Evidence map›Paper›PMID 26808983›Full record

ArticleeLife2016

Photo-switchable tweezers illuminate pore-opening motions of an ATP-gated P2X ion channel.

Chloé Habermacher, Adeline Martz, Nicolas Calimet, Damien Lemoine, Laurie Peverini, Alexandre Specht, Marco Cecchini, Thomas Grutter

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
6.7field-weighted citation impact, top 3% 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

23 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  6. Optical control of PIEZO1 channels.Nature communications · 2023
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  18. On the permeation of large organic cations through the pore of ATP-gated P2X receptors.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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  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

8 authors at 4 institutions in 1 country.

Chloé HabermacherUniversité de Strasbourg, Faculté de Pharmacie, Illkirch, France.
Adeline MartzUniversité de Strasbourg, Faculté de Pharmacie, Illkirch, France.
Nicolas CalimetISIS, Unité Mixte de Recherche 7006, Laboratoire d'Ingénierie des Fonctions Moléculaires, Strasbourg, France.
Damien LemoineUniversité de Strasbourg, Faculté de Pharmacie, Illkirch, France.
Laurie PeveriniUniversité de Strasbourg, Faculté de Pharmacie, Illkirch, France.
Alexandre SpechtUniversité de Strasbourg, Faculté de Pharmacie, Illkirch, France.
Marco CecchiniISIS, Unité Mixte de Recherche 7006, Laboratoire d'Ingénierie des Fonctions Moléculaires, Strasbourg, France.
Thomas GrutterUniversité de Strasbourg, Faculté de Pharmacie, Illkirch, France.
Laboratoire de Chémo-biologie synthétique et thérapeutique · FRCentre National de la Recherche Scientifique · FRInstitut de Science et d'Ingénierie Supramoléculaires · FRUniversité de Strasbourg · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

P2X receptors function by opening a transmembrane pore in response to extracellular ATP. Recent crystal structures solved in apo and ATP-bound states revealed molecular motions of the extracellular domain following agonist binding. However, the mechanism of pore opening still remains controversial. Here we use photo-switchable cross-linkers as 'molecular tweezers' to monitor a series of inter-residue distances in the transmembrane domain of the P2X2 receptor during activation. These experimentally based structural constraints combined with computational studies provide high-resolution models of the channel in the open and closed states. We show that the extent of the outer pore expansion is significantly reduced compared to the ATP-bound structure. Our data further reveal that the inner and outer ends of adjacent pore-lining helices come closer during opening, likely through a hinge-bending motion. These results provide new insight into the gating mechanism of P2X receptors and establish a versatile strategy applicable to other membrane proteins.

Indexed as

Adenosine TriphosphateAnimalsIon ChannelsModels, BiologicalMolecular Dynamics SimulationOptical TweezersProtein ConformationRatsReceptors, Purinergic P2X2Adenosine TriphosphateIon ChannelsReceptors, Purinergic P2X2azobenzene photoswitchbiophysicsgating mechanismneurosciencenoneP2X receptorsstructural biology

Identifiers

PMID26808983
PMCPMC4739762
OpenAlexW2263049754

What OpenQuestion holds

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LicenceCC BY
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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.