Nature Communications (Aug 2016)
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,
- Rob Bristow,
- Peter Cheung,
- Grant S. Stewart,
- Brian Raught,
- Anne Hakem,
- Razqallah Hakem
Affiliations
- Kiran Kumar Naidu Guturi
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Miyuki Bohgaki
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Toshiyuki Bohgaki
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Tharan Srikumar
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Deborah Ng
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Ramya Kumareswaran
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Samah El Ghamrasni
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Justin Jeon
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Parasvi Patel
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Mohamed Saad Eldin
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Rob Bristow
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Peter Cheung
- Department of Biology, York University
- Grant S. Stewart
- School of Cancer Sciences, University of Birmingham
- Brian Raught
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Anne Hakem
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- Razqallah Hakem
- Department of Medical Biophysics, Princess Margaret Cancer Centre, Ontario Cancer Institute, University Health Network, University of Toronto
- DOI
- https://doi.org/10.1038/ncomms12638
- Journal volume & issue
-
Vol. 7,
no. 1
pp. 1 – 13
Abstract
The E3 ligase RNF168 is essential for the signalling of DNA double strand break and its mutations are associated with the RIDDLE syndrome. Here the authors identify TOP2a as substrate for RNF168 and USP10; providing a link between the RNF168/USP10 axis, TOP2a and the response to anti-cancer drugs that target TOP2.
