Evidence map›Paper›PMID 27277303›Full record

ArticleScientific reports2016

Functional and pharmacological characterization of two different ASIC1a/2a heteromers reveals their sensitivity to the spider toxin PcTx1.

Niko Joeres, Katrin Augustinowski, Andreas Neuhof, Marc Assmann, Stefan Gründer

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  7. Proline substitutions in the ASIC1 β11-12 linker slow desensitization.bioRxiv : the preprint server for biology · 2024
    Article
  8. Review
  9. Article
  10. Article
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  12. Intoxicating effects of alcohol depend on acid-sensing ion channels.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2023
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  13. Article
  14. Article
  15. Review
  16. 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

5 authors at 1 institution in 1 country.

Niko JoeresInstitute of Physiology, RWTH Aachen University, Pauwelsstrasse 30, D-52074 Aachen, Germany.
Katrin AugustinowskiInstitute of Physiology, RWTH Aachen University, Pauwelsstrasse 30, D-52074 Aachen, Germany.
Andreas NeuhofInstitute of Physiology, RWTH Aachen University, Pauwelsstrasse 30, D-52074 Aachen, Germany.
Marc AssmannInstitute of Physiology, RWTH Aachen University, Pauwelsstrasse 30, D-52074 Aachen, Germany.
Stefan GründerInstitute of Physiology, RWTH Aachen University, Pauwelsstrasse 30, D-52074 Aachen, Germany.
RWTH Aachen University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Acid Sensing Ion Channels (ASICs) detect extracellular proton signals and are involved in synaptic transmission and pain sensation. ASIC subunits assemble into homo- and heteromeric channels composed of three subunits. Single molecule imaging revealed that heteromers composed of ASIC1a and ASIC2a, which are widely expressed in the central nervous system, have a flexible 2:1/1:2 stoichiometry. It was hitherto not possible, however, to functionally differentiate these two heteromers. To have a homogenous population of ASIC1a/2a heteromers with either 2:1 or 1:2 stoichiometry, we covalently linked subunits in the desired configuration and characterized their functional properties in Xenopus oocytes. We show that the two heteromers have slightly different proton affinity, with an additional ASIC1a subunit increasing apparent affinity. Moreover, we found that zinc, which potentiates ASIC2a-containing ASICs but not homomeric ASIC1a, potentiates both heteromers. Finally, we show that PcTx1, which binds at subunit-subunit interfaces of homomeric ASIC1a, inhibits both heteromers suggesting that ASIC2a can also contribute to a PcTx1 binding site. Using this functional fingerprint, we show that rat cortical neurons predominantly express the ASIC1a/2a heteromer with a 2:1 stoichiometry. Collectively, our results reveal the contribution of individual subunits to the functional properties of ASIC1a/2a heteromers.

Indexed as

Protein MultimerizationAcid Sensing Ion Channel BlockersAcid Sensing Ion ChannelsAnimalsBinding SitesCerebral CortexNeuronsPeptidesProtein BindingProtein SubunitsRatsRats, WistarSpider VenomsXenopusAcid Sensing Ion Channel BlockersAcid Sensing Ion ChannelsAsic1 protein, ratAsic2 protein, ratPcTX1 protein, Psalmopoeus cambridgeiPeptidesProtein SubunitsSpider Venoms

Identifiers

PMID27277303
PMCPMC4899722
OpenAlexW2411281350

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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.