Evidence map›Paper›PMID 30634573›Full record

ReviewInternational journal of molecular sciences2019

New Structures and Gating of Voltage-Dependent Potassium (Kv) Channels and Their Relatives: A Multi-Domain and Dynamic Question.

Francisco Barros, Luis A Pardo, Pedro Domínguez, Luisa Maria Sierra, Pilar de la Peña

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Modular architecture of KEMBO reports · 2025
    Review
  3. HInternational journal of molecular sciences · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Discovery of KMedicinal research reviews · 2021
    Review
  12. Dynamic NaeLife · 2021
    Article
  13. Influence of Kv11.1 (hERG1) KPflugers Archiv : European journal of physiology · 2021
    Article
  14. Review
  15. Exploring KFrontiers in molecular biosciences · 2021
    Article
  16. Review
  17. Atomistic Insights of Calmodulin Gating of Complete Ion Channels.International journal of molecular sciences · 2020
    Review
  18. Review
  19. Article
  20. The EAG Voltage-Dependent KFrontiers in pharmacology · 2020
    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.

Francisco BarrosDepartamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Edificio Santiago Gascón, Campus de El Cristo, 33006 Oviedo, Asturias, Spain. fbarros@uniovi.es.
Luis A PardoOncophysiology Group, Max Planck Institute of Experimental Medicine, Hermann-Rein-Strasse 3, 37075 Göttingen, Germany. pardo@em.mpg.de.ORCID 0000-0003-1375-4349
Pedro DomínguezDepartamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Edificio Santiago Gascón, Campus de El Cristo, 33006 Oviedo, Asturias, Spain. pdluengo@uniovi.es.
Luisa Maria SierraDepartamento de Biología Funcional (Area de Genética), Instituto Universitario de Oncología del Principado de Asturias (IUOPA), Universidad de Oviedo, 33006 Oviedo, Asturias, Spain. lmsierra@uniovi.es.ORCID 0000-0002-9046-1171
Pilar de la PeñaDepartamento de Bioquímica y Biología Molecular, Universidad de Oviedo, Edificio Santiago Gascón, Campus de El Cristo, 33006 Oviedo, Asturias, Spain. pdelapena@uniovi.es.ORCID 0000-0002-3915-730X

Funding

Ministerio de Economía y Competitividad BFU2015-66429-P and CTQ2016-80069-C2-1-R
6 · The paper itself

Abstract

Voltage-dependent potassium channels (Kv channels) are crucial regulators of cell excitability that participate in a range of physiological and pathophysiological processes. These channels are molecular machines that display a mechanism (known as gating) for opening and closing a gate located in a pore domain (PD). In Kv channels, this mechanism is triggered and controlled by changes in the magnitude of the transmembrane voltage sensed by a voltage-sensing domain (VSD). In this review, we consider several aspects of the VSD⁻PD coupling in Kv channels, and in some relatives, that share a common general structure characterized by a single square-shaped ion conduction pore in the center, surrounded by four VSDs located at the periphery. We compile some recent advances in the knowledge of their architecture, based in cryo-electron microscopy (cryo-EM) data for high-resolution determination of their structure, plus some new functional data obtained with channel variants in which the covalent continuity between the VSD and PD modules has been interrupted. These advances and new data bring about some reconsiderations about the use of exclusively a classical electromechanical lever model of VSD⁻PD coupling by some Kv channels, and open a view of the Kv-type channels as allosteric machines in which gating may be dynamically influenced by some long-range interactional/allosteric mechanisms.

Indexed as

Ion Channel GatingQuantitative Structure-Activity RelationshipAllosteric RegulationAnimalsCryoelectron MicroscopyHumansModels, MolecularPotassium Channels, Voltage-GatedProtein ConformationProtein DomainsPotassium Channels, Voltage-Gatedelectro-allosteric couplinggatingion channelsKv channelsmolecular architecturestructure

Identifiers

PMID30634573
PMCPMC6359393

What Socratic 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 Socratic graph.