Ring finger protein 126 (RNF126) suppresses ionizing radiation-induced p53-binding protein 1 (53BP1) focus formation

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Title
Ring finger protein 126 (RNF126) suppresses ionizing radiation-induced p53-binding protein 1 (53BP1) focus formation
Author(s)
Nam Soo Lee; Hae Ryung Chang; Soomi Kim; Jae-Hoon Ji; Joorak Lee; Hyun Ji Lee; Yoojeong Seo; Misun Kang; Joo Seok Han; Kyungjae Myung; Yonghwan Kim; Hongtae Kim
Publication Date
2018-01
Journal
JOURNAL OF BIOLOGICAL CHEMISTRY, v.293, no.2, pp.588 - 598
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Abstract
Cells have evolved sophisticated mechanisms to maintain genomic integrity in response to DNA damage. Ionizing radiation (IR)–induced DNA damage results in the formation of IR-induced foci (iRIF) in the nucleus. The iRIF formation is part of the DNA damage response (DDR), which is an essential signaling cascade that must be strictly regulated because either the loss of or an augmented DDR leads to loss of genome integrity. Accordingly, negative regulation of the DDR is as critical as its activation. In this study, we have identified ring finger protein 126 (RNF126) as a negative regulator of the DDR from a screen of iRIF containing 53BP1. RNF126 over-expression abolishes not only the formation of 53BP1 iRIF, but also RNF168, FK2, RAP80, and BRCA1. However, the iRIF formation of H2AX, MDC1, and RNF8 is maintained, indicating that RNF126 acts between RNF8 and RNF168 during the DDR. In addition, RNF126 over-expression consistently resultes in the loss of RNF168-mediated H2A mono-ubiquitination at lysine (K)13/15 and the inhibition of the non-homologous end joining capability. Taken together, our findings reveal that RNF126 is a novel factor involved in the negative regulation of DDR, which is important for sustaining genomic integrity. (c) 2018 by The American Society for Biochemistry and Molecular Biology, Inc.
URI
https://pr.ibs.re.kr/handle/8788114/4300
ISSN
1083-351X
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > Journal Papers (저널논문)
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