Evidence map›Paper›PMID 26272615›Full record

ArticleThe Journal of biological chemistry2015

Unliganded fibroblast growth factor receptor 1 forms density-independent dimers.

Laëtitia Comps-Agrar, Diana Ronai Dunshee, Dan L Eaton, Junichiro Sonoda

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Phosphate-Sensing.Advances in experimental medicine and biology · 2022
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. FGF Family: From Drug Development to Clinical Application.International journal of molecular sciences · 2018
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

4 authors at 1 institution in 1 country.

Laëtitia Comps-AgrarFrom the Biochemical and Cellular Pharmacology, Protein Chemistry, and compsagrar.laetitia@gene.com.
Diana Ronai DunsheeMolecular Biology, Genentech, Inc., South San Francisco, California 94080.
Dan L EatonProtein Chemistry, and.
Junichiro SonodaMolecular Biology, Genentech, Inc., South San Francisco, California 94080 junichis@gene.com.
Gene Therapy Laboratory · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibroblast growth factors receptors (FGFRs) are thought to initiate intracellular signaling cascades upon ligand-induced dimerization of the extracellular domain. Although the existence of unliganded FGFR1 dimers on the surface of living cells has been proposed, this notion remains rather controversial. Here, we employed time-resolved Förster resonance energy transfer combined with SNAP- and ACP-tag labeling in COS7 cells to monitor dimerization of full-length FGFR1 at the cell-surface with or without the coreceptor βKlotho. Using this approach we observed homodimerization of unliganded FGFR1 that is independent of its surface density. The homo-interaction signal observed for FGFR1 was indeed as robust as that obtained for epidermal growth factor receptor (EGFR) and was further increased by the addition of activating ligands or pathogenic mutations. Mutational analysis indicated that the kinase and the transmembrane domains, rather than the extracellular domain, mediate the ligand-independent FGFR1 dimerization. In addition, we observed a formation of a higher order ligand-independent complex by the c-spliced isoform of FGFR1 and βKlotho. Collectively, our approach provides novel insights into the assembly and dynamics of the full-length FGFRs on the cell surface.

Indexed as

AnimalsCell MembraneChlorocebus aethiopsCOS CellsDNA Mutational AnalysisEnzyme-Linked Immunosorbent AssayErbB ReceptorsFibroblast Growth FactorsFlow CytometryFluorescence Resonance Energy TransferHumansKlotho ProteinsLigandsMembrane ProteinsMutationPhosphorylationErbB ReceptorsFGFR1 protein, humanfibroblast growth factor 21Fibroblast Growth FactorsKLB protein, humanKlotho ProteinsLigandsMembrane ProteinsReceptor, Fibroblast Growth Factor, Type 1dimerizationfgf21fibroblast growth factor (FGF)fibroblast growth factor receptor (FGFR)fluorescence resonance energy transfer (FRET)receptor structure-functionreceptor-tyrosine kinasetr-fret

Identifiers

PMID26272615
PMCPMC4591805
OpenAlexW2149796552

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.