Journal
NUCLEIC ACIDS RESEARCH
Volume 41, Issue 3, Pages 1698-1710Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gks1278
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Funding
- American Cancer Society [IRG-58-010-52]
- National Institute of Health (NIH) [GM098535, CA132755, CA130899, R01CA130899]
- Siteman Career Award in Breast Cancer Research
- Department of Defense
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Protein ubiquitination plays an important role in activating the DNA damage response and maintaining genomic stability. In response to DNA double-strand breaks (DSBs), a ubiquitination cascade occurs at DNA lesions. Here, we show that checkpoint with Forkhead-associated (FHA) and RING finger domain protein (CHFR), an E3 ubiquitin ligase, is recruited to DSBs by poly(ADP-ribose) (PAR). At DSBs, CHFR regulates the first wave of protein ubiquitination. Moreover, CHFR ubiquitinates PAR polymerase 1 (PARP1) and regulates chromatin-associated PARP1 in vivo. Thus, these results demonstrate that CHFR is an important E3 ligase in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation.
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