Junying Qin

Abstract RAD18, an important ubiquitin E3 ligase, plays a dual role in translesion DNA synthesis (TLS) and homologous recombination (HR) repair. However, whether and how the regulatory mechanism of O-linked N-acetylglucosamine (O-GlcNAc) modification governing RAD18 and its function during these processes remains unknown. Here, we report that human RAD18, can undergo O-GlcNAcylation at Ser130/Ser164/Thr468, which is important for optimal RAD18 accumulation at DNA damage sites.

Yingying Wu‡,§,¶, Junying Qin‡, Fubing Li‡, Chuanyu Yang‡, Zhen Li‖, Zhongmei Zhou‡, Hailin Zhang‡, Yunxi Li‖, Xinye Wang‡, Rong Liu‡, Qian Tao**, Wenlin Chen‖1 and Ceshi Chen‡,‡‡,§§2 ‡Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences and Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, 650223, China §University of the Chinese Academy of Sciences, Beijing 101407, China ¶First Affiliated Hospital of Kunming...

Yingying Wu1, Junying Qin1, Fubing Li1, Chuanyu Yang1, Zhen Li2, Zhongmei Zhou3, Hailin Zhang4, Yunxi Li2, Xinye Wang1, Rong Liu5, Qian Tao6, Wenlin Chen7 and Ceshi Chen3* 1Kunming Institute of Zoology, China 2Department of Breast Surgery, the 3rd Affiliated Hospital of Kunming Medical University, China 3Kunming Institute of Zoology, CAS, China 4Kunming Institute of Zoology, Chinese Academy of Sciences 5Kunming Institute of Zoology, Chinese Academy of Sciences, China 6The Chinese University...