IMR Press / FBL / Volume 13 / Issue 17 / DOI: 10.2741/3184

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Article
Mammalian ADP-ribosyltransferases and ADP-ribosylhydrolases
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1 Institute of Immunology, University Medical Center Hamburg-Eppendorf, Martinistr. 52, D-20246 Hamburg, Germany
2 ESRF, 6 rue Jules Horowitz, F-38043 Grenoble Cedex 09, France
3 EMBL Hamburg Outstation, c/o DESY, Notkestr. 85, D-22603 Hamburg, Germany

*Author to whom correspondence should be addressed.

 

Front. Biosci. (Landmark Ed) 2008, 13(17), 6716–6729; https://doi.org/10.2741/3184
Published: 1 May 2008
Abstract

ADP-ribosyltransferases (ARTs) and ADP-ribosylhydrolases (ARHs) catalyze opposing reactions, which are termed ADP-ribosylation and de-ADP-ribosylation. ARTs transfer the ADP-ribose unit from NAD (nicotinamide adenine dinucleotide) onto an acceptor, while ARHs release the ADP-ribose from the target. Like protein phosphorylation, ADP-ribosylation is a posttranslational modification regulating protein function. In many cases, ADP-ribosylation inactivates the target protein. Numerous bacterial toxins intoxicate cells by attaching an ADP-ribose moiety to a functionally important amino acid residue, thereby blocking the interaction of the target protein with other proteins. In other cases, ADP-ribosylation activates protein function. On the surface of T cells, ART2.2 ADP-ribosylates the P2X7 purinoceptor on arginine 125, thereby gating the P2X7 ion channel by presenting a ligand to its nucleotide-binding site. ADP-ribosylation is not limited to protein targets and ARTs have been described that ADP-ribosylate DNA, RNA, and small molecules. Mammalian cells express distinct families of ARTs and ARHs. Recently, molecular cloning, site directed mutagenesis and three-dimensional structural analyses of prototype mammalian ARTs and ARHs have shed fresh insight into the structure and function of these intriguing enzymes.

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