Evidence map›Paper›PMID 28007894›Full record

ArticleThe EMBO journal2017

The pseudophosphatase STYX targets the F-box of FBXW7 and inhibits SCFFBXW7 function.

Veronika Reiterer, Cristina Figueras-Puig, Francois Le Guerroue, Stefano Confalonieri, Manuela Vecchi, Dasaradha Jalapothu, Sandip M Kanse, Raymond J Deshaies, Pier Paolo Di Fiore, Christian Behrends and 1 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Correlations of the expression of Cx43, SCFWorld journal of gastrointestinal oncology · 2025
    Article
  6. Molecular insights and clinical implications for the tumor suppressor role of SCFBiochimica et biophysica acta. Reviews on cancer · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Pseudophosphatases as Regulators of MAPK Signaling.International journal of molecular sciences · 2021
    Review
  11. The Roles of Pseudophosphatases in Disease.International journal of molecular sciences · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 6 institutions in 5 countries.

Veronika ReitererInstitute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Cristina Figueras-PuigBiotechnology Institute Thurgau, Kreuzlingen, Switzerland.
Francois Le GuerroueInstitute of Biochemistry II, Medical School Goethe University, Frankfurt, Germany.
Stefano ConfalonieriThe FIRC Institute for Molecular Oncology, IFOM, Milan, Italy.
Manuela VecchiDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, USA.
Dasaradha JalapothuInstitute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Sandip M KanseInstitute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Raymond J DeshaiesDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, USA.
Pier Paolo Di FioreThe FIRC Institute for Molecular Oncology, IFOM, Milan, Italy.
Christian BehrendsInstitute of Biochemistry II, Medical School Goethe University, Frankfurt, Germany christian.behrends@mail03.med.uni-muenchen.de hesso.farhan@medisin.uio.no.ORCID 0000-0002-9184-7607
Hesso FarhanInstitute of Basic Medical Sciences, University of Oslo, Oslo, Norway christian.behrends@mail03.med.uni-muenchen.de hesso.farhan@medisin.uio.no.ORCID 0000-0002-0889-8463
University of Oslo · NOCalifornia Institute of Technology · USGoethe University Frankfurt · DEBiotechnology Institute Thurgau · CHIFOM · ITUniversity of Milan · IT

Funding

Regulation of cullin - RING ubiquitin ligasesR01GM065997 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DESHAIES, RAYMOND J · 2002 to 2018
$4.5M
NIGMS NIH HHS R01 GM065997
6 · The paper itself

Abstract

The F-box protein FBXW7 is the substrate-recruiting subunit of an SCF ubiquitin ligase and a major tumor-suppressor protein that is altered in several human malignancies. Loss of function of FBXW7 results in the stabilization of numerous proteins that orchestrate cell proliferation and survival. Little is known about proteins that directly regulate the function of this protein. In the current work, we have mapped the interactome of the enigmatic pseudophosphatase STYX We reasoned that a catalytically inactive phosphatase might have adopted novel mechanisms of action. The STYX interactome contained several F-box proteins, including FBXW7. We show that STYX binds to the F-box domain of FBXW7 and disables its recruitment into the SCF complex. Therefore, STYX acts as a direct inhibitor of FBXW7, affecting the cellular levels of its substrates. Furthermore, we find that levels of STYX and FBXW7 are anti-correlated in breast cancer patients, which affects disease prognosis. We propose the STYX-FBXW7 interaction as a promising drug target for future investigations.

Indexed as

Breast NeoplasmsCell Cycle ProteinsF-Box ProteinsF-Box-WD Repeat-Containing Protein 7HumansIntracellular Signaling Peptides and ProteinsNuclear ProteinsSKP Cullin F-Box Protein LigasesUbiquitin-Protein LigasesCell Cycle ProteinsF-Box ProteinsF-Box-WD Repeat-Containing Protein 7FBXW7 protein, humanIntracellular Signaling Peptides and ProteinsNuclear ProteinsSKP Cullin F-Box Protein LigasesSTYX protein, humanUbiquitin-Protein Ligasesbreast cancerCullin–RING ubiquitin ligaseF‐box proteinmass spectrometrypseudophosphatase

Identifiers

PMID28007894
PMCPMC5286380
OpenAlexW2562563357

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.