Physiological relevance of the endogenous mono(ADP-ribosyl)ation of cellular proteins

FEBS J. 2005 Sep;272(18):4565-75. doi: 10.1111/j.1742-4658.2005.04876.x.


The mono(ADP-ribosyl)ation reaction is a post-translational modification that is catalysed by both bacterial toxins and eukaryotic enzymes, and that results in the transfer of ADP-ribose from betaNAD+ to various acceptor proteins. In mammals, both intracellular and extracellular reactions have been described; the latter are due to glycosylphosphatidylinositol-anchored or secreted enzymes that are able to modify their targets, which include the purinergic receptor P2X7, the defensins and the integrins. Intracellular mono(ADP-ribosyl)ation modifies proteins that have roles in cell signalling and metabolism, such as the chaperone GRP78/BiP, the beta-subunit of heterotrimeric G-proteins and glutamate dehydrogenase. The molecular identification of the intracellular enzymes, however, is still missing. A better molecular understanding of this reaction will help in the full definition of its role in cell physiology and pathology.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • ADP Ribose Transferases / chemistry
  • ADP Ribose Transferases / metabolism*
  • ADP Ribose Transferases / physiology
  • Animals
  • Endoplasmic Reticulum Chaperone BiP
  • Humans
  • Protein Processing, Post-Translational*
  • Proteins / metabolism*
  • Signal Transduction
  • Substrate Specificity


  • Endoplasmic Reticulum Chaperone BiP
  • HSPA5 protein, human
  • Proteins
  • ADP Ribose Transferases