Nuclear ADP-Ribosylation and Its Role in Chromatin Plasticity, Cell Differentiation, and Epigenetics

Annu Rev Biochem. 2015;84:227-63. doi: 10.1146/annurev-biochem-060614-034506. Epub 2015 Feb 26.

Abstract

Protein ADP-ribosylation is an ancient posttranslational modification with high biochemical complexity. It alters the function of modified proteins or provides a scaffold for the recruitment of other proteins and thus regulates several cellular processes. ADP-ribosylation is governed by ADP-ribosyltransferases and a subclass of sirtuins (writers), is sensed by proteins that contain binding modules (readers) that recognize specific parts of the ADP-ribosyl posttranslational modification, and is removed by ADP-ribosylhydrolases (erasers). The large amount of experimental data generated and technical progress made in the last decade have significantly advanced our knowledge of the function of ADP-ribosylation at the molecular level. This review summarizes the current knowledge of nuclear ADP-ribosylation reactions and their role in chromatin plasticity, cell differentiation, and epigenetics and discusses current progress and future perspectives.

Keywords: ADP-ribosylation; ARTD; NAD; PAR; PARP; chromatin; histone.

Publication types

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

MeSH terms

  • ADP Ribose Transferases / metabolism
  • Adenosine Diphosphate Ribose / metabolism*
  • Animals
  • Cell Differentiation
  • Chromatin / metabolism*
  • Epigenesis, Genetic*
  • Humans
  • N-Glycosyl Hydrolases / metabolism
  • Protein Processing, Post-Translational*
  • Protein Structure, Tertiary
  • Proteins / chemistry
  • Proteins / metabolism

Substances

  • Chromatin
  • Proteins
  • Adenosine Diphosphate Ribose
  • ADP Ribose Transferases
  • N-Glycosyl Hydrolases
  • ADP-ribosylarginine hydrolase