Evidence map›Paper›PMID 17541788›Full record

ArticlePflugers Archiv : European journal of physiology2007

The selectivity, voltage-dependence and acid sensitivity of the tandem pore potassium channel TASK-1: contributions of the pore domains.

K H Yuill, P J Stansfeld, I Ashmole, M J Sutcliffe, P R Stanfield

Open access · hybridAbstract read
In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. KScience advances · 2020
    Article
  4. The Impact of HeterozygousJournal of the American Heart Association · 2017
    Article
  5. Much more than a leak: structure and function of K₂p-channels.Pflugers Archiv : European journal of physiology · 2015
    Review
  6. Review
  7. Article
  8. A novel channelopathy in pulmonary arterial hypertension.The New England journal of medicine · 2013
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Gating of two pore domain potassium channels.The Journal of physiology · 2010
    Review
  15. Gating the pore of potassium leak channels.European biophysics journal : EBJ · 2009
    Review
  16. Article
  17. Article
  18. Acid-sensitive ion channels and receptors.Handbook of experimental pharmacology · 2009
    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

5 authors at 3 institutions in 1 country.

K H YuillMolecular Physiology Group, Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK.
P J Stansfeld
I Ashmole
M J Sutcliffe
P R Stanfield
University of Warwick · GBUniversity of Leicester · GBUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council BB/C511305/1Biotechnology and Biological Sciences Research Council C15267Medical Research CouncilWellcome Trust 079863
6 · The paper itself

Abstract

We have investigated the contribution to ionic selectivity of residues in the selectivity filter and pore helices of the P1 and P2 domains in the acid sensitive potassium channel TASK-1. We used site directed mutagenesis and electrophysiological studies, assisted by structural models built through computational methods. We have measured selectivity in channels expressed in Xenopus oocytes, using voltage clamp to measure shifts in reversal potential and current amplitudes when Rb+ or Na+ replaced extracellular K+. Both P1 and P2 contribute to selectivity, and most mutations, including mutation of residues in the triplets GYG and GFG in P1 and P2, made channels non-selective. We interpret the effects of these--and of other mutations--in terms of the way the pore is likely to be stabilised structurally. We show also that residues in the outer pore mouth contribute to selectivity in TASK-1. Mutations resulting in loss of selectivity (e.g. I94S, G95A) were associated with slowing of the response of channels to depolarisation. More important physiologically, pH sensitivity is also lost or altered by such mutations. Mutations that retained selectivity (e.g. I94L, I94V) also retained their response to acidification. It is likely that responses both to voltage and pH changes involve gating at the selectivity filter.

Indexed as

AnimalsComputer SimulationElectrophysiologyFemaleHydrogen-Ion ConcentrationIon TransportMembrane PotentialsMiceMutationNerve Tissue ProteinsPatch-Clamp TechniquesPorinsPotassium Channels, Tandem Pore DomainProtein Structure, TertiaryRubidiumSodiumNerve Tissue ProteinsPorinsPotassium Channels, Tandem Pore Domainpotassium channel subfamily K member 3RubidiumSodium

Identifiers

PMID17541788
PMCPMC2492388
OpenAlexW2012586234

What OpenQuestion holds

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LicenceTDM
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.