Crosstalk of ADP-ribosylation and ubiquitination
Despite the attachment of chemical groups in ADP-ribosylation and small proteins in ubiquitination, these posttranslational modifications have multiple analogies, as they target a range of residues and form polymers that can also become branched.
Proteins tagged with ADP-ribosylation or ubiquitination are read by an expanding repertoire of reading modules, some of which are incorporated into large macromolecular complexes.
Crosstalk in the post-translational modifications can occur via direct complex formation, genetic interactions, reading and hydrolysis of the other modification, and direct ADP-ribosylation of ubiquitin or vice versa.
The new discoveries of hybrid ADPribosyl–ubiquitin modifications, ubiquitination of ADP-ribosylation, and modification of nucleic acids add to the complexity and crosstalk between these post-translational modifications, with undiscovered biochemical potential.
https://www.cell.com/trends/biochemical-sciences/fulltext/S0968-0004(26)00036-8
https://sciencemission.com/ADP-ribosylation-and-ubiquitination
