Evidence map›Paper›PMID 19959478›Full record

ArticleThe Journal of biological chemistry2010

Potassium channel silencing by constitutive endocytosis and intracellular sequestration.

Sylvain Feliciangeli, Magalie P Tardy, Guillaume Sandoz, Franck C Chatelain, Richard Warth, Jacques Barhanin, Saïd Bendahhou, Florian Lesage

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

46 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure-Function Relationships of KAdvances in experimental medicine and biology · 2026
    Review
  4. ACPA-Induced ATP release and KCell communication and signaling : CCS · 2025
    Article
  5. Article
  6. Article
  7. Lysosomal Potassium Channels.Handbook of experimental pharmacology · 2023
    Review
  8. Article
  9. Structural Basis for pH-gating of the KNature communications · 2022
    Article
  10. Article
  11. Article
  12. Article
  13. The Pharmacology of Two-Pore Domain Potassium Channels.Handbook of experimental pharmacology · 2021
    Article
  14. Article
  15. Article
  16. Emerging Roles of TWIK-1 Heterodimerization in the Brain.International journal of molecular sciences · 2017
    Review
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 4 institutions in 2 countries.

Sylvain FeliciangeliInstitut de Pharmacologie Moléculaire et Cellulaire, CNRS, and Université de Nice Sophia-Antipolis, Sophia-Antipolis, 06560 Valbonne, France.
Magalie P Tardy
Guillaume Sandoz
Franck C Chatelain
Richard Warth
Jacques Barhanin
Saïd Bendahhou
Florian Lesage
Centre National de la Recherche Scientifique · FRInstitut de Pharmacologie Moléculaire et Cellulaire · FRUniversité Côte d'Azur · FRUniversity of Regensburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tandem of P domains in a weak inwardly rectifying K(+) channel 1 (TWIK1) is a K(+) channel that produces unusually low levels of current. Replacement of lysine 274 by a glutamic acid (K274E) is associated with stronger currents. This mutation would prevent conjugation of a small ubiquitin modifier peptide to Lys-274, a mechanism proposed to be responsible for channel silencing. However, we found no biochemical evidence of TWIK1 sumoylation, and we showed that the conservative change K274R did not increase current, suggesting that K274E modifies TWIK1 gating through a charge effect. Now we rule out an eventual effect of K274E on TWIK1 trafficking, and we provide convincing evidence that TWIK1 silencing results from its rapid retrieval from the cell surface. TWIK1 is internalized via a dynamin-dependent mechanism and addressed to the recycling endosomal compartment. Mutation of a diisoleucine repeat located in its cytoplasmic C terminus (I293A,I294A) stabilizes TWIK1 at the plasma membrane, resulting in robust currents. The effects of I293A,I294A on channel trafficking and of K274E on channel activity are cumulative, promoting even more currents. Activation of serotoninergic receptor 5-HT(1)R or adrenoreceptor alpha2A-AR stimulates TWIK1 but has no effect on TWIK1I293A,I294A, suggesting that G(i) protein activation is a physiological signal for increasing the number of active channels at the plasma membrane.

Indexed as

AnimalsCell LineCell MembraneDogsElectrophysiologyEndocytosisHumansImmunohistochemistryMicroscopy, ElectronMutationPhosphorylationPotassium Channels, Tandem Pore DomainProtein TransportReceptors, Serotonin, 5-HT1SerotoninKCNK1 protein, humanPotassium Channels, Tandem Pore DomainReceptors, Serotonin, 5-HT1Serotonin

Identifiers

PMID19959478
PMCPMC2836085
OpenAlexW2082355313

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.