Evidence map›Paper›PMID 21487019›Full record

ArticleThe Journal of biological chemistry2011

Fibroblast growth factor receptor 3 (FGFR3) is a strong heat shock protein 90 (Hsp90) client: implications for therapeutic manipulation.

Melanie B Laederich, Catherine R Degnin, Gregory P Lunstrum, Paul Holden, William A Horton

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. HSP90-CDC37 functions as a chaperone for the oncogenic FGFR3-TACC3 fusion.Molecular therapy : the journal of the American Society of Gene Therapy · 2022
    Article
  7. Article
  8. Review
  9. Review
  10. Achondroplasia: a comprehensive clinical review.Orphanet journal of rare diseases · 2019
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Fibroblast growth factor signaling in myofibroblasts differs from lipofibroblasts during alveolar septation in mice.American journal of physiology. Lung cellular and molecular physiology · 2015
    Article
  16. Review
  17. Review
  18. Article
  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

5 authors at 3 institutions in 1 country.

Melanie B LaederichResearch Center, Shriners Hospital for Children, Department of Cell & Developmental Biology, Oregon Health & Science University, Portland, Oregon 97239, USA.
Catherine R Degnin
Gregory P Lunstrum
Paul Holden
William A Horton
Shriners Hospitals for Children - Erie · USShriners Hospitals for Children - Portland · USOregon Health & Science University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibroblast growth factor receptor 3 (FGFR3) is a key regulator of growth and differentiation, whose aberrant activation causes a number of genetic diseases including achondroplasia and cancer. Hsp90 is a specialized molecular chaperone involved in stabilizing a select set of proteins termed clients. Here, we delineate the relationship of Hsp90 and co-chaperone Cdc37 with FGFR3 and the FGFR family. FGFR3 strongly associates with these chaperone complexes and depends on them for stability and function. Inhibition of Hsp90 function using the geldanamycin analog 17-AAG induces the ubiquitination and degradation of FGFR3 and reduces the signaling capacity of FGFR3. Other FGFRs weakly interact with these chaperones and are differentially influenced by Hsp90 inhibition. The Hsp90-related ubiquitin ligase CHIP is able to interact and destabilize FGFR3. Our results establish FGFR3 as a strong Hsp90 client and suggest that modulating Hsp90 chaperone complexes may beneficially influence the stability and function of FGFR3 in disease.

Indexed as

UbiquitinationAchondroplasiaAnimalsBenzoquinonesCell Cycle ProteinsChaperoninsChlorocebus aethiopsCOS CellsEnzyme StabilityHSP90 Heat-Shock ProteinsHumansLactams, MacrocyclicMiceMolecular ChaperonesReceptor, Fibroblast Growth Factor, Type 3BenzoquinonesCDC37 protein, humanCdc37 protein, mouseCell Cycle ProteinsChaperoninsFGFR3 protein, humanFgfr3 protein, mouseHSP90 Heat-Shock ProteinsLactams, MacrocyclicMolecular ChaperonesReceptor, Fibroblast Growth Factor, Type 3tanespimycin

Identifiers

PMID21487019
PMCPMC3103339
OpenAlexW1987343069

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.