Abstract
Protein ADP-ribosylation is an important posttranslational modification that plays versatile roles in multiple biological processes. ADP-ribosylation is catalyzed by a group of enzymes known as ADP-ribosyltransferases (ARTs). Using nicotinamide adenine dinucleotide (NAD+) as the donor, ARTs covalently link single or multiple ADP-ribose moieties from NAD+ to the substrates, forming mono ADP-ribosylation or poly ADP-ribosylation (PARylation). Novel functions of ARTs and ADPribosylation have been revealed over the past few years. Here we summarize the current knowledge on ARTs and PARylation.
Keywords: ADP-ribosylation, ADP-ribosyltransferase, ART, ARTD, PAR, PARylation.
Current Protein & Peptide Science
Title:ADP-Ribosyltransferases and Poly ADP-Ribosylation
Volume: 16 Issue: 6
Author(s): Chao Liu and Xiaochun Yu
Affiliation:
Keywords: ADP-ribosylation, ADP-ribosyltransferase, ART, ARTD, PAR, PARylation.
Abstract: Protein ADP-ribosylation is an important posttranslational modification that plays versatile roles in multiple biological processes. ADP-ribosylation is catalyzed by a group of enzymes known as ADP-ribosyltransferases (ARTs). Using nicotinamide adenine dinucleotide (NAD+) as the donor, ARTs covalently link single or multiple ADP-ribose moieties from NAD+ to the substrates, forming mono ADP-ribosylation or poly ADP-ribosylation (PARylation). Novel functions of ARTs and ADPribosylation have been revealed over the past few years. Here we summarize the current knowledge on ARTs and PARylation.
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Cite this article as:
Liu Chao and Yu Xiaochun, ADP-Ribosyltransferases and Poly ADP-Ribosylation, Current Protein & Peptide Science 2015; 16 (6) . https://dx.doi.org/10.2174/1389203716666150504122435
DOI https://dx.doi.org/10.2174/1389203716666150504122435 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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