Beyond protein modification: the rise of non-canonical ADP-ribosylation

Journal article

ADP-ribosylation has primarily been known as post-translational modification of proteins. As signalling strategy conserved in all domains of life, it modulates substrate activity, localisation, stability or interactions, thereby regulating a variety of cellular processes and microbial pathogenicity. Yet over the last years, there is increasing evidence of non-canonical forms of ADP-ribosylation that are catalysed by certain members of the ADP-ribosyltransferase family and go beyond traditional protein ADP-ribosylation signalling. New macromolecular targets such as nucleic acids and new ADP-ribose derivatives have been established, notably extending the repertoire of ADP-ribosylation signalling. Based on the physiological relevance known so far, non-canonical ADP-ribosylation deserves its recognition next to the traditional protein ADP-ribosylation modification and which we therefore review in the following.

Authors: Schuller, M; Ahel, I

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: Biochemical Society
• Journal: Biochemical Journal
• Volume: 479
• Issue: 4
• Pages: 463-477
• Place of publication: England
• Publication date: 2022-02-17
• Acceptance date: 2022-01-21
• DOI: 10.1042/bcj20210280
• EISSN: 1470-8728
• ISSN: 0264-6021
• Pmid: 35175282
• Language: English
• Keywords: thymidine; ubiquitin; structure-activity relationship; Poly(ADP-ribose) Polymerases; ADP-Ribosylation; regulatory sequences; FFR; adenosine diphosphate; ADP ribose transferases; ribonucleic acid; signal transduction; guanosine; n-glycosyl hydrolases