TRAIP/RNF206 is required for recruitment of RAP80 to sites of DNA damage

Nam Soo Lee, Hee Jin Chung, Hyoung-June Kim, Seo Yun Lee, Jae-Hoon Ji, Yoojeong Seo, Seung Hun Han, Minji Choi, Miyong Yun, Seok-Geun Lee, Kyungjae Myung, Yonghwan Kim (), Ho Chul Kang () and Hongtae Kim ()
Additional contact information
Nam Soo Lee: Sungkyunkwan University
Hee Jin Chung: Sungkyunkwan University
Hyoung-June Kim: Sungkyunkwan University
Seo Yun Lee: Genomic Instability Research Center, Ajou University School of Medicine
Jae-Hoon Ji: Genomic Instability Research Center, Ajou University School of Medicine
Yoojeong Seo: Sookmyung Women's University
Seung Hun Han: Sungkyunkwan University
Minji Choi: College of Korean Medicine, Kyung Hee University
Miyong Yun: College of Korean Medicine, Kyung Hee University
Seok-Geun Lee: College of Korean Medicine, Kyung Hee University
Kyungjae Myung: Center for Genomic Integrity, Institute for Basic Science (IBS), Ulsan National Institute of Science and Technology
Yonghwan Kim: Sookmyung Women's University
Ho Chul Kang: Genomic Instability Research Center, Ajou University School of Medicine
Hongtae Kim: Sungkyunkwan University

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: Abstract RAP80 localizes to sites of DNA insults to enhance the DNA-damage responses. Here we identify TRAIP/RNF206 as a novel RAP80-interacting protein and find that TRAIP is necessary for translocation of RAP80 to DNA lesions. Depletion of TRAIP results in impaired accumulation of RAP80 and functional downstream partners, including BRCA1, at DNA lesions. Conversely, accumulation of TRAIP is normal in RAP80-depleted cells, implying that TRAIP acts upstream of RAP80 recruitment to DNA lesions. TRAIP localizes to sites of DNA damage and cells lacking TRAIP exhibit classical DNA-damage response-defect phenotypes. Biochemical analysis reveals that the N terminus of TRAIP is crucial for RAP80 interaction, while the C terminus of TRAIP is required for TRAIP localization to sites of DNA damage through a direct interaction with RNF20–RNF40. Taken together, our findings demonstrate that the novel RAP80-binding partner TRAIP regulates recruitment of the damage signalling machinery and promotes homologous recombination.

Date: 2016
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DOI: 10.1038/ncomms10463

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