Evidence map›Paper›PMID 18186042›Full record

ArticleJournal of cellular physiology2008

FGFR4 and its novel splice form in myogenic cells: Interplay of glycosylation and tyrosine phosphorylation.

Boguslaw A Kwiatkowski, Irina Kirillova, Robert E Richard, David Israeli, Zipora Yablonka-Reuveni

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  9. A contemporary atlas of the mouse diaphragm: myogenicity, vascularity, and the Pax3 connection.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2012
    Article
  10. Article
  11. FGFR4 blockade exerts distinct antitumorigenic effects in human embryonal versus alveolar rhabdomyosarcoma.Clinical cancer research : an official journal of the American Association for Cancer Research · 2012
    Article
  12. Review
  13. Article
  14. The skeletal muscle satellite cell: still young and fascinating at 50.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2011
    Article
  15. Article
  16. Article
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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

5 authors at 2 institutions in 2 countries.

Boguslaw A KwiatkowskiDepartment of Biological Structure, University of Washington School of Medicine, Seattle, Washington 98195, USA.
Irina Kirillova
Robert E Richard
David Israeli
Zipora Yablonka-Reuveni
University of Washington · USGenethon (France) · FR

Funding

Myogenic Stem Cell Function in Aging Skeletal MuscleR01AG021566 · NIA · UNIVERSITY OF WASHINGTON · PI YABLONKA-REUVENI, ZIPORA · 2002 to 2012
$3.6M
Satellite Cells and Skeletal Muscle Growth DynamicsR01AG013798 · NIA · UNIVERSITY OF WASHINGTON · PI YABLONKA-REUVENI, ZIPORA · 1995 to 2008
$1.8M
NIA NIH HHS AG013798NIA NIH HHS AG021566NIA NIH HHS R01 AG013798NIA NIH HHS R01 AG021566
6 · The paper itself

Abstract

The family of fibroblast growth factor receptors (FGFRs) is encoded by four distinct genes. FGFR1 and FGFR4 are both expressed during myogenesis, but whereas the function of FGFR1 in myoblast proliferation has been documented, the role of FGFR4 remains unknown. Here, we report on a new splice form of FGFR4 cloned from primary cultures of mouse satellite cells. This form, named FGFR4(-16), lacks the entire exon 16, resulting in a deletion within the FGFR kinase domain. Expression of FGFR4(-16) coincided with that of wild-type FGFR4 in all FGFR4-expressing tissues examined. Moreover, expression of both FGFR4 forms correlated with the onset of myogenic differentiation, as determined in mouse C2C12 cells and in the inducible myogenic system of 10T(1/2)-MyoD-ER cell line. Both endogenous and overexpressed forms of FGFR4 exhibited N-glycosylation. In contrast to FGFR1, induced homodimerization of FGFR4 proteins did not result in receptor tyrosine phosphorylation. Surprisingly, coexpression of FGFR4 forms and a chimeric FGFR1 protein resulted in FGFR4 tyrosine phosphorylation, raising the possibility that FGFR4 phosphorylation might be enabled by a heterologous tyrosine kinase activity. Collectively, the present study reveals novel characteristics of mouse FGFR4 gene products and delineates their expression pattern during myogenesis. Our findings suggest that FGFR4 functions in a distinctly different manner than the prototype FGFR during myogenic differentiation.

Indexed as

Alternative SplicingAnimalsBlotting, WesternCell DifferentiationCell LineCells, CulturedDNA, ComplementaryGlycosylationHumansMiceMice, Inbred C57BLMuscle CellsPhosphorylationPhosphotyrosineProtein IsoformsReceptor, Fibroblast Growth Factor, Type 1DNA, ComplementaryPhosphotyrosineProtein IsoformsReceptor, Fibroblast Growth Factor, Type 1Receptor, Fibroblast Growth Factor, Type 3Receptor, Fibroblast Growth Factor, Type 4

Identifiers

PMID18186042
PMCPMC3276070
OpenAlexW2065740736

What OpenQuestion holds

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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.