Evidence map›Paper›PMID 42560358›Full record

ArticleThe Journal of general physiology2026

Equivalent gain-of-function variants in KCNK3 and KCNK9 and their contribution to distinct TASK K2P channelopathies.

Kate M Crowther, Thibault R H Jouen-Tachoire, Peter Proks, Peter Rory Hall, Emma L Veale, Janina Sörmann, Karin E J Rödström, Thomas Müller, Saskia B Wortmann, Nina Barisic and 14 more

Abstract read
In one paragraph

Article in The Journal of general physiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

24 authors.

Kate M Crowther *Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.ORCID 0000-0002-6384-8637
Thibault R H Jouen-Tachoire *Clarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.ORCID 0000-0001-5867-994X
Peter ProksClarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.ORCID 0000-0001-6097-3646
Peter Rory HallClarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.ORCID 0000-0001-6832-0922
Emma L VealeMedway School of Pharmacy, Universities of Greenwich and Kent at Medway, Chatham Maritime, UK.ORCID 0000-0002-6778-9929
Janina SörmannClarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.ORCID 0000-0002-3288-6681
Karin E J RödströmClarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.ORCID 0000-0002-2952-0400
Thomas MüllerBayer AG, Research & Development, Pharmaceuticals , Wuppertal, Germany.ORCID 0000-0001-9017-4781
Saskia B WortmannUniversity Children's Hospital, Paracelsus Medical University , Salzburg, Austria.ORCID 0000-0002-1968-8103
Nina BarisicUniversity Hospital Centre Split, School of Medicine, University of Zagreb , Zagreb, Croatia.ORCID 0000-0002-8839-1522
Natalie HauserDepartment of Pediatrics, Inova Fairfax Hospital, Falls Church, VA, USA.ORCID 0000-0001-7663-1851
Vincenzo SalpietroDepartment of Neuromuscular Diseases, UCL Queen Square Institute of Neurology, London, UK.ORCID 0000-0003-0132-7921
RaeLynn ForsythDepartment of Pediatrics, UPMC Children's Hospital of Pittsburgh, Pittsburgh, PA, USA.ORCID 0000-0001-8264-6240
Linford WilliamsDepartment of Pediatrics, UPMC Children's Hospital of Pittsburgh, Pittsburgh, PA, USA.ORCID 0009-0002-2821-2307
Nora DerrabiDepartment of Anatomic Pathology, CHU Ibn Rochd Hospital, Casablanca, Morocco.ORCID 0009-0001-1618-329X
Carlos A BacinoDepartment of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA.ORCID 0000-0002-4342-5012
Jill A RosenfeldDepartment of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA.ORCID 0000-0001-5664-7987
Henry HouldenDepartment of Neuromuscular Diseases, UCL Queen Square Institute of Neurology, London, UK.ORCID 0000-0002-2866-7777
Simon NewsteadKavli Institute for Nanoscience Discovery, University of Oxford , Oxford, UK.ORCID 0000-0001-7432-2270
Caroline F WrightDepartment of Clinical and Biomedical Sciences, University of Exeter Medical School, Exeter, UK.ORCID 0000-0003-2958-5076
James FashamDepartment of Clinical and Biomedical Sciences, University of Exeter Medical School, Exeter, UK.ORCID 0000-0002-7614-9202
Alistair A MathieMedway School of Pharmacy, Universities of Greenwich and Kent at Medway, Chatham Maritime, UK.ORCID 0000-0001-6094-2890
Reza MaroofianDepartment of Neuromuscular Diseases, UCL Queen Square Institute of Neurology, London, UK.ORCID 0000-0001-6763-1542
Stephen J TuckerClarendon Laboratory, Department of Physics, University of Oxford, Oxford, UK.ORCID 0000-0001-8996-2000

Funding

Biotechnology and Biological Sciences Research Council BB/S008608/1Biotechnology and Biological Sciences Research Council BB/T002018/1Biotechnology and Biological Sciences Research Council BB/T008784/1Biotechnology and Biological Sciences Research Council MR/W017741/1Medical Research CouncilUniversity of OxfordWellcome TrustWellcome Trust 102161/B/13/ZWellcome Trust WT084655MA
6 · The paper itself

Abstract

Gain-of-function (GoF) missense variants in the two-pore domain (K2P) K+ channel TASK-1 (KCNK3) result in developmental delay with sleep apnea (DDSA), a neurodevelopmental channelopathy, while loss-of-function (LoF) variants cause pulmonary arterial hypertension. However, for the related TASK-3 channel (KCNK9), both LoF and GoF variants underlie a distinct neurodevelopmental disorder, KCNK9 imprinting syndrome (KIS). The relationship between genotype and phenotype in these disorders is further complicated because TASK-1 and TASK-3 can co-assemble into heteromeric channels with distinct functional properties. Here, we report additional patients with missense variants in KCNK3 and KCNK9 and investigate the effect of four novel genetic variants on the functional properties of homomeric and heteromeric TASK channels. Interestingly, two of these new pathogenic GoF variants (R131H and L122V) are found in both TASK-1 and TASK-3 and have equivalent functional effects on heteromeric TASK-1/TASK-3 channel activity, yet result in different clinical phenotypes. We have also determined a cryo-EM structure for the pathogenic L122V mutant TASK-3 channel, which suggests that subtle changes in gating and permeation within the inner cavity are responsible for its activatory effect. Overall, these results highlight the dominant role that homomeric TASK channels likely play in defining their associated channelopathies as well as the complexity of interpreting K+ channel dysfunction in pathophysiology.

Indexed as

ChannelopathiesGain of Function MutationNerve Tissue ProteinsPotassium Channels, Tandem Pore DomainFemaleHEK293 CellsHumansMaleMutation, MissenseKCNK9 protein, humanNerve Tissue ProteinsPotassium Channels, Tandem Pore Domainpotassium channel subfamily K member 3

Identifiers

PMID42560358
PMCPMC13446175

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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.