Reprogramming cellular events by poly(ADP-ribose)-binding proteins

Jana Krietsch, Michèle Rouleau, Émilie Pic, Chantal Ethier, Ted M. Dawson, Valina L. Dawson, Jean Yves Masson, Guy G. Poirier, Jean Philippe Gagné

Research output: Contribution to journalReview articlepeer-review

Abstract

Poly(ADP-ribosyl)ation is a posttranslational modification catalyzed by the poly(ADP-ribose) polymerases (PARPs). These enzymes covalently modify glutamic, aspartic and lysine amino acid side chains of acceptor proteins by the sequential addition of ADP-ribose (ADPr) units. The poly(ADP-ribose) (pADPr) polymers formed alter the physico-chemical characteristics of the substrate with functional consequences on its biological activities. Recently, non-covalent binding to pADPr has emerged as a key mechanism to modulate and coordinate several intracellular pathways including the DNA damage response, protein stability and cell death. In this review, we describe the basis of non-covalent binding to pADPr that has led to the emerging concept of pADPr-responsive signaling pathways. This review emphasizes the structural elements and the modular strategies developed by pADPr-binding proteins to exert a fine-tuned control of a variety of pathways. Poly(ADP-ribosyl)ation reactions are highly regulated processes, both spatially and temporally, for which at least four specialized pADPr-binding modules accommodate different pADPr structures and reprogram protein functions. In this review, we highlight the role of well-characterized and newly discovered pADPr-binding modules in a diverse set of physiological functions.

Original languageEnglish (US)
Pages (from-to)1066-1087
Number of pages22
JournalMolecular Aspects of Medicine
Volume34
Issue number6
DOIs
StatePublished - Dec 2013

Keywords

  • Macro domain
  • PARG
  • PARP
  • PBZ
  • Poly(ADP-ribose)
  • WWE

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Clinical Biochemistry

Fingerprint

Dive into the research topics of 'Reprogramming cellular events by poly(ADP-ribose)-binding proteins'. Together they form a unique fingerprint.

Cite this