title: The recognition and removal of cellular poly(ADP-ribose) signals.
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.
authors.affiliation: Cancer Research UK, Paterson Institute for Cancer Research, University of Manchester, Manchester, UK.
authors.forename: Eva
authors.initials: E
authors.lastname: Barkauskaite
authors.forename: Gytis
authors.initials: G
authors.lastname: Jankevicius
authors.forename: Andreas G
authors.initials: AG
authors.lastname: Ladurner
authors.forename: Ivan
authors.initials: I
authors.lastname: Ahel
authors.forename: Gyula
authors.initials: G
authors.lastname: Timinszky
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D020134:Catalytic Domain; D004249:DNA Damage / Q000502:physiology; D006026:Glycoside Hydrolases / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011064:Poly Adenosine Diphosphate Ribose / Q000737:chemistry / Q000378:metabolism*; D054730:Protein Interaction Domains and Motifs; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D011506:Proteins; C024857:poly(ADP)-ribosylated proteins; D011064:Poly Adenosine Diphosphate Ribose; D006026:Glycoside Hydrolases; C022407:poly ADP-ribose glycohydrolase
keywords: ADP-ribosylation; PAR-binding zinc finger domain; WWE domain; macrodomain; poly(ADP-ribose); poly(ADP-ribose) glycohydrolase; poly(ADP-ribose) polymerase