ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease

作者：Bernhard Lüscher, Mareike Bütepage, Laura Eckei, Sarah Krieg, Patricia Verheugd, Brian H. Shilton · 发表于：Chemical Reviews · 年份：2017 · DOI：10.1021/acs.chemrev.7b00122 · 被引用次数：262 · 研究领域：PARP inhibition in cancer therapy、Calcium signaling and nucleotide metabolism、Toxin Mechanisms and Immunotoxins

Posttranslational modifications (PTMs) regulate protein functions and interactions. ADP-ribosylation is a PTM, in which ADP-ribosyltransferases use nicotinamide adenine dinucleotide (NAD + ) to modify target proteins with ADP-ribose. This modification can occur as mono- or poly-ADP-ribosylation. The latter involves the synthesis of long ADP-ribose chains that have specific properties due to the nature of the polymer. ADP-Ribosylation is reversed by hydrolases that cleave the glycosidic bonds either between ADP-ribose units or between the protein proximal ADP-ribose and a given amino acid side chain. Here we discuss the properties of the different enzymes associated with ADP-ribosylation and the consequences of this PTM on substrates. Furthermore, the different domains that interpret either mono- or poly-ADP-ribosylation and the implications for cellular processes are described.