Evidence map›Paper›PMID 19696444›Full record

ArticleThe Journal of biological chemistry2009

Novel mechanisms of fibroblast growth factor receptor 1 regulation by extracellular matrix protein anosmin-1.

Youli Hu, Scott E Guimond, Paul Travers, Steven Cadman, Erhard Hohenester, Jeremy E Turnbull, Soo-Hyun Kim, Pierre-Marc Bouloux

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 1 synthesis or guideline pooled it, 85 citations in OpenAlex.

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  8. Frontiers in endocrinology · 2023
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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

8 authors at 5 institutions in 1 country.

Youli HuCentre for Neuroendocrinology, University College London Medical School, Royal Free Campus, London NW32PF. y.hu@medsch.ucl.ac.uk
Scott E Guimond
Paul Travers
Steven Cadman
Erhard Hohenester
Jeremy E Turnbull
Soo-Hyun Kim
Pierre-Marc Bouloux
University College London · GBUniversity of Liverpool · GBImperial College London · GBMRC Centre for Regenerative Medicine · GBThe Royal Free Hospital · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F006616/1Biotechnology and Biological Sciences Research Council BB/F007167/1Wellcome Trust 083942
6 · The paper itself

Abstract

Activation of fibroblast growth factor (FGF) signaling is initiated by a multiprotein complex formation between FGF, FGF receptor (FGFR), and heparan sulfate proteoglycan on the cell membrane. Cross-talk with other factors could affect this complex assembly and modulate the biological response of cells to FGF. We have previously demonstrated that anosmin-1, a glycosylated extracellular matrix protein, interacts with the FGFR1 signaling complex and enhances its activity in an IIIc isoform-specific and HS-dependent manner. The molecular mechanism of anosmin-1 action on FGFR1 signaling, however, remains unknown. Here, we show that anosmin-1 directly binds to FGFR1 with high affinity. This interaction involves domains in the N terminus of anosmin-1 (cysteine-rich region, whey acidic protein-like domain and the first fibronectin type III domain) and the D2-D3 extracellular domains of FGFR1. In contrast, anosmin-1 binds to FGFR2IIIc with much lower affinity and displays negligible binding to FGFR3IIIc. We also show that FGFR1-bound anosmin-1, although capable of binding to FGF2 alone, cannot bind to a FGF2.heparin complex, thus preventing FGFR1.FGF2.heparin complex formation. By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex. Furthermore, a functional interaction between anosmin-1 and the FGFR1 signaling complex is demonstrated by immunofluorescence co-localization and Transwell migration assays where anosmin-1 was shown to induce opposing effects during chemotaxis of human neuronal cells. Our study provides molecular and cellular evidence for a modulatory action of anosmin-1 on FGFR1 signaling, whereby binding of anosmin-1 to FGFR1 and heparin can play a dual role in assembly and activity of the ternary FGFR1.FGF2.heparin complex.

Indexed as

AnimalsCell MembraneChemotaxisChlorocebus aethiopsCOS CellsExtracellular Matrix ProteinsFibroblast Growth Factor 2Heparan SulfateHumansMultiprotein ComplexesNerve Tissue ProteinsNeuronsProtein BindingProtein Structure, TertiaryReceptor, Fibroblast Growth Factor, Type 1Receptor, Fibroblast Growth Factor, Type 2ANOS1 protein, humanExtracellular Matrix ProteinsFGFR1 protein, humanFGFR3 protein, humanFibroblast Growth Factor 2Heparan SulfateMultiprotein ComplexesNerve Tissue ProteinsReceptor, Fibroblast Growth Factor, Type 1Receptor, Fibroblast Growth Factor, Type 2Receptor, Fibroblast Growth Factor, Type 3

Identifiers

PMID19696444
PMCPMC2785620
OpenAlexW2024319790

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.