Evidence map›Paper›PMID 28100490›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Amino-terminal domains of kainate receptors determine the differential dependence on Neto auxiliary subunits for trafficking.

Nengyin Sheng, Yun Stone Shi, Roger A Nicoll

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

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  13. National science review · 2019
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  17. Subunit-specific role for the amino-terminal domain of AMPA receptors in synaptic targeting.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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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 2 countries.

Nengyin ShengDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143.
Yun Stone ShiDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143.
Roger A NicollDepartment of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143; roger.nicoll@ucsf.edu.
University of California, San Francisco · USModel Animal Research Center · CN

Funding

Synaptic Glutamate Receptor Trafficking.R01MH080379 · NIMH · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI NICOLL, ROGER A · 2007 to 2016
$5.3M
NIMH NIH HHS R01 MH080379
6 · The paper itself

Abstract

The kainate receptor (KAR), a subtype of glutamate receptor, mediates excitatory synaptic responses at a subset of glutamatergic synapses. However, the molecular mechanisms underlying the trafficking of its different subunits are poorly understood. Here we use the CA1 hippocampal pyramidal cell, which lacks KAR-mediated synaptic currents, as a null background to determine the minimal requirements for the extrasynaptic and synaptic expression of the GluK2 subunit. We find that the GluK2 receptor itself, in contrast to GluK1, traffics to the neuronal surface and synapse efficiently and the auxiliary subunits Neto1 and Neto2 caused no further enhancement of these two trafficking processes. However, the regulation of GluK2 biophysical properties by Neto proteins is the same as that of GluK1. We further determine that it is the amino-terminal domains (ATDs) of GluK1 and GluK2 that control the strikingly different trafficking properties between these two receptors. Moreover, the ATDs are critical for synaptic expression of heteromeric receptors at mossy fiber-CA3 synapses and also mediate the differential dependence on Neto proteins for surface and synaptic trafficking of GluK1 and GluK2. These results highlight the fundamental differences between the two major KAR subunits and their interplay with Neto auxiliary proteins.

Indexed as

Amino Acid SubstitutionAnimalsCA1 Region, HippocampalDimerizationGluK2 Kainate ReceptorKainic Acid ReceptorsLDL-Receptor Related ProteinsMembrane ProteinsMiceMiniature Postsynaptic PotentialsOrgan Culture TechniquesPatch-Clamp TechniquesProtein DomainsProtein Interaction MapsProtein TransportPyramidal CellsGluK2 Kainate ReceptorKainic Acid ReceptorsLDL-Receptor Related ProteinsMembrane ProteinsNeto1 protein, mouseNeto2 protein, ratReceptors, N-Methyl-D-AspartateRecombinant Proteinsamino-terminal domainkainate receptorNeto proteinssynaptic trafficking

Identifiers

PMID28100490
PMCPMC5293104
OpenAlexW2578118706

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.