Oncotarget

Research Papers:

Mono-ADP-ribosylation of histone 3 at arginine-117 promotes proliferation through its interaction with P300

Feng Ling, Yi Tang, Ming Li, Qing-Shu Li, Xian Li, Lian Yang, Wei Zhao, Cong-Cong Jin, Zhen Zeng, Chang Liu, Cheng-Fang Wu, Wen-Wen Chen, Xiao Lin, Ya-Lan Wang _ and Michael D. Threadgill

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Oncotarget. 2017; 8:72773-72787. https://doi.org/10.18632/oncotarget.20347

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Abstract

Feng Ling1,*, Yi Tang1,*, Ming Li1, Qing-Shu Li1, Xian Li1, Lian Yang1, Wei Zhao1, Cong-Cong Jin1, Zhen Zeng1, Chang Liu1, Cheng-Fang Wu1, Wen-Wen Chen1, Xiao Lin1, Ya-Lan Wang1 and Michael D. Threadgill2

1Department of Pathology, Molecular Medicine and Cancer Research Center, Chongqing Medical University, Chongqing, China

2Department of Pharmacy and Pharmacology, University of Bath, Bath, UK

*Feng Ling and Yi Tang are co-first authorship

Correspondence to:

Ya-Lan Wang, email: [email protected]

Keywords: site of mono-ADP-ribosylation, histone modification, colon carcinoma, proliferation, P300

Received: March 03, 2017    Accepted: July 25, 2017    Published: August 18, 2017

ABSTRACT

Relatively little attention has been paid to ADP-ribosylated modifications of histones, especially to mono-ADP-ribosylation. As an increasing number of mono-ADP-ribosyltransferases have been identified in recent studies, the functions of mono-ADP-ribosylated proteins have aroused research interest. In particular, histones are substrates of some mono-ADP-ribosyltransferases and mono-ADP-ribosylated histone have been detected in physiological or pathological processes. In this research, arginine-117 (Arg-117; R-117) of hsitone3(H3) is identified as the a site of mono-ADP-ribosylation in colon carcinoma(the first such site to be identified); this posttranslational modification may promote the proliferation of colon carcinoma cells in vitro and in vivo. Using a point-mutant lentivirus transfection and using an activator of P300 allowed us to observe the mono-ADP-ribosylation at H3R117 and enhancement of the activity of P300 to up-regulate the level of acetylated β-catenin, which could increase the expression of c-myc and cyclin D1.


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