein BindingReceptors, AMPASequence DeletionCacng2 protein, mouseCalcium Channelsglutamate receptor ionotropic, AMPA 2Receptors, AMPATARP gamma-8 protein, mousebiophysicsdesensitizationglutamatemodulationneurosciencenonereceptor kineticsstructural biologysuperactivation

Identifiers

PMID28871958
PMCPMC5599240

What OpenQuestion holds

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Registered trials

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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.