Abstract:
:Unrestrained 53BP1 activity at DNA double-strand breaks (DSBs) hampers DNA end resection and upsets DSB repair pathway choice. RNF169 acts as a molecular rheostat to limit 53BP1 deposition at DSBs, but how this fine balance translates to DSB repair control remains undefined. In striking contrast to 53BP1, ChIP analyses of AsiSI-induced DSBs unveiled that RNF169 exhibits robust accumulation at DNA end-proximal regions and preferentially targets resected, RPA-bound DSBs. Accordingly, we found that RNF169 promotes CtIP-dependent DSB resection and favors homology-mediated DSB repair, and further showed that RNF169 dose-dependently stimulates single-strand annealing repair, in part, by alleviating the 53BP1-imposed barrier to DSB end resection. Our results highlight the interplay of RNF169 with 53BP1 in fine-tuning choice of DSB repair pathways.
journal_name
Proc Natl Acad Sci U S Aauthors
An L,Dong C,Li J,Chen J,Yuan J,Huang J,Chan KM,Yu CH,Huen MSYdoi
10.1073/pnas.1804823115subject
Has Abstractpub_date
2018-08-28 00:00:00pages
E8286-E8295issue
35eissn
0027-8424issn
1091-6490pii
1804823115journal_volume
115pub_type
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