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

Biochem J. 2022 Feb 17;479(4):463-477. doi: 10.1042/BCJ20210280.

Abstract

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.

Keywords: ADP-ribosylation; PARP; nucleic acids; protein modification.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP Ribose Transferases / chemistry
  • ADP Ribose Transferases / classification
  • ADP Ribose Transferases / physiology
  • ADP-Ribosylation / physiology*
  • Adenosine Diphosphate / metabolism
  • Guanosine / metabolism
  • N-Glycosyl Hydrolases / physiology
  • Poly(ADP-ribose) Polymerases / metabolism
  • Regulatory Sequences, Ribonucleic Acid
  • Signal Transduction
  • Structure-Activity Relationship
  • Thymidine / metabolism
  • Ubiquitin / metabolism

Substances

  • Regulatory Sequences, Ribonucleic Acid
  • Ubiquitin
  • Guanosine
  • Adenosine Diphosphate
  • ADP Ribose Transferases
  • Poly(ADP-ribose) Polymerases
  • N-Glycosyl Hydrolases
  • ADP-ribosylarginine hydrolase
  • Thymidine