Journal
FEBS JOURNAL
Volume 280, Issue 15, Pages 3491-3507Publisher
WILEY
DOI: 10.1111/febs.12358
Keywords
ADP-ribosylation; macrodomain; poly(ADP-ribose) glycohydrolase; poly(ADP-ribose) polymerase; PAR-binding zinc finger domain; poly(ADP-ribose); WWE domain
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Funding
- Ludwig Maximilian University of Munich
- Center for Integrated Protein Science Munich
- Deutsche Forschungsgemeinschaft [LA 2489/1-1]
- EU FP7 Marie Curie Initial Training Network 'Nucleosome4D'
- Deutsche Akademische Austauschdienst [55934632]
- Cancer Research UK
- European Research Council
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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.
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