Evidence map›Paper›PMID 34009126›Full record

ArticleeLife2021

Voltage-clamp fluorometry analysis of structural rearrangements of ATP-gated channel P2X2 upon hyperpolarization.

Rizki Tsari Andriani, Yoshihiro Kubo

Abstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Extracellular salt bridge networks around S4 implicated in HCN channel gating and heart disease.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. 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

2 authors.

Rizki Tsari AndrianiDivision of Biophysics and Neurobiology, National Institute for Physiological Sciences, Aichi, Japan.ORCID 0000-0002-9242-469X
Yoshihiro KuboDivision of Biophysics and Neurobiology, National Institute for Physiological Sciences, Aichi, Japan.ORCID 0000-0001-6707-0837

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gating of the ATP-activated channel P2X2 has been shown to be dependent not only on [ATP] but also on membrane voltage, despite the absence of a canonical voltage-sensor domain. We aimed to investigate the structural rearrangements of rat P2X2 during ATP- and voltage-dependent gating, using a voltage-clamp fluorometry technique. We observed fast and linearly voltage-dependent fluorescence intensity (F) changes at Ala337 and Ile341 in the TM2 domain, which could be due to the electrochromic effect, reflecting the presence of a converged electric field. We also observed slow and voltage-dependent F changes at Ala337, which reflect structural rearrangements. Furthermore, we determined that the interaction between Ala337 in TM2 and Phe44 in TM1, which are in close proximity in the ATP-bound open state, is critical for activation. Taking these results together, we propose that the voltage dependence of the interaction within the converged electric field underlies the voltage-dependent gating.

Indexed as

Adenosine TriphosphateAnimalsFluorometryIon Channel GatingKineticsMembrane PotentialsMicroscopy, FluorescenceMutationProtein DomainsPurinergic P2X Receptor AgonistsRatsReceptors, Purinergic P2X2Structure-Activity RelationshipXenopus laevisAdenosine TriphosphateP2rx2 protein, ratPurinergic P2X Receptor AgonistsReceptors, Purinergic P2X2fluorescent unnatural amino acidmolecular biophysicsP2X2structural biologyvoltage-clamp fluorometryxenopus

Identifiers

PMID34009126
PMCPMC8184218

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.