Evidence map›Paper›PMID 20159980›Full record

ArticleThe Journal of biological chemistry2010

Three homologous subunits form a high affinity peptide-gated ion channel in Hydra.

Stefan Dürrnagel, Anne Kuhn, Charisios D Tsiairis, Michael Williamson, Hubert Kalbacher, Cornelis J P Grimmelikhuijzen, Thomas W Holstein, Stefan Gründer

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. The Drosophila DEG/ENaC PPK12 is a NaScientific reports · 2025
    Article
  2. Neuropeptides: The Evergreen Jack-of-All-Trades in Neuronal Circuit Development and Regulation.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  3. A conserved peptide-binding pocket in HyNaC/ASIC ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Aromatic amino acids in the finger domain of the FMRFamide-gated NaPflugers Archiv : European journal of physiology · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Modulation of the FMRFamide-gated NaPflugers Archiv : European journal of physiology · 2017
    Article
  15. Article
  16. Review
  17. Back to the Basics: Cnidarians Start to Fire.Trends in neurosciences · 2017
    Review
  18. Animal-microbe interactions and the evolution of nervous systems.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2016
    Review
  19. Article
  20. ASICs and neuropeptides.Neuropharmacology · 2015
    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.

Stefan DürrnagelDepartment of Physiology, RWTH Aachen University, Aachen, Germany.
Anne Kuhn
Charisios D Tsiairis
Michael Williamson
Hubert Kalbacher
Cornelis J P Grimmelikhuijzen
Thomas W Holstein
Stefan Gründer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recently, three ion channel subunits of the degenerin (DEG)/epithelial Na(+) channel (ENaC) gene family have been cloned from the freshwater polyp Hydra magnipapillata, the Hydra Na(+) channels (HyNaCs) 2-4. Two of them, HyNaC2 and HyNaC3, co-assemble to form an ion channel that is gated by the neuropeptides Hydra-RFamides I and II. The HyNaC2/3 channel is so far the only cloned ionotropic receptor from cnidarians and, together with the related ionotropic receptor FMRFamide-activated Na(+) channel (FaNaC) from snails, the only known peptide-gated ionotropic receptor. The HyNaC2/3 channel has pore properties, like a low Na(+) selectivity and a low amiloride affinity, that are different from other channels of the DEG/ENaC gene family, suggesting that a component of the native Hydra channel might still be lacking. Here, we report the cloning of a new ion channel subunit from Hydra, HyNaC5. The new subunit is closely related to HyNaC2 and -3 and co-localizes with HyNaC2 and -3 to the base of the tentacles. Coexpression in Xenopus oocytes of HyNaC5 with HyNaC2 and -3 largely increases current amplitude after peptide stimulation and affinity of the channel to Hydra-RFamides I and II. Moreover, the HyNaC2/3/5 channel has altered pore properties and amiloride affinity, more similarly to other DEG/ENaC channels. Collectively, our results suggest that the three homologous subunits HyNaC2, -3, and -5 form a peptide-gated ion channel in Hydra that could contribute to fast synaptic transmission.

Indexed as

AmilorideAmino Acid SequenceAnimalsCloning, MolecularDegenerin Sodium ChannelsEpithelial Sodium ChannelsEvolution, MolecularFeeding BehaviorFemaleHydraIn Situ HybridizationIn Vitro TechniquesIon Channel GatingIon ChannelsMolecular Sequence DataNerve Tissue ProteinsAmilorideDegenerin Sodium ChannelsEpithelial Sodium ChannelsIon ChannelsNerve Tissue ProteinsProtein SubunitsRecombinant ProteinsSodium Channel Blockers

Identifiers

PMID20159980
PMCPMC2852933

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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.