Evidence map›Paper›PMID 25565632›Full record

ArticleOncotarget2014

The cylindromatosis gene product, CYLD, interacts with MIB2 to regulate notch signalling.

Neil Rajan, Richard J R Elliott, Alice Smith, Naomi Sinclair, Sally Swift, Christopher J Lord, Alan Ashworth

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Ubiquitination and Deubiquitination in Oral Disease.International journal of molecular sciences · 2021
    Review
  7. Genetic Testing in CYLD Cutaneous Syndrome: An Update.The application of clinical genetics · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. The role of deubiquitinases in breast cancer.Cancer metastasis reviews · 2016
    Review
  16. Article
  17. CYLD Promotes TNF-Mediators of inflammation · 2016
    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

7 authors at 3 institutions in 1 country.

Neil RajanThe CRUK Gene Function Laboratory and Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research, London, SW3 6JB, UK. Institute of Genetic Medicine, Newcastle University, Newcastle upon Tyne, NE1 3BZ, UK.
Richard J R ElliottThe CRUK Gene Function Laboratory and Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research, London, SW3 6JB, UK.
Alice SmithThe CRUK Gene Function Laboratory and Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research, London, SW3 6JB, UK.
Naomi SinclairInstitute of Genetic Medicine, Newcastle University, Newcastle upon Tyne, NE1 3BZ, UK.
Sally SwiftThe CRUK Gene Function Laboratory and Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research, London, SW3 6JB, UK.
Christopher J LordThe CRUK Gene Function Laboratory and Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research, London, SW3 6JB, UK.
Alan AshworthThe CRUK Gene Function Laboratory and Breakthrough Breast Cancer Research Centre, The Institute of Cancer Research, London, SW3 6JB, UK.
Breast Cancer Now · GBInstitute of Cancer Research · GBNewcastle University · GB

Funding

Cancer Research UK 14276Medical Research Council G0701367
6 · The paper itself

Abstract

CYLD, an ubiquitin hydrolase, has an expanding repertoire of regulatory roles in cell signalling and is dysregulated in a number of cancers. To dissect CYLD function we used a proteomics approach to identify CYLD interacting proteins and identified MIB2, an ubiquitin ligase enzyme involved in Notch signalling, as a protein which interacts with CYLD. Coexpression of CYLD and MIB2 resulted in stabilisation of MIB2 protein levels and was associated with reduced levels of JAG2, a ligand implicated in Notch signalling. Conversely, gene silencing of CYLD using siRNA, resulted in increased JAG2 expression and upregulation of Notch signalling. We investigated Notch pathway activity in skin tumours from patients with germline mutations in CYLD and found that JAG2 protein levels and Notch target genes were upregulated. In particular, RUNX1 was overexpressed in CYLD defective tumour cells. Finally, primary cell cultures of CYLD defective tumours demonstrated reduced viability when exposed to γ-secretase inhibitors that pharmacologically target Notch signalling. Taken together these data indicate an oncogenic dependency on Notch signalling and suggest potential novel therapeutic approaches for patients with CYLD defective tumours.

Indexed as

Deubiquitinating Enzyme CYLDHEK293 CellsHumansImmunohistochemistryImmunoprecipitationNeoplasmsOligonucleotide Array Sequence AnalysisReal-Time Polymerase Chain ReactionReceptors, NotchSignal TransductionSkin NeoplasmsTissue Array AnalysisTumor Suppressor ProteinsUbiquitin-Protein LigasesCYLD protein, humanDeubiquitinating Enzyme CYLDMIB2 protein, humanReceptors, NotchTumor Suppressor ProteinsUbiquitin-Protein Ligases

Identifiers

PMID25565632
PMCPMC4322962
OpenAlexW1955352820

What OpenQuestion 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 OpenQuestion graph.