Abstract

53BP1 is a key player in non-homologous end joining (NHEJ). Here the authors reveal an important role for the multifunctional homodimeric protein hub dynein light chain 1 (DYNLL1) in increasing the efficacy of 53BP1-mediated repair of DNA double-strand breaks (DSBs) by NHEJ.

Details

Title
The ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity
Author
Becker, Jordan R 1 ; Cuella-Martin, Raquel 1 ; Barazas, Marco 2 ; Liu, Rui 3 ; Oliveira, Catarina 1   VIAFID ORCID Logo  ; Oliver, Antony W 4   VIAFID ORCID Logo  ; Bilham, Kirstin 1 ; Holt, Abbey B 5 ; Blackford, Andrew N 6 ; Heierhorst, Jörg 7   VIAFID ORCID Logo  ; Jonkers, Jos 2 ; Rottenberg, Sven 8   VIAFID ORCID Logo  ; J Ross Chapman 1   VIAFID ORCID Logo 

 Genome Integrity Laboratory, Wellcome Centre for Human Genetics, University of Oxford, Oxford, UK 
 Division of Molecular Pathology, Oncode Institute, The Netherlands Cancer Institute, Amsterdam, The Netherlands 
 St. Vincent’s Institute of Medical Research, Fitzroy, VIC, Australia 
 Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, UK 
 MRC Brain Network Dynamics Unit, Department of Pharmacology, University of Oxford, Oxford, UK 
 Department of Oncology, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford, UK; CRUK/MRC Oxford Institute for Radiation Oncology, University of Oxford, Oxford, UK 
 St. Vincent’s Institute of Medical Research, Fitzroy, VIC, Australia; Department of Medicine at St. Vincent’s Hospital, Melbourne Medical School, The University of Melbourne, Fitzroy, VIC, Australia 
 Division of Molecular Pathology, Oncode Institute, The Netherlands Cancer Institute, Amsterdam, The Netherlands; Institute of Animal Pathology, Vetsuisse Faculty, University of Bern, Bern, Switzerland 
Pages
1-12
Publication year
2018
Publication date
Dec 2018
Publisher
Nature Publishing Group
e-ISSN
20411723
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
2157866181
Copyright
© 2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.