Evidence map›Paper›PMID 29540831›Full record

ArticleOncogene2018

FES-related tyrosine kinase activates the insulin-like growth factor-1 receptor at sites of cell adhesion.

Joanna Stanicka, Leonie Rieger, Sandra O'Shea, Orla Cox, Michael Coleman, Ciara O'Flanagan, Barbara Addario, Nuala McCabe, Richard Kennedy, Rosemary O'Connor

Open access · greenAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. IGF-1R targeting in cancer - does sub-cellular localization matter?Journal of experimental & clinical cancer research : CR · 2023
    Review
  7. Review
  8. Review
  9. Fer and FerT: A New Regulatory Link between Sperm and Cancer Cells.International journal of molecular sciences · 2023
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  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

10 authors at 1 institution in 1 country.

Joanna StanickaCell Biology Laboratory, School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland.
Leonie RiegerCell Biology Laboratory, School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland.
Sandra O'SheaCell Biology Laboratory, School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland.
Orla CoxCell Biology Laboratory, School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland.
Michael ColemanCell Biology Laboratory, School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland.
Ciara O'FlanaganCell Biology Laboratory, School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland.
Barbara AddarioCell Biology Laboratory, School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland.
Nuala McCabeCentre for Cancer Research and Cell Biology and Almac Diagnostics, Queens University Belfast, Belfast, Northern Ireland.
Richard KennedyCentre for Cancer Research and Cell Biology and Almac Diagnostics, Queens University Belfast, Belfast, Northern Ireland.
Rosemary O'ConnorCell Biology Laboratory, School of Biochemistry and Cell Biology, University College Cork, Cork, Ireland. r.oconnor@ucc.ie.
University College Cork · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

IGF-1 receptor (IGF-1R) and integrin cooperative signaling promotes cancer cell survival, proliferation, and motility, but whether this influences cancer progression and therapy responses is largely unknown. Here we investigated the non-receptor tyrosine adhesion kinase FES-related (FER), following its identification as a potential mediator of sensitivity to IGF-1R kinase inhibition in a functional siRNA screen. We found that FER and the IGF-1R co-locate in cells and can be co-immunoprecipitated. Ectopic FER expression strongly enhanced IGF-1R expression and phosphorylation on tyrosines 950 and 1131. FER phosphorylated these sites in an IGF-1R kinase-independent manner and also enhanced IGF-1-mediated phosphorylation of SHC, and activation of either AKT or MAPK-signaling pathways in different cells. The IGF-1R, β1 Integrin, FER, and its substrate cortactin were all observed to co-locate in cell adhesion complexes, the disruption of which reduced IGF-1R expression and activity. High FER expression correlates with phosphorylation of SHC in breast cancer cell lines and with a poor prognosis in patient cohorts. FER and SHC phosphorylation and IGF-1R expression could be suppressed with a known anaplastic lymphoma kinase inhibitor (AP26113) that shows high specificity for FER kinase. Overall, we conclude that FER enhances IGF-1R expression, phosphorylation, and signaling to promote cooperative growth and adhesion signaling that may facilitate cancer progression.

Indexed as

Cell AdhesionCell Line, TumorCell MembraneCell MovementEpithelial-Mesenchymal TransitionHumansIntegrin beta1MAP Kinase Signaling SystemMCF-7 CellsOrganophosphorus CompoundsPhosphorylationProtein-Tyrosine KinasesPyrimidinesReceptor, IGF Type 1Receptors, SomatomedinbrigatinibIGF1R protein, humanIntegrin beta1Organophosphorus CompoundsProtein-Tyrosine Kinasesproto-oncogene protein c-fes-fpsPyrimidinesReceptor, IGF Type 1Receptors, Somatomedin

Identifiers

PMID29540831
OpenAlexW2794225111

What Socratic 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 Socratic graph.