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논문 기본 정보

자료유형
학술저널
저자정보
Yu, Seung Eun (Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University) Park, Su Hyung (Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University) Jang, Yeun Kyu (Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University)
저널정보
한국통합생물학회 Animal cells and systems Animal cells and systems 제22권 제1호
발행연도
2018.1
수록면
22 - 28 (7page)

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The histone demethylase lysine-specific demethylase 4A (KDM4A/Jmjd2A) has diverse functions, including involvement in gene regulation and cell cycle, and plays an oncogenic role in cancer cells. The modulation of KDM4A through post-translational modifications remains unclear. Here, we show that small ubiquitin-like modifier (SUMO) 1-mediated modification of KDM4A was required for interaction with tumor suppressor p53. Our data revealed that KDM4A is mainly sumoylated at lysine residue 471. However, the SUMO modification resulted in little change in subcellular localization, demethylase activity, or protein stability of KMD4A. Intriguingly, co-immunoprecipitation data revealed that sumoylation-defective mutants of KDM4A had a lower binding ability with p53 compared to that of wild-type KDM4A, suggesting a positive role for sumoylation in the interaction between KDM4A and p53. Together, these data suggest that KDM4A is post-translationally modified by SUMO, and this sumoylation may be a novel regulatory switch for controlling the interplay between KDM4A and p53.

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