deADPribosylation

DeADPribosylation is a post-translational modification where one or more ADP-ribose moieties are covalently attached to a protein. This process is catalyzed by a family of enzymes called ADP-ribosyltransferases (ARTs). The addition of ADP-ribose can occur on various amino acid residues, including glutamate, aspartate, cysteine, serine, threonine, and arginine, depending on the specific ART enzyme. ADP-ribosylation can be a reversible process, with the removal of ADP-ribose moieties carried out by ADP-ribosylhydrolases (also known as deacetylases or PARG enzymes).

This modification plays a critical role in a wide array of cellular processes. These include DNA repair, transcription, signal transduction, protein stability, and immune responses. The addition of ADP-ribose can alter the protein's structure, function, and interactions with other molecules. For instance, it can affect protein localization, enzyme activity, or create binding sites for other proteins. The branching of ADP-ribose chains can also influence the functional outcome of the modification, with mono-ADP-ribosylation and poly-ADP-ribosylation having distinct biological effects. Dysregulation of ADP-ribosylation pathways has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.