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USP4 auto-deubiquitylation promotes homologous recombination

Abstract:

Repair of DNA double-strand breaks is crucial for maintaining genome integrity and is governed by post-translational modifications such as protein ubiquitylation. Here, we establish that the deubiquitylating enzyme USP4 promotes DNA-end resection and DNA repair by homologous recombination. We also report that USP4 interacts with CtIP and the MRE11-RAD50-NBS1 (MRN) complex and is required for CtIP recruitment to DNA damage sites. Furthermore, we show that USP4 is ubiquitylated on multiple site...

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Publication status:
Published
Peer review status:
Peer reviewed

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Target Discovery Institute
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Target Discovery Institute
Role:
Author
More from this funder
Name:
John Fell Fund
Grant:
133/075
More from this funder
Name:
European Research Council
Grant:
FP7/2007-2013) HEALTH-F2-2010-259893
Advanced Grant DDREAM
More from this funder
Name:
Wellcome Trust
Grant:
WT092096
097813/Z/11/Z
More from this funder
Name:
Cancer Research UK
Grant:
C6/A11224
C6/A14831
C6946/A14492
Publisher:
Cell Press
Journal:
Molecular Cell More from this journal
Volume:
60
Issue:
3
Pages:
362-373
Publication date:
2015-10-08
Acceptance date:
2015-09-18
DOI:
EISSN:
1097-4164
ISSN:
1097-4164
Language:
English
Keywords:
Pubs id:
pubs:570871
UUID:
uuid:6ac84b8d-ba40-4026-8627-146cd97a1b21
Local pid:
pubs:570871
Source identifiers:
570871
Deposit date:
2016-03-30

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