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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.

Original publication

DOI

10.1111/febs.12358

Type

Journal article

Journal

FEBS J

Publication Date

08/2013

Volume

280

Pages

3491 - 3507

Keywords

ADP-ribosylation, PAR-binding zinc finger domain, WWE domain, macrodomain, poly(ADP-ribose), poly(ADP-ribose) glycohydrolase, poly(ADP-ribose) polymerase, Amino Acid Sequence, Animals, Bacterial Proteins, Catalytic Domain, DNA Damage, Glycoside Hydrolases, Humans, Models, Molecular, Molecular Sequence Data, Poly Adenosine Diphosphate Ribose, Protein Interaction Domains and Motifs, Protein Processing, Post-Translational, Proteins, Signal Transduction