Evidence map›Paper›PMID 27558965›Full record

ArticleNature communications2016

RNF168 and USP10 regulate topoisomerase IIα function via opposing effects on its ubiquitylation.

Kiran Kumar Naidu Guturi, Miyuki Bohgaki, Toshiyuki Bohgaki, Tharan Srikumar, Deborah Ng, Ramya Kumareswaran, Samah El Ghamrasni, Justin Jeon, Parasvi Patel, Mohamed Saad Eldin and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Deubiquitylating Enzymes in Cancer and Immunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  8. Article
  9. Article
  10. Article
  11. Emerging Roles of RNF168 in Tumor Progression.Molecules (Basel, Switzerland) · 2023
    Review
  12. Article
  13. Review
  14. Review
  15. Review
  16. SUMO: A Swiss Army Knife for Eukaryotic Topoisomerases.Frontiers in molecular biosciences · 2022
    Review
  17. Review
  18. Review
  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

16 authors at 3 institutions in 2 countries.

Kiran Kumar Naidu GuturiDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Miyuki BohgakiDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Toshiyuki BohgakiDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Tharan SrikumarDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.ORCID http://orcid.org/0000-0003-3359-0281
Deborah NgDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Ramya KumareswaranDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Samah El GhamrasniDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Justin JeonDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Parasvi PatelDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Mohamed Saad EldinDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Rob BristowDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Peter CheungDepartment of Biology, York University, Toronto, Ontario, Canada M3J 1P3.
Grant S StewartSchool of Cancer Sciences, University of Birmingham, Birmingham B15 2TT, UK.
Brian RaughtDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Anne HakemDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Razqallah HakemDepartment of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto, Toronto, Ontario, Canada M5G 1L7.
Ontario Institute for Cancer Research · CAUniversity of Birmingham · GBYork University · CA

Funding

Cancer Research UK 13030
6 · The paper itself

Abstract

Topoisomerase IIα (TOP2α) is essential for chromosomal condensation and segregation, as well as genomic integrity. Here we report that RNF168, an E3 ligase mutated in the human RIDDLE syndrome, interacts with TOP2α and mediates its ubiquitylation. RNF168 deficiency impairs decatenation activity of TOP2α and promotes mitotic abnormalities and defective chromosomal segregation. Our data also indicate that RNF168 deficiency, including in human breast cancer cell lines, confers resistance to the anti-cancer drug and TOP2 inhibitor etoposide. We also identify USP10 as a deubiquitylase that negatively regulates TOP2α ubiquitylation and restrains its chromatin association. These findings provide a mechanistic link between the RNF168/USP10 axis and TOP2α ubiquitylation and function, and suggest a role for RNF168 in the response to anti-cancer chemotherapeutics that target TOP2.

Indexed as

AnimalsAntineoplastic AgentsCell Line, TumorChromosome SegregationCraniofacial AbnormalitiesDNA, CatenatedDNA Topoisomerases, Type IIDrug Resistance, NeoplasmEtoposideFibroblastsGene Knockdown TechniquesHEK293 CellsHumansImmunologic Deficiency SyndromesLearning DisabilitiesMiceAntineoplastic AgentsDNA, CatenatedDNA Topoisomerases, Type IIEtoposidePoly-ADP-Ribose Binding ProteinsRNA, Small InterferingRNF168 protein, humanRNF168 protein, mouseTOP2A protein, humanTop2a protein, mouseTopoisomerase II InhibitorsUbiquitin-Protein LigasesUbiquitin ThiolesteraseUSP10 protein, humanUSP10 protein, mouse

Identifiers

PMID27558965
PMCPMC5007378
OpenAlexW2516402455

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.