The recognition and removal of cellular poly(ADP-ribose) signals

FEBS J. 2013 Aug;280(15):3491-507. doi: 10.1111/febs.12358. Epub 2013 Jun 18.

Abstract

Poly(ADP-ribosyl)ation is involved in the regulation of a variety of cellular pathways, including, but not limited to, transcription, chromatin, DNA damage and other stress signalling. Similar to other tightly regulated post-translational modifications, poly(ADP-ribosyl)ation employs 'writers', 'readers' and 'erasers' to confer regulatory functions. The generation of poly(ADP-ribose) is catalyzed by poly(ADP-ribose) polymerase enzymes, which use NAD(+) as a cofactor to sequentially transfer ADP-ribose units generating long polymers, which, in turn, can affect protein function or serve as a recruitment platform for additional factors. Historically, research has focused on poly(ADP-ribose) generation pathways, with knowledge about PAR recognition and degradation lagging behind. Over recent years, several discoveries have significantly furthered our understanding of poly(ADP-ribose) recognition and, even more so, of poly(ADP-ribose) degradation. In this review, we summarize current knowledge about the protein modules recognizing poly(ADP-ribose) and discuss the newest developments on the complete reversibility of poly(ADP-ribosyl)ation.

Keywords: ADP-ribosylation; PAR-binding zinc finger domain; WWE domain; macrodomain; poly(ADP-ribose); poly(ADP-ribose) glycohydrolase; poly(ADP-ribose) polymerase.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Catalytic Domain
  • DNA Damage / physiology
  • Glycoside Hydrolases / chemistry
  • Glycoside Hydrolases / metabolism
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Poly Adenosine Diphosphate Ribose / chemistry
  • Poly Adenosine Diphosphate Ribose / metabolism*
  • Protein Interaction Domains and Motifs
  • Protein Processing, Post-Translational*
  • Proteins / chemistry
  • Proteins / metabolism*
  • Signal Transduction*

Substances

  • Bacterial Proteins
  • Proteins
  • poly(ADP)-ribosylated proteins
  • Poly Adenosine Diphosphate Ribose
  • Glycoside Hydrolases
  • poly ADP-ribose glycohydrolase