Evidence map›Paper›PMID 26205423›Full record

ArticleNature communications2015

Mechanism of potassium ion uptake by the Na(+)/K(+)-ATPase.

Juan P Castillo, Huan Rui, Daniel Basilio, Avisek Das, Benoît Roux, Ramon Latorre, Francisco Bezanilla, Miguel Holmgren

Abstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Multistate Kinetic Model of the Sodium-Potassium ATPase.The journal of physical chemistry. B · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Digoxin and its NaBioorganic & medicinal chemistry · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. The NaThe Journal of biological chemistry · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. NaMolecules (Basel, Switzerland) · 2021
    Review
  19. Binding of cardiotonic steroids to NaProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  20. A NaFrontiers in cell and developmental biology · 2021
    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

8 authors.

Juan P Castillo1] Laboratorio de Fisiología Celular, Facultad de Ciencias, Universidad de Chile, Montemar 254006, Chile [2] Centro Interdisciplinario de Neurociencia de Valparaíso, Universidad de Valparaíso, Valparaíso 2366103, Chile.
Huan RuiDepartment of Biochemistry and Molecular Biology, University of Chicago, Gordon Center for Integrative Sciences, Chicago, Illinois 60637, USA.
Daniel Basilio1] Laboratorio de Fisiología Celular, Facultad de Ciencias, Universidad de Chile, Montemar 254006, Chile [2] Facultad de Ciencias, Universidad de Chile, Santiago 7800003, Chile.
Avisek DasDepartment of Biochemistry and Molecular Biology, University of Chicago, Gordon Center for Integrative Sciences, Chicago, Illinois 60637, USA.
Benoît RouxDepartment of Biochemistry and Molecular Biology, University of Chicago, Gordon Center for Integrative Sciences, Chicago, Illinois 60637, USA.
Ramon Latorre1] Laboratorio de Fisiología Celular, Facultad de Ciencias, Universidad de Chile, Montemar 254006, Chile [2] Centro Interdisciplinario de Neurociencia de Valparaíso, Universidad de Valparaíso, Valparaíso 2366103, Chile.
Francisco Bezanilla1] Laboratorio de Fisiología Celular, Facultad de Ciencias, Universidad de Chile, Montemar 254006, Chile [2] Department of Biochemistry and Molecular Biology, University of Chicago, Gordon Center for Integrative Sciences, Chicago, Illinois 60637, USA.
Miguel Holmgren1] Laboratorio de Fisiología Celular, Facultad de Ciencias, Universidad de Chile, Montemar 254006, Chile [2] Molecular Neurophysiology Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA.

Funding

Synthetic Antigen Binder CoreU54GM087519 · NIGMS · UNIVERSITY OF CHICAGO · PI PEROZO, EDUARDO A · 2010 to 2017
$31.9M
Structure and Function of Membrane ProteinsZIANS002993 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI HOLMGREN, MIGUEL · 2009 to 2025
$24.0M
TrainingP41GM103712 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FAEDER, JAMES · 2012 to 2021
$16.3M
The Electrophysiological Studies of Voltage Gated ChannelsR01GM030376 · NIGMS · UNIVERSITY OF CHICAGO · PI BEZANILLA, FRANCISCO J · 1985 to 2025
$9.1M
Computational Studies of Ion Channels - Resubmission 01R01GM062342 · NIGMS · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI ROUX, BENOIT · 2001 to 2022
$8.7M
Structure and Function of Membrane ProteinsZ01NS002993 · NINDS · NEUROLOGICAL DISORDERS AND STROKE · PI HOLMGREN, MIGUEL · 2002 to 2008
$1.1M
Charge translocation by the sodium-potassium pump in the giant axon of the HumbolR03TW008351 · FIC · UNIVERSITY OF CHICAGO · PI BEZANILLA, FRANCISCO J · 2009 to 2011
$166k
FIC NIH HHS R03 TW008351Intramural NIH HHS Z01 NS002993NIGMS NIH HHS P41 GM103712NIGMS NIH HHS P41GM103712-S1NIGMS NIH HHS R01 GM030376NIGMS NIH HHS R01-GM030376NIGMS NIH HHS R01 GM062342NIGMS NIH HHS R01-GM062342NIGMS NIH HHS U54 GM087519NIGMS NIH HHS U54-GM087519
6 · The paper itself

Abstract

The Na(+)/K(+)-ATPase restores sodium (Na(+)) and potassium (K(+)) electrochemical gradients dissipated by action potentials and ion-coupled transport processes. As ions are transported, they become transiently trapped between intracellular and extracellular gates. Once the external gate opens, three Na(+) ions are released, followed by the binding and occlusion of two K(+) ions. While the mechanisms of Na(+) release have been well characterized by the study of transient Na(+) currents, smaller and faster transient currents mediated by external K(+) have been more difficult to study. Here we show that external K(+) ions travelling to their binding sites sense only a small fraction of the electric field as they rapidly and simultaneously become occluded. Consistent with these results, molecular dynamics simulations of a pump model show a wide water-filled access channel connecting the binding site to the external solution. These results suggest a mechanism of K(+) gating different from that of Na(+) occlusion.

Indexed as

AnimalsDecapodiformesMolecular Dynamics SimulationPatch-Clamp TechniquesPotassiumSodium-Potassium-Exchanging ATPasePotassiumSodium-Potassium-Exchanging ATPase

Identifiers

PMID26205423
PMCPMC4515779

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.