West China School of Medicine,Sichuan University,State Key Laboratory of Oral Diseases,National Clinical Research Center for Oral Diseases,West China Hospital of Stomatology,Sichuan University,Chengdu,China,State Key Laboratory of Oral Diseases,National Clinical Research Center for Oral Diseases,West China Hospital of Stomatology,Sichuan University,Chengdu,China,State Key Laboratory of Oral Diseases,National Clinical Research Center for Oral Diseases,West China Hospital of Stomatology,Sichuan University,Chengdu,China
This work was supported by a grant from The National Natural Science Foundation of China (81172579)
WRAP53 beta, a protein with a WD40 domain, plays an essential role in the maintenance of Cajal body stability, RNA splicing, and telomere elongation. WRAP53 β dysfunction is related to dyskeratosis congenita, tumor, progressive spinal muscular atrophy, premature aging and other diseases. Recent studies have found that WRAP53 β is an important scaffold protein essential for DNA double strand break repair (DSBs). It can be recruited to DNA damage sites in a H2AX, ATM and MDC1-dependent manner and phosphorylated by ATM. Then the phosphorylated WRAP53 β recruits ubiquitin E3 ligase RNF8 through its WD40 domain leading to histone H2AX ubiquitination, and further aggregation of downstream repair factors for DNA damage repair. In this review, we summarize the recent advances in the specific role and underlying mechanisms of WRAP53 β in the repair of DNA damages.
YAO Yu-Fei, CUI Bo-Miao, XIAO Li-Ying, LI Yan. Progress of WRAP53 β Regulating DNA Damage Repair[J]. Progress in Biochemistry and Biophysics,2018,45(6):613-620
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