Evidence map›Paper›PMID 23754382›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Filter gate closure inhibits ion but not water transport through potassium channels.

Torben Hoomann, Nadin Jahnke, Andreas Horner, Sandro Keller, Peter Pohl

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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
3.0field-weighted citation impact, top 8% 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, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. YidC fromBiomolecules · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Multiple pore lining residues modulate water permeability of GlpF.Protein science : a publication of the Protein Society · 2022
    Article
  9. Article
  10. ScatteringNanoscale advances · 2021
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Ion permeation in potassium ion channels.Acta crystallographica. Section D, Structural biology · 2020
    Review
  18. Pore-modulating toxins exploit inherent slow inactivation to block KProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. 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

5 authors at 2 institutions in 2 countries.

Torben HoomannInstitute of Biophysics, Johannes Kepler University of Linz, 4020 Linz, Austria.
Nadin Jahnke
Andreas Horner
Sandro Keller
Peter Pohl
Johannes Kepler University of Linz · ATUniversity of Kaiserslautern · DE

Funding

Austrian Science Fund FWF P 19716
6 · The paper itself

Abstract

The selectivity filter of K(+) channels is conserved throughout all kingdoms of life. Carbonyl groups of highly conserved amino acids point toward the lumen to act as surrogates for the water molecules of K(+) hydration. Ion conductivity is abrogated if some of these carbonyl groups flip out of the lumen, which happens (i) in the process of C-type inactivation or (ii) during filter collapse in the absence of K(+). Here, we show that K(+) channels remain permeable to water, even after entering such an electrically silent conformation. We reconstituted fluorescently labeled and constitutively open mutants of the bacterial K(+) channel KcsA into lipid vesicles that were either C-type inactivating or noninactivating. Fluorescence correlation spectroscopy allowed us to count both the number of proteoliposomes and the number of protein-containing micelles after solubilization, providing the number of reconstituted channels per proteoliposome. Quantification of the per-channel increment in proteoliposome water permeability with the aid of stopped-flow experiments yielded a unitary water permeability pf of (6.9 ± 0.6) × 10(-13) cm(3)⋅s(-1) for both mutants. "Collapse" of the selectivity filter upon K(+) removal did not alter pf and was fully reversible, as demonstrated by current measurements through planar bilayers in a K(+)-containing medium to which K(+)-free proteoliposomes were fused. Water flow through KcsA is halved by 200 mM K(+) in the aqueous solution, which indicates an effective K(+) dissociation constant in that range for a singly occupied channel. This questions the widely accepted hypothesis that multiple K(+) ions in the selectivity filter act to mutually destabilize binding.

Indexed as

Bacterial ProteinsCell Membrane PermeabilityIon Channel GatingIon TransportModels, MolecularMutagenesis, Site-DirectedMutant ProteinsPotassium ChannelsProtein ConformationProteolipidsRecombinant ProteinsStreptomyces lividansWaterBacterial ProteinsMutant ProteinsPotassium Channelsprokaryotic potassium channelProteolipidsproteoliposomesRecombinant ProteinsWateraquaporinbrain water homeostasisknock-on mechanismmembrane channelsprotein reconstitution

Identifiers

PMID23754382
PMCPMC3696751
OpenAlexW2126468837

What OpenQuestion holds

Textmetadata
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.