期刊
CHEMICAL REVIEWS
卷 118, 期 3, 页码 216-260出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.chemrev.7b00122
关键词
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资金
- German Reseach Foundation DFG [LU466/16-1]
- IZKF Aachen of the Medical School, RWTH Aachen University [O2-1-2014]
- Excellence Initiative of the RWTH Aachen University [StUpPD_119_13]
- START program of the Faculty of Medicine, RWTH Aachen University [117/15]
- NSERC (Natural Sciences and Engineering Research Council) Canada
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.
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