| Literature DB >> 29172462 |
Bernhard Lüscher1, Mareike Bütepage1, Laura Eckei1, Sarah Krieg1, Patricia Verheugd1, Brian H Shilton1,2.
Abstract
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.Entities:
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Year: 2017 PMID: 29172462 DOI: 10.1021/acs.chemrev.7b00122
Source DB: PubMed Journal: Chem Rev ISSN: 0009-2665 Impact factor: 60.622