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

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....

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Detalles Bibliográficos
Autores principales: Ling, Feng, Tang, Yi, Li, Ming, Li, Qing-Shu, Li, Xian, Yang, Lian, Zhao, Wei, Jin, Cong-Cong, Zeng, Zhen, Liu, Chang, Wu, Cheng-Fang, Chen, Wen-Wen, Lin, Xiao, Wang, Ya-Lan, Threadgill, Michael D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Impact Journals LLC 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5641168/
https://www.ncbi.nlm.nih.gov/pubmed/29069825
http://dx.doi.org/10.18632/oncotarget.20347
Descripción
Sumario: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.