2. Academic Validation
  3. TRAIP/RNF206 is required for recruitment of RAP80 to sites of DNA damage

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

  • Nat Commun. 2016 Jan 19;7:10463. doi: 10.1038/ncomms10463.
Nam Soo Lee 1,  Hee Jin Chung 1,  Hyoung-June Kim 1,  Seo Yun Lee 2,  Jae-Hoon Ji 2,  Yoojeong Seo 3,  Seung Hun Han 1,  Minji Choi 4,  Miyong Yun 4,  Seok-Geun Lee 4,  Kyungjae Myung 5,  Yonghwan Kim 3,  Ho Chul Kang 2,  Hongtae Kim 1 6
Affiliations

Affiliations

  • 1 Department of Biological Sciences, Sungkyunkwan University, Suwon 440-746, Republic of Korea.
  • 2 Genomic Instability Research Center, Ajou University School of Medicine, Suwon 16499, Korea.
  • 3 Department of Biological Sciences, Sookmyung Women's University, Seoul 04310, Republic of Korea.
  • 4 Department of Science in Korean Medicine, College of Korean Medicine, Kyung Hee University, Seoul 02447, Korea.
  • 5 Center for Genomic Integrity, Institute for Basic Science (IBS), Ulsan National Institute of Science and Technology, Ulsan 44919, Korea.
  • 6 Center for Neuroscience Imaging Research, Institute for Basic Science, Sungkyunkwan University, Suwon 440-746, Korea.
PMID: 26781088 DOI: 10.1038/ncomms10463
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.

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