H3 ubiquitination by NEDD4 regulates H3 acetylation and tumorigenesis

Xian Zhang, Binkui Li, Abdol Hossein Rezaeian, Xiaohong Xu, Ping-Chieh Chou, Guoxiang Jin, Fei Han, Bo-Syong Pan, Chi-Yun Wang, Jie Long, Anmei Zhang, Chih-Yang Huang, Fuu-Jen Tsai, Chang-Hai Tsai, Christopher Logothetis and Hui-Kuan Lin ()
Additional contact information
Xian Zhang: Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA
Binkui Li: The University of Texas MD Anderson Cancer Center
Abdol Hossein Rezaeian: The University of Texas MD Anderson Cancer Center
Xiaohong Xu: The University of Texas MD Anderson Cancer Center
Ping-Chieh Chou: Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA
Guoxiang Jin: Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA
Fei Han: Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA
Bo-Syong Pan: Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA
Chi-Yun Wang: Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA
Jie Long: Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA
Anmei Zhang: Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA
Chih-Yang Huang: Graduate Institute of Basic Medical Science, China Medical University
Fuu-Jen Tsai: College of Chinese Medicine, China Medical University
Chang-Hai Tsai: Asia University
Christopher Logothetis: University of Texas MD Anderson Cancer Center
Hui-Kuan Lin: Wake Forest School of Medicine, Medical Center Boulevard, Winston-Salem, North Carolina 27157, USA

Nature Communications, 2017, vol. 8, issue 1, 1-15

Abstract: Abstract Dynamic changes in histone modifications under various physiological cues play important roles in gene transcription and cancer. Identification of new histone marks critical for cancer development is of particular importance. Here we show that, in a glucose-dependent manner, E3 ubiquitin ligase NEDD4 ubiquitinates histone H3 on lysine 23/36/37 residues, which specifically recruits histone acetyltransferase GCN5 for subsequent H3 acetylation. Genome-wide analysis of chromatin immunoprecipitation followed by sequencing reveals that NEDD4 regulates glucose-induced H3 K9 acetylation at transcription starting site and enhancer regions. Integrative analysis of ChIP-seq and microarray data sets also reveals a consistent role of NEDD4 in transcription activation and H3 K9 acetylation in response to glucose. Functionally, we show that NEDD4-mediated H3 ubiquitination, by transcriptionally activating IL1α, IL1β and GCLM, is important for tumour sphere formation. Together, our study reveals the mechanism for glucose-induced transcriptome reprograming and epigenetic regulation in cancer by inducing NEDD4-dependent H3 ubiquitination.

Date: 2017
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DOI: 10.1038/ncomms14799

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