Evidence map›Paper›PMID 24726893›Full record

ArticleCellular signalling2014

The primary cilium influences interleukin-1β-induced NFκB signalling by regulating IKK activity.

A K T Wann, J P Chapple, M M Knight

Open access · hybridAbstract read
In one paragraph

Article in Cellular signalling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-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

33 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Ciliary IFT88 Protects Coordinated Adolescent Growth Plate Ossification From Disruptive Physiological Mechanical Forces.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Primary Cilia in the Skin: Functions in Immunity and Therapeutic Potential.Frontiers in cell and developmental biology · 2021
    Review
  15. Review
  16. Article
  17. Article
  18. TheScience signaling · 2020
    Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

A K T WannInstitute of Bioengineering and School of Engineering and Materials Science, Queen Mary University of London, Bancroft Road, Mile End, London E1 4NS, United Kingdom. Electronic address: a.wann@qmul.ac.uk.
J P ChappleCentre for Endocrinology, William Harvey Research Institute, Barts and the London School of Medicine and Dentistry, Queen Mary University of London, John Vane science building, Charterhouse square, London EC1M 6BQ, United Kingdom. Electronic address: j.p.chapple@qmul.ac.uk.
M M KnightInstitute of Bioengineering and School of Engineering and Materials Science, Queen Mary University of London, Bancroft Road, Mile End, London E1 4NS, United Kingdom. Electronic address: M.M.Knight@qmul.ac.uk.
Queen Mary University of London · GB

Funding

Versus Arthritis 19830
6 · The paper itself

Abstract

The primary cilium is an organelle acting as a master regulator of cellular signalling. We have previously shown that disruption of primary cilia assembly, through targeting intraflagellar transport, is associated with muted nitric oxide and prostaglandin responses to the inflammatory cytokine interleukin-1β (IL-1β). Here, we show that loss of the primary cilium disrupts specific molecular signalling events in cytosolic NFκB signalling. The induction of cyclooxygenase 2 (COX2) and inducible nitrous oxide synthase (iNOS) protein is abolished. Cells unable to assemble cilia exhibit unaffected activation of IκB kinase (IKK), but delayed and reduced degradation of IκB, due to diminished phosphorylation of inhibitor of kappa B (IκB) by IKK. This results in both delayed and reduced NFκB p65 nuclear translocation and nuclear transcript binding. We also demonstrate that heat shock protein 27 (hsp27), an established regulator of IKK, is localized to the ciliary axoneme and cellular levels are dramatically disrupted with loss of the primary cilium. These results suggest that the primary cilia compartment exerts influence over NFκB signalling. We propose that the cilium is a locality for regulation of the molecular events defining NFκB signalling events, tuning signalling as appropriate.

Indexed as

AnimalsCell LineChondrocytesCiliaCyclooxygenase 2HSP27 Heat-Shock ProteinsI-kappa B ProteinsInterleukin-1betaMiceNF-kappa BNitric Oxide Synthase Type IIPhosphorylationSignal TransductionCyclooxygenase 2HSP27 Heat-Shock ProteinsI-kappa B ProteinsInterleukin-1betaNF-kappa BNitric Oxide Synthase Type IINos2 protein, mousePtgs2 protein, mouseChondrocyteIKKInflammationInterleukin-1NFκB signallingPrimary cilium

Identifiers

PMID24726893
PMCPMC4064300
OpenAlexW2057881087

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.