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

Chem Rev. 2018 Feb 14;118(3):1092-1136. doi: 10.1021/acs.chemrev.7b00122. Epub 2017 Nov 27.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ADP Ribose Transferases / chemistry
  • ADP Ribose Transferases / metabolism*
  • ADP-Ribosylation
  • Adenosine Diphosphate Ribose / metabolism*
  • Cell Death
  • DNA Damage
  • Humans
  • Hydrolases / chemistry
  • Hydrolases / metabolism
  • NAD / metabolism
  • Signal Transduction
  • Substrate Specificity


  • NAD
  • Adenosine Diphosphate Ribose
  • ADP Ribose Transferases
  • Hydrolases