ATM induces MacroD2 nuclear export upon DNA damage.

ADP-ribosylation is a dynamic post-translation modification that regulates the early phase of various DNA repair pathways by recruiting repair factors to chromatin. ADP-ribosylation levels are defined by the activities of specific transferases and hydrolases. However, except for the transferase PARP1/ARDT1 little is known about regulation of these enzymes.

Poly-ADP-ribosylation signaling during DNA damage repair.

Poly-ADP-ribosylation is a post-translational modification generated in high amounts by poly-ADP-ribose polymerases (PARPs) in response to cellular stress, especially genotoxic stimuli. DNA damage-induced PARylation significantly changes local chromatin structure and triggers the accumulation of several DNA damage response (DDR) proteins at the DNA lesions. In this review, we will discuss the regulation of chromatin structure and DNA damage repair machineries by DNA damage-induced poly-ADP-ribosylation.

Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease.

Adenosine diphosphate (ADP)-ribosylation is a post-translational protein modification implicated in the regulation of a range of cellular processes. A family of proteins that catalyse ADP-ribosylation reactions are the poly(ADP-ribose) (PAR) polymerases (PARPs). PARPs covalently attach an ADP-ribose nucleotide to target proteins and some PARP family members can subsequently add additional ADP-ribose units to generate a PAR chain.

A family of macrodomain proteins reverses cellular mono-ADP-ribosylation.

ADP-ribosylation is a reversible post-translational modification with wide-ranging biological functions in all kingdoms of life. A variety of enzymes use NAD(+) to transfer either single or multiple ADP-ribose (ADPr) moieties onto distinct amino acid substrates, often in response to DNA damage or other stresses. Poly-ADPr-glycohydrolase readily reverses poly-ADP-ribosylation induced by the DNA-damage sensor PARP1 and other enzymes, but it does not remove the most proximal ADPr linked to the target amino acid.