Evidence map›Paper›PMID 19064667›Full record

ArticleThe Journal of cell biology2008

Protein kinase CK2 contributes to the organization of sodium channels in axonal membranes by regulating their interactions with ankyrin G.

Aline Bréchet, Marie-Pierre Fache, Anna Brachet, Géraldine Ferracci, Agnés Baude, Marie Irondelle, Sandrine Pereira, Christophe Leterrier, Bénédicte Dargent

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.

0numbers the graph read from it
0cells of the map it votes in
120citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

120 citing papers in PubMed, 171 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Coupling of functionality to trafficking of KCNQ2/3 potassium channels at the axon initial segment.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. An ankyrin G-binding motif mediates TRAAK periodic localization at axon initial segments of hippocampal pyramidal neurons.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Characterization of NaLife science alliance · 2024
    Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review

60 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Aline BréchetInstitut National de la Santé et de la Recherche Médicale, Unité Mixte de Recherche 641, Marseille F-13916, France.
Marie-Pierre Fache
Anna Brachet
Géraldine Ferracci
Agnés Baude
Marie Irondelle
Sandrine Pereira
Christophe Leterrier
Bénédicte Dargent
Institut de Neurobiologie de la Méditerranée · FRUnité de Neurobiologie des canaux Ioniques et de la Synapse · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In neurons, generation and propagation of action potentials requires the precise accumulation of sodium channels at the axonal initial segment (AIS) and in the nodes of Ranvier through ankyrin G scaffolding. We found that the ankyrin-binding motif of Na(v)1.2 that determines channel concentration at the AIS depends on a glutamate residue (E1111), but also on several serine residues (S1112, S1124, and S1126). We showed that phosphorylation of these residues by protein kinase CK2 (CK2) regulates Na(v) channel interaction with ankyrins. Furthermore, we observed that CK2 is highly enriched at the AIS and the nodes of Ranvier in vivo. An ion channel chimera containing the Na(v)1.2 ankyrin-binding motif perturbed endogenous sodium channel accumulation at the AIS, whereas phosphorylation-deficient chimeras did not. Finally, inhibition of CK2 activity reduced sodium channel accumulation at the AIS of neurons. In conclusion, CK2 contributes to sodium channel organization by regulating their interaction with ankyrin G.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsAnkyrinsAxonsCasein Kinase IICell MembraneCells, CulturedCluster AnalysisGlutamic AcidHippocampusIon Channel GatingMolecular Sequence DataPhosphorylationPoint MutationProtein BindingAnkyrinsCasein Kinase IIGlutamic AcidProtein Kinase InhibitorsSerineSodium Channels

Identifiers

PMID19064667
PMCPMC2600743
OpenAlexW2107738760

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.