Evidence map›Paper›PMID 19635856›Full record

ArticleThe Journal of general physiology2009

Mutations reveal voltage gating of CNGA1 channels in saturating cGMP.

Juan Ramón Martínez-François, Yanping Xu, Zhe Lu

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2009. 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
1.5field-weighted citation impact, top 18% 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, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. CNG channel structure, function, and gating: a tale of conformational flexibility.Pflugers Archiv : European journal of physiology · 2021
    Review
  4. Article
  5. Article
  6. An Unorthodox Mechanism Underlying Voltage Sensitivity of TRPV1 Ion Channel.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Structural studies of ion permeation and Ca2+ blockage of a bacterial channel mimicking the cyclic nucleotide-gated channel pore.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  15. Article
  16. Article
  17. Gating in CNGA1 channels.Pflugers Archiv : European journal of physiology · 2010
    Review
  18. Article
  19. Article
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 1 institution in 1 country.

Juan Ramón Martínez-FrançoisDepartment of Physiology, Howard Hughes Medical Institute, University of Pennsylvania, Philadelphia, PA 19104, USA.
Yanping Xu
Zhe Lu
University of Pennsylvania · US

Funding

Permeation of Inward Rectifier K+ ChannelsR01GM055560 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI LU, ZHE · 1997 to 2024
$8.4M
Howard Hughes Medical InstituteNIGMS NIH HHS GM55560NIGMS NIH HHS R01 GM055560
6 · The paper itself

Abstract

Activity of cyclic nucleotide-gated (CNG) cation channels underlies signal transduction in vertebrate visual receptors. These highly specialized receptor channels open when they bind cyclic GMP (cGMP). Here, we find that certain mutations restricted to the region around the ion selectivity filter render the channels essentially fully voltage gated, in such a manner that the channels remain mostly closed at physiological voltages, even in the presence of saturating concentrations of cGMP. This voltage-dependent gating resembles the selectivity filter-based mechanism seen in KcsA K(+) channels, not the S4-based mechanism of voltage-gated K(+) channels. Mutations that render CNG channels gated by voltage loosen the attachment of the selectivity filter to its surrounding structure, thereby shifting the channel's gating equilibrium toward closed conformations. Significant pore opening in mutant channels occurs only when positive voltages drive the pore from a low-probability open conformation toward a second open conformation to increase the channels' open probability. Thus, the structure surrounding the selectivity filter has evolved to (nearly completely) suppress the expression of inherent voltage-dependent gating of CNGA1, ensuring that the binding of cGMP by itself suffices to open the channels at physiological voltages.

Indexed as

MutationAmino Acid SequenceAnimalsBinding SitesCyclic GMPCyclic Nucleotide-Gated Cation ChannelsElectrophysiologyIon Channel GatingModels, MolecularMolecular Sequence DataOocytesPatch-Clamp TechniquesPotassium Channels, Voltage-GatedXenopus laevisCyclic GMPCyclic Nucleotide-Gated Cation ChannelsPotassium Channels, Voltage-Gated

Identifiers

PMID19635856
PMCPMC2717697
OpenAlexW2125530007

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.