Evidence map›Paper›PMID 15800067›Full record

ArticleMolecular biology of the cell2005

Human ether-a-go-go-related gene 1 channels are physically linked to beta1 integrins and modulate adhesion-dependent signaling.

Alessia Cherubini, Giovanna Hofmann, Serena Pillozzi, Leonardo Guasti, Olivia Crociani, Emanuele Cilia, Paola Di Stefano, Simona Degani, Manuela Balzi, Massimo Olivotto and 5 more

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

74 citing papers in PubMed, 155 citations in OpenAlex.

  1. Ion channels and actin: A tale of two friends.Histology and histopathology · 2025
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  7. Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Review
  9. Review
  10. Article
  11. Antagonistic roles of Ras-MAPK and Akt signaling in integrin-KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022
    Article
  12. Review
  13. Targeting Ion Channels for Cancer Treatment: Current Progress and Future Challenges.Reviews of physiology, biochemistry and pharmacology · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

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

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

15 authors at 4 institutions in 2 countries.

Alessia CherubiniDepartment of Experimental Pathology and Oncology, University of Firenze, 50134 Firenze, Italy.
Giovanna Hofmann
Serena Pillozzi
Leonardo Guasti
Olivia Crociani
Emanuele Cilia
Paola Di Stefano
Simona Degani
Manuela Balzi
Massimo Olivotto
Enzo Wanke
Andrea Becchetti
Paola Defilippi
Randy Wymore
Annarosa Arcangeli
University of Florence · ITUniversity of Turin · ITUniversity of Milano-Bicocca · ITOklahoma State University Medical Center · US

Funding

Telethon GGP02208
6 · The paper itself

Abstract

Adhesive receptors of the integrin family are primarily involved in cell-extracellular matrix adhesion. Additionally, integrins trigger multiple signaling pathways that are involved in cell migration, proliferation, survival, and differentiation. We previously demonstrated that the activation of integrins containing the beta(1) subunit leads to a selective increase in potassium currents carried by the human ether-a-go-go-related gene (hERG) channels in neuroblastoma and leukemia cells; this current activation modulates adhesion-dependent differentiation in these cells. We hypothesized that the cross-talk between integrins and hERG channels could be traced back to the assembly of a macromolecular signaling complex comprising the two proteins. We tested this hypothesis in both SH-SY5Y neuroblastoma cells and in human embryonic kidney 293 cells stably transfected with hERG1 and, therefore, expressing only the full-length hERG1 protein on the plasma membrane. The beta(1) integrin and hERG1 coprecipitate in these cells and colocalize in both intracellular and surface membrane compartments. The two proteins also coprecipitate with caveolin-1, suggesting the localization of the complex in lipid rafts/caveolae. hERG1-transfected cells undergo an activation of hERG currents after beta(1) integrin-mediated adhesion to fibronectin; concomitant with this activation, the focal adhesion kinase associates with the hERG1 protein and becomes tyrosine phosphorylated. Using hERG1-specific inhibitors, we show that the tyrosine phosphorylation of focal adhesion kinase is strictly dependent on hERG channel activity. Similarly, the activity of the small GTPase Rac1 turned out to be dependent on hERG currents. On the whole, these data indicate that the hERG1 protein associates with beta(1) integrins and modulates adhesion receptor signaling.

Indexed as

Cell AdhesionSignal TransductionCell Culture TechniquesCell LineCell Line, TumorCell MembraneERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsFibronectinsFlow CytometryFluorescent Antibody TechniqueHumansIntegrin beta ChainsIntracellular MembranesKidneyModels, BiologicalERG1 Potassium ChannelEther-A-Go-Go Potassium ChannelsFibronectinsIntegrin beta ChainsKCNH2 protein, humanrac1 GTP-Binding Protein

Identifiers

PMID15800067
PMCPMC1142440
OpenAlexW2101654808

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.