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

Authors
Lee, NS | Chung, HJ | Kim, HJ | Lee, SY | Ji, JH  | Seo, YJ | Han, SH | Choi, MJ | Yun, MY | Lee, SG | Myung, KJ | Kim, YH | Kang, HC  | Kim, HT
Citation
Nature communications, 7. : 10463-10463, 2016
Journal Title
Nature communications
ISSN
2041-1723
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.
MeSH

DOI
10.1038/ncomms10463
PMID
26781088
Appears in Collections:
Journal Papers > Research Organization > Genomic Instability Research Center
Journal Papers > School of Medicine / Graduate School of Medicine > Physiology
Ajou Authors
강, 호철  |  지, 재훈
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