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

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Title
TRAIP/RNF206 is required for recruitment of RAP80 to sites of DNA damage
Author(s)
Lee, NS; Chung, HJ; Kim, HJ; Lee, SY; Ji, JH; Seo, Y; Han, SH; Choi, M; Yun, M; Lee, SG; Kyungjae Myung; Kim, Y; Kang, HC; Hongtae Kim
Publication Date
2016-01
Journal
NATURE COMMUNICATIONS, v.7, no., pp.10463 -
Publisher
NATURE PUBLISHING GROUP
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
URI
http://pr.ibs.re.kr/handle/8788114/2463
DOI
10.1038/ncomms10463
ISSN
2041-1723
Appears in Collections:
Center for Neuroscience Imaging Research (뇌과학 이미징 연구단) > Journal Papers (저널논문)
Center for Genomic Integrity(유전체 항상성 연구단) > Journal Papers (저널논문)
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