SnapShot: ADP-Ribosylation Signaling

Mol Cell. 2015 Jun 18;58(6):1134-1134.e1. doi: 10.1016/j.molcel.2015.06.001.

Abstract

Intracellular protein ADP-ribosylation is catalyzed by diphteria toxin-like ADP-ribosyltransferases (ARTDs, formerly PARPs) ("writers"), which use NAD(+) for the modification of different amino acids. While some ARTD members catalyze protein poly-ADP-ribosylation, most of them are mono-ADP-ribosyltransferases. ADP-ribosylation is recognized by protein domains ("readers") and reversed by different enzymes ("erasers"). ADP-ribosylation signaling regulates several key cellular processes during health and disease.

MeSH terms

  • ADP Ribose Transferases / metabolism
  • Adenosine Diphosphate Ribose / chemistry
  • Adenosine Diphosphate Ribose / metabolism*
  • Biosynthetic Pathways
  • Humans
  • Models, Chemical
  • Molecular Structure
  • NAD / metabolism
  • Niacinamide / metabolism
  • Poly (ADP-Ribose) Polymerase-1
  • Poly Adenosine Diphosphate Ribose / chemistry
  • Poly Adenosine Diphosphate Ribose / metabolism*
  • Poly(ADP-ribose) Polymerases / metabolism*
  • Signal Transduction*

Substances

  • NAD
  • Adenosine Diphosphate Ribose
  • Niacinamide
  • Poly Adenosine Diphosphate Ribose
  • ADP Ribose Transferases
  • PARP1 protein, human
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerases