AUNIP/C1orf135 directs DNA double-strand breaks towards the homologous recombination repair pathway

Jiangman Lou, Hongxia Chen, Jinhua Han, Hanqing He, Michael S. Y. Huen, Xin-hua Feng, Ting Liu and Jun Huang ()
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Jiangman Lou: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou
Hongxia Chen: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou
Jinhua Han: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou
Hanqing He: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou
Michael S. Y. Huen: School of Biomedical Sciences, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong Special Administrative Region
Xin-hua Feng: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou
Ting Liu: Department of Cell Biology, Zhejiang University School of Medicine, Hangzhou
Jun Huang: Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou

Nature Communications, 2017, vol. 8, issue 1, 1-14

Abstract: Abstract DNA double-strand breaks (DSBs) are mainly repaired by either homologous recombination (HR) or non-homologous end-joining (NHEJ). Here, we identify AUNIP/C1orf135, a largely uncharacterized protein, as a key determinant of DSB repair pathway choice. AUNIP physically interacts with CtIP and is required for efficient CtIP accumulation at DSBs. AUNIP possesses intrinsic DNA-binding ability with a strong preference for DNA substrates that mimic structures generated at stalled replication forks. This ability to bind DNA is necessary for the recruitment of AUNIP and its binding partner CtIP to DSBs, which in turn drives CtIP-dependent DNA-end resection and HR repair. Accordingly, loss of AUNIP or ablation of its ability to bind to DNA results in cell hypersensitivity toward a variety of DSB-inducing agents, particularly those that induce replication-associated DSBs. Our findings provide new insights into the molecular mechanism by which DSBs are recognized and channeled to the HR repair pathway.

Date: 2017
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DOI: 10.1038/s41467-017-01151-w

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